ID AGAL_HUMAN Reviewed; 429 AA. AC P06280; Q6LER7; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 02-SEP-2026, entry version 253. DE RecName: Full=Alpha-galactosidase A {ECO:0000305}; DE EC=3.2.1.22 {ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852}; DE AltName: Full=Alpha-D-galactosidase A; DE AltName: Full=Alpha-D-galactoside galactohydrolase; DE AltName: Full=Galactosylgalactosylglucosylceramidase GLA {ECO:0000305}; DE AltName: Full=Melibiase; DE AltName: INN=Agalsidase; DE Flags: Precursor; GN Name=GLA {ECO:0000312|HGNC:HGNC:4296}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fibroblast; RX PubMed=3036505; DOI=10.1111/j.1432-1033.1987.tb11438.x; RA Tsuji S., Martin B.M., Kaslow D.C., Migeon B.R., Choudary P.V., RA Stubblefield B.K., Mayor J.A., Murray G.J., Barranger J.A., Ginns E.I.; RT "Signal sequence and DNA-mediated expression of human lysosomal alpha- RT galactosidase A."; RL Eur. J. Biochem. 165:275-280(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Lymphoblast; RX PubMed=2542896; DOI=10.1093/nar/17.8.3301; RA Kornreich R., Desnick R.J., Bishop D.F.; RT "Nucleotide sequence of the human alpha-galactosidase A gene."; RL Nucleic Acids Res. 17:3301-3302(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7626884; DOI=10.1007/bf00364796; RA Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W., RA Gibbs R.A.; RT "Sixty-nine kilobases of contiguous human genomic sequence containing the RT alpha-galactosidase A and Bruton's tyrosine kinase loci."; RL Mamm. Genome 6:334-338(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-429, AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Lung; RX PubMed=3014515; DOI=10.1073/pnas.83.13.4859; RA Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., RA Desnick R.J.; RT "Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding RT the mature enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4859-4863(1986). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64. RX PubMed=2892762; DOI=10.1016/0378-1119(87)90374-x; RA Quinn M., Hantzopoulos P., Fidanza V., Calhoun D.H.; RT "A genomic clone containing the promoter for the gene encoding the human RT lysosomal enzyme, alpha-galactosidase A."; RL Gene 58:177-188(1987). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64. RX PubMed=2836863; DOI=10.1073/pnas.85.11.3903; RA Bishop D.F., Kornreich R., Desnick R.J.; RT "Structural organization of the human alpha-galactosidase A gene: further RT evidence for the absence of a 3' untranslated region."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3903-3907(1988). RN [9] RP RNA EDITING OF POSITION 396. RX PubMed=7503918; DOI=10.1093/nar/23.14.2636; RA Novo F.J., Kruszewski A., McDermot K.D., Goldspink G., Gorecki D.C.; RT "Editing of human alpha-galactosidase RNA resulting in a pyrimidine to RT purine conversion."; RL Nucleic Acids Res. 23:2636-2640(1995). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=8804427; DOI=10.1016/0014-5793(96)00863-0; RA Kase R., Bierfreund U., Klein A., Kolter T., Itoh K., Suzuki M., RA Hashimoto Y., Sandhoff K., Sakuraba H.; RT "Only sphingolipid activator protein B (SAP-B or saposin B) stimulates the RT degradation of globotriaosylceramide by recombinant human lysosomal alpha- RT galactosidase in a detergent-free liposomal system."; RL FEBS Lett. 393:74-76(1996). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-215. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 32-422 IN COMPLEX WITH PRODUCT, RP HOMODIMERIZATION, AND GLYCOSYLATION AT ASN-139; ASN-192 AND ASN-215. RX PubMed=15003450; DOI=10.1016/j.jmb.2004.01.035; RA Garman S.C., Garboczi D.N.; RT "The molecular defect leading to Fabry disease: structure of human alpha- RT galactosidase."; RL J. Mol. Biol. 337:319-335(2004). RN [15] RP REVIEW ON FABRYD VARIANTS. RX PubMed=7911050; DOI=10.1002/humu.1380030204; RA Eng C.M., Desnick R.J.; RT "Molecular basis of Fabry disease: mutations and polymorphisms in the human RT alpha-galactosidase A gene."; RL Hum. Mutat. 3:103-111(1994). RN [16] RP INVOLVEMENT IN FABRYD, AND VARIANT FABRYD SER-40. RX PubMed=2152885; DOI=10.1016/0014-5793(90)80046-l; RA Koide T., Ishiura M., Iwai K., Inoue M., Kaneda Y., Okada Y., Uchida T.; RT "A case of Fabry's disease in a patient with no alpha-galactosidase A RT activity caused by a single amino acid substitution of Pro-40 by Ser."; RL FEBS Lett. 259:353-356(1990). RN [17] RP VARIANT FABRYD VAL-296. RX PubMed=1846223; DOI=10.1056/nejm199102073240607; RA von Scheidt W., Eng C.M., Fitzmaurice T.F., Erdmann E., Hubner G., RA Olsen E.G.J., Christomanou H., Kandolf R., Bishop D.F., Desnick R.J.; RT "An atypical variant of Fabry's disease with manifestations confined to the RT myocardium."; RL N. Engl. J. Med. 324:395-399(1991). RN [18] RP VARIANT FABRYD GLN-301. RX PubMed=2171331; RA Sakuraba H., Oshima A., Fukuhara Y., Shimmoto M., Nagao Y., Bishop D.F., RA Desnick R.J., Suzuki Y.; RT "Identification of point mutations in the alpha-galactosidase A gene in RT classical and atypical hemizygotes with Fabry disease."; RL Am. J. Hum. Genet. 47:784-789(1990). RN [19] RP VARIANT FABRYD TRP-356. RX PubMed=2539398; DOI=10.1172/jci114027; RA Bernstein H.S., Bishop D.F., Astrin K.H., Kornreich R., Eng C.M., RA Sakuraba H., Desnick R.J.; RT "Fabry disease: six gene rearrangements and an exonic point mutation in the RT alpha-galactosidase gene."; RL J. Clin. Invest. 83:1390-1399(1989). RN [20] RP VARIANTS FABRYD GLN-66; CYS-112; GLU-279; GLN-301 AND ARG-328. RX PubMed=1315715; DOI=10.1007/bf00207037; RA Ishii S., Sakuraba H., Suzuki Y.; RT "Point mutations in the upstream region of the alpha-galactosidase A gene RT exon 6 in an atypical variant of Fabry disease."; RL Hum. Genet. 89:29-32(1992). RN [21] RP VARIANTS FABRYD SER-34; GLY-56; ARG-162; GLN-227; VAL-264; VAL-266; RP PHE-297; TYR-313; ALA-328 AND ARG-404 DEL. RX PubMed=7504405; RA Eng C.M., Resnick-Silverman L.A., Niehaus D.J., Astrin K.H., Desnick R.J.; RT "Nature and frequency of mutations in the alpha-galactosidase A gene that RT cause Fabry disease."; RL Am. J. Hum. Genet. 53:1186-1197(1993). RN [22] RP VARIANTS FABRYD SER-34; SER-215; ALA-269; LYS-327 AND ARG-361. RX PubMed=8395937; DOI=10.1093/hmg/2.7.1051; RA Davies J.P., Winchester B.G., Malcolm S.; RT "Mutation analysis in patients with the typical form of Anderson-Fabry RT disease."; RL Hum. Mol. Genet. 2:1051-1053(1993). RN [23] RP VARIANTS FABRYD ARG-35; LEU-49; VAL-165 AND GLU-316. RX PubMed=8069316; DOI=10.1093/hmg/3.4.667; RA Davies J.P., Christomanou H., Winchester B.G., Malcolm S.; RT "Detection of 8 new mutations in the alpha-galactosidase A gene in Fabry RT disease."; RL Hum. Mol. Genet. 3:667-669(1994). RN [24] RP VARIANTS FABRYD SER-52; PHE-56; LYS-59; ARG-89; LYS-100; HIS-112; PRO-131; RP PRO-143; VAL-144; SER-146; TYR-172; ASN-219; ASN-244; LYS-272; ASP-288 AND RP GLN-342. RX PubMed=7531540; DOI=10.1093/hmg/3.10.1795; RA Eng C.M., Niehaus D.J., Enriquez A.L., Burgert T.S., Ludman M.D., RA Desnick R.J.; RT "Fabry disease: twenty-three mutations including sense and antisense CpG RT alterations and identification of a deletional hot-spot in the alpha- RT galactosidase A gene."; RL Hum. Mol. Genet. 3:1795-1799(1994). RN [25] RP VARIANTS FABRYD GLN-66; CYS-112; VAL-156; VAL-166; ALA-260; GLU-279; RP ILE-296; GLN-301; LYS-320; ARG-328 AND SER-373. RX PubMed=7575533; DOI=10.1006/bbrc.1995.2416; RA Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., RA Suzuki Y.; RT "Galactose stabilizes various missense mutants of alpha-galactosidase in RT Fabry disease."; RL Biochem. Biophys. Res. Commun. 214:1219-1224(1995). RN [26] RP VARIANTS FABRYD TYR-142; VAL-156 AND VAL-166. RX PubMed=7759078; DOI=10.1007/bf00223869; RA Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y.; RT "Alpha-galactosidase gene mutations in Fabry disease: heterogeneous RT expressions of mutant enzyme proteins."; RL Hum. Genet. 95:557-561(1995). RN [27] RP VARIANTS FABRYD PRO-32; SER-34; ASP-85; THR-156 AND GLN-301. RX PubMed=7599642; DOI=10.1002/humu.1380050316; RA Madsen K.M., Hasholt L., Soerensen S.A., Lagerstroem Fermer M., Dahl N.; RT "Two novel mutations (L32P) and (G85N) among five different missense RT mutations in six Danish families with Fabry's disease."; RL Hum. Mutat. 5:277-278(1995). RN [28] RP VARIANTS FABRYD PRO-20 AND ILE-296. RX PubMed=7596372; DOI=10.1056/nejm199508033330504; RA Nakao S., Takenaka T., Maeda M., Kodama C., Tanaka A., Tahara M., RA Yoshida A., Kuriyama M., Hayashibe H., Sakuraba H., Tanaka H.; RT "An atypical variant of Fabry's disease in men with left ventricular RT hypertrophy."; RL N. Engl. J. Med. 333:288-293(1995). RN [29] RP VARIANT FABRYD GLN-301. RX PubMed=8738659; RA Sawada K., Mizoguchi K., Hishida A., Kaneko E., Koide Y., Nishimura K., RA Kimura M.; RT "Point mutation in the alpha-galactosidase A gene of atypical Fabry disease RT with only nephropathy."; RL Clin. Nephrol. 45:289-294(1996). RN [30] RP VARIANTS FABRYD VAL-42; SER-49; TYR-56; HIS-92; GLY-93; THR-205; CYS-236; RP GLY-287; HIS-298 AND ARG-340. RX PubMed=8875188; DOI=10.1159/000472202; RA Davies J.P., Eng C.M., Hill J.A., Malcolm S., MacDermot K., RA Winchester B.G., Desnick R.J.; RT "Fabry disease: fourteen alpha-galactosidase A mutations in unrelated RT families from the United Kingdom and other European countries."; RL Eur. J. Hum. Genet. 4:219-224(1996). RN [31] RP VARIANT FABRYD PHE-383 DEL. RX PubMed=8834244; DOI=10.1007/bf02267068; RA Cariolou M.A., Christodoulides M., Manoli P., Kokkofitou A., Tsambaos D.; RT "Novel trinucleotide deletion in Fabry's disease."; RL Hum. Genet. 97:468-470(1996). RN [32] RP VARIANTS FABRYD ARG-52; CYS-162; ARG-265 AND 316-VAL--ASP-322 DEL. RX PubMed=8931708; DOI=10.1007/s004390050292; RA Germain D.P., Biasotto M., Tosi M., Meo T., Kahn A., Poenaru L.; RT "Fluorescence-assisted mismatch analysis (FAMA) for exhaustive screening of RT the alpha-galactosidase A gene and detection of carriers in Fabry RT disease."; RL Hum. Genet. 98:719-726(1996). RN [33] RP VARIANTS FABRYD ARG-52; GLU-128; THR-205; THR-284; LYS-298 AND GLU-358 DEL. RX PubMed=8807334; RX DOI=10.1002/(sici)1098-1004(1996)8:1<38::aid-humu5>3.0.co;2-l; RA Blanch L.C., Meaney C., Morris C.P.; RT "A sensitive mutation screening strategy for Fabry disease: detection of RT nine mutations in the alpha-galactosidase A gene."; RL Hum. Mutat. 8:38-43(1996). RN [34] RP VARIANT FABRYD ASN-231. RX PubMed=8863162; DOI=10.1136/jmg.33.8.682; RA Redonnet-Vernhet I., Ploos van Amstel J.K., Jansen R.P.M., Wevers R.A., RA Salvayre R., Levade T.; RT "Uneven X inactivation in a female monozygotic twin pair with Fabry disease RT and discordant expression of a novel mutation in the alpha-galactosidase A RT gene."; RL J. Med. Genet. 33:682-688(1996). RN [35] RP VARIANTS FABRYD PRO-20; SER-40; GLN-66; VAL-72; CYS-112; TYR-142; VAL-156; RP VAL-166; ASN-242; ALA-260; ASP-261; GLU-279; ILE-296; GLN-301; LYS-320; RP ARG-328; GLU-358 DEL AND SER-373. RX PubMed=9105656; DOI=10.1016/s0387-7604(96)00486-x; RA Takata T., Okumiya T., Hayashibe H., Shimmoto M., Kase R., Itoh K., RA Utsumi K., Kamei S., Sakuraba H.; RT "Screening and detection of gene mutations in Japanese patients with Fabry RT disease by non-radioactive single-stranded conformation polymorphism RT analysis."; RL Brain Dev. 19:111-116(1997). RN [36] RP VARIANTS FABRYD VAL-31; 45-LEU-HIS-46 DELINS ARG-SER; ARG-46; CYS-86; RP PRO-89; THR-91; TYR-92; TYR-94; VAL-97; THR-100; LEU-113; SER-134; ARG-138; RP THR-143; ARG-148; VAL-163; VAL-170; TYR-202; 205-PRO--TYR-207 DEL; ASP-216; RP SER-263; CYS-287; SER-298 AND ARG-404 DEL. RX PubMed=9100224; DOI=10.1007/bf03401671; RA Eng C.M., Ashley G.A., Burgert T.S., Enriquez A.L., D'Souza M., RA Desnick R.J.; RT "Fabry disease: thirty-five mutations in the alpha-galactosidase A gene in RT patients with classic and variant phenotypes."; RL Mol. Med. 3:174-182(1997). RN [37] RP VARIANT FABRYD THR-65. RX PubMed=9554750; RX DOI=10.1002/(sici)1098-1004(1998)11:4<328::aid-humu11>3.0.co;2-n; RA Chen C.-H., Shyu P.-W., Wu S.-J., Sheu S.-S., Desnick R.J., Hsiao K.-J.; RT "Identification of a novel point mutation (S65T) in alpha-galactosidase A RT gene in Chinese patients with Fabry disease."; RL Hum. Mutat. 11:328-330(1998). RN [38] RP VARIANT FABRYD LYS-358. RX PubMed=9452068; DOI=10.1002/humu.1380110147; RA Miyazaki T., Kajita M., Ohmori S., Mizutani N., Niwa T., Murata Y., Seo H.; RT "A novel mutation (E358K) in the alpha-galactosidase A gene detected in a RT Japanese family with Fabry disease."; RL Hum. Mutat. Suppl. 1:S139-S140(1998). RN [39] RP VARIANT FABRYD VAL-72. RX PubMed=9452090; DOI=10.1002/humu.1380110169; RA Okumiya T., Kawamura O., Itoh K., Kase R., Ishii S., Kamei S., Sakuraba H.; RT "Novel missense mutation (M72V) of alpha-galactosidase gene and its RT expression product in an atypical Fabry hemizygote."; RL Hum. Mutat. Suppl. 1:S213-S216(1998). RN [40] RP VARIANTS FABRYD SER-40; SER-215; ASP-224; TYR-313 AND TRP-THR-SER-247 INS. RX PubMed=9452111; DOI=10.1002/humu.1380110190; RA Guffon N., Froissart R., Chevalier-Porst F., Maire I.; RT "Mutation analysis in 11 French patients with Fabry disease."; RL Hum. Mutat. Suppl. 1:S288-S290(1998). RN [41] RP VARIANTS FABRYD TRP-202; GLY-223; ASP-224; GLN-301 AND LYS-327. RX PubMed=10208848; DOI=10.1006/bbrc.1999.0310; RA Germain D.P., Poenaru L.; RT "Fabry disease: identification of novel alpha-galactosidase A mutations and RT molecular carrier detection by use of fluorescent chemical cleavage of RT mismatches."; RL Biochem. Biophys. Res. Commun. 257:708-713(1999). RN [42] RP VARIANT FABRYD LYS-341. RX PubMed=10090526; DOI=10.1016/s0009-8981(98)00133-8; RA Beyer E.M., Karpova E.A., Udalova O.V., Ploos van Amstel J.K., RA van Diggelen O.P., Tsvetkova I.V.; RT "The multiple cases of Fabry disease in a Russian family caused by an E341K RT amino acid substitution in the alpha-galactosidase A."; RL Clin. Chim. Acta 280:81-89(1999). RN [43] RP CHARACTERIZATION OF VARIANTS FABRYD GLU-279 AND GLN-301, FUNCTION, RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=10838196; DOI=10.1016/s0925-4439(00)00024-7; RA Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoh K., RA Sandhoff K., Sakuraba H.; RT "Characterization of two alpha-galactosidase mutants (Q279E and R301Q) RT found in an atypical variant of Fabry disease."; RL Biochim. Biophys. Acta 1501:227-235(2000). RN [44] RP VARIANTS FABRYD VAL-42; CYS-112; ARG-142; ARG-148; VAL-165; ASP-183; RP SER-215; CYS-235; LEU-236; HIS-244; LEU-259; ILE-267; PHE-289; GLU-321; RP GLU-358 DEL AND TYR-378. RX PubMed=10666480; DOI=10.1007/bf03401993; RA Topaloglu A.K., Ashley G.A., Tong B., Shabbeer J., Astrin K.H., Eng C.M., RA Desnick R.J.; RT "Twenty novel mutations in the alpha-galactosidase A gene causing Fabry RT disease."; RL Mol. Med. 5:806-811(1999). RN [45] RP VARIANT FABRYD ASN-266. RX PubMed=11076046; DOI=10.1034/j.1399-0004.2000.580311.x; RA Lee J.-K., Kim G.-H., Kim J.-S., Kim K.-K., Lee M.-C., Yoo H.-W.; RT "Identification of four novel mutations in five unrelated Korean families RT with Fabry disease."; RL Clin. Genet. 58:228-233(2000). RN [46] RP VARIANTS FABRYD LEU-40; SER-95; CYS-112; HIS-112; ASN-148; ARG-172; RP VAL-187; SER-224; ARG-226; GLN-227; THR-230; HIS-266; GLN-301 AND TYR-320. RX PubMed=10916280; RA Ashton-Prolla P., Tong B., Shabbeer J., Astrin K.H., Eng C.M., RA Desnick R.J.; RT "Fabry disease: twenty-two novel mutations in the alpha-galactosidase A RT gene and genotype/phenotype correlations in severely and mildly affected RT hemizygotes and heterozygotes."; RL J. Invest. Med. 48:227-235(2000). RN [47] RP VARIANT FABRYD ASP-373. RX PubMed=11295840; DOI=10.1002/humu.41; RA Germain D.P., Salard D., Fellmann F., Azibi K., Caillaud C., Bernard M.-C., RA Poenaru L.; RT "Identification of a novel de novo mutation (G373D) in the alpha- RT galactosidase A gene (GLA) in a patient affected with Fabry disease."; RL Hum. Mutat. 17:353-353(2001). RN [48] RP VARIANTS FABRYD TYR-46; GLY-47; PRO-49; SER-94; SER-95; CYS-112; SER-113; RP THR-143; SER-215; ARG-258; ARG-259; ILE-267; HIS-279; HIS-280; HIS-298; RP TYR-313; HIS-363; ASP-377; ALA-409 AND THR-409. RX PubMed=11668641; DOI=10.1002/humu.1219; RA Blaydon D., Hill J.A., Winchester B.G.; RT "Fabry disease: 20 novel GLA mutations in 35 families."; RL Hum. Mutat. 18:459-459(2001). RN [49] RP VARIANT FABRYD PRO-143. RX PubMed=11889412; DOI=10.1097/00005792-200203000-00003; RA Branton M.H., Schiffmann R., Sabnis S.G., Murray G.J., Quirk J.M., RA Altarescu G., Goldfarb L., Brady R.O., Balow J.E., Austin H.A. III, RA Kopp J.B.; RT "Natural history of Fabry renal disease: influence of alpha-galactosidase A RT activity and genetic mutations on clinical course."; RL Medicine (Baltimore) 81:122-138(2002). RN [50] RP VARIANT FABRYD ALA-410. RX PubMed=12694230; DOI=10.1034/j.1399-0004.2003.00050.x; RA Yang C.-C., Lai L.-W., Whitehair O., Hwu W.-L., Chiang S.-C., Lien Y.-H.H.; RT "Two novel mutations in the alpha-galactosidase A gene in Chinese patients RT with Fabry disease."; RL Clin. Genet. 63:205-209(2003). RN [51] RP CHARACTERIZATION OF VARIANT FABRYD THR-65. RX PubMed=12786754; DOI=10.1034/j.1399-0004.2003.00077.x; RA Lai L.-W., Whitehair O., Wu M.-J., O'Meara M., Lien Y.-H.H.; RT "Analysis of splice-site mutations of the alpha-galactosidase A gene in RT Fabry disease."; RL Clin. Genet. 63:476-482(2003). RN [52] RP VARIANT FABRYD SER-272. RX PubMed=15162124; DOI=10.1038/sj.ejhg.5201184; RA Verovnik F., Benko D., Vujkovac B., Linthorst G.E.; RT "Remarkable variability in renal disease in a large Slovenian family with RT Fabry disease."; RL Eur. J. Hum. Genet. 12:678-681(2004). RN [53] RP VARIANTS FABRYD VAL-31; LEU-42; ARG-43; ASN-93; CYS-112; HIS-112; SER-112; RP SER-134; VAL-135; ASP-171; PHE-201; SER-215; GLU-234; ASP-261; TYR-264; RP VAL-264; GLY-276; PRO-285; PHE-300; ALA-328; VAL-328; LYS-338; ALA-358; RP GLU-358 DEL; ARG-404 DEL AND SER-414. RX PubMed=15712228; DOI=10.1002/humu.20144; RA Shabbeer J., Robinson M., Desnick R.J.; RT "Detection of alpha-galactosidase a mutations causing Fabry disease by RT denaturing high performance liquid chromatography."; RL Hum. Mutat. 25:299-305(2005). RN [54] RP VARIANT FABRYD THR-143. RX PubMed=16533976; DOI=10.1001/archneur.63.3.453; RA Nance C.S., Klein C.J., Banikazemi M., Dikman S.H., Phelps R.G., RA McArthur J.C., Rodriguez M., Desnick R.J.; RT "Later-onset Fabry disease: an adult variant presenting with the cramp- RT fasciculation syndrome."; RL Arch. Neurol. 63:453-457(2006). RN [55] RP VARIANTS FABRYD 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; RP THR-219; GLN-356 AND CYS-360, AND CHARACTERIZATION OF VARIANTS FABRYD RP 12-CYS--LEU-14 DEL; PRO-46; GLN-66; ASN-93; VAL-120; THR-219; GLN-356 AND RP CYS-360. RX PubMed=19621417; DOI=10.1002/humu.21074; RA Hwu W.L., Chien Y.H., Lee N.C., Chiang S.C., Dobrovolny R., Huang A.C., RA Yeh H.Y., Chao M.C., Lin S.J., Kitagawa T., Desnick R.J., Hsu L.W.; RT "Newborn screening for Fabry disease in Taiwan reveals a high incidence of RT the later-onset GLA mutation c.936+919G>A (IVS4+919G>A)."; RL Hum. Mutat. 30:1397-1405(2009). RN [56] RP CHARACTERIZATION OF VARIANTS FABRYD ASP-20; PRO-20; PRO-21; GLY-33; GLU-35; RP TRP-36; SER-40; THR-42; PRO-45; ASP-48; TYR-56; LEU-60; PHE-64; ASP-80; RP HIS-86; ASN-91; THR-91; SER-94; TYR-94; ILE-113; THR-121; LEU-164; GLY-164; RP GLN-167; PHE-180; VAL-187; SER-196; THR-198; TYR-202; ARG-204; ARG-213; RP LEU-214; MET-219; PRO-227; SER-228; VAL-242; PHE-243; PRO-247; LYS-249; RP THR-253; ALA-254; ARG-259; ARG-262; GLY-269; GLY-276; VAL-309; ASN-315; RP ALA-316; SER-317; TYR-320; ARG-323; ARG-327; LEU-327; ARG-328; ARG-330; RP PRO-342; GLY-352; PRO-356; LYS-358; SER-360; ALA-375; SER-392; SER-399 AND RP ARG-404 DEL, CHARACTERIZATION OF VARIANTS PRO-3; VAL-3; GLY-71; THR-154; RP VAL-289 AND ASN-313, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=26415523; DOI=10.1002/humu.22910; RA Lukas J., Scalia S., Eichler S., Pockrandt A.M., Dehn N., Cozma C., RA Giese A.K., Rolfs A.; RT "Functional and clinical consequences of novel alpha-galactosidase A RT mutations in Fabry disease."; RL Hum. Mutat. 37:43-51(2016). RN [57] RP VARIANT FABRYD ARG-47, CHARACTERIZATION OF VARIANTS FABRYD ARG-47 AND RP GLY-47, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=27211852; DOI=10.1080/00207454.2016.1191483; RA Ge W., Wei B., Zhu H., Miao Z., Zhang W., Leng C., Li J., Zhang D., Sun M., RA Xu X.; RT "A novel mutation of alpha-galactosidase A gene causes Fabry disease RT mimicking primary erythromelalgia in a Chinese family."; RL Int. J. Neurosci. 2016:1-6(2016). RN [58] RP VARIANT FABRYD THR-143. RX PubMed=27142856; DOI=10.1186/s13023-016-0441-z; RA Lenders M., Weidemann F., Kurschat C., Canaan-Kuehl S., Duning T., RA Stypmann J., Schmitz B., Reiermann S., Kraemer J., Blaschke D., Wanner C., RA Brand S.M., Brand E.; RT "Alpha-Galactosidase A p.A143T, a non-Fabry disease-causing variant."; RL Orphanet J. Rare Dis. 11:54-54(2016). CC -!- FUNCTION: Catalyzes the hydrolysis of glycosphingolipids and CC participates in their degradation in the lysosome. CC {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose CC residues in alpha-D-galactosides, including galactose CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22; CC Evidence={ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:27211852}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a globoside Gb3Cer (d18:1(4E)) + H2O = a beta-D-Gal-(1->4)- CC beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + D-galactose; CC Xref=Rhea:RHEA:21112, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:17950, ChEBI:CHEBI:18313; CC Evidence={ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21113; CC Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a globoside Gb3Cer + H2O = a beta-D-galactosyl-(1->4)-beta-D- CC glucosyl-(1<->1)-ceramide + D-galactose; Xref=Rhea:RHEA:48020, CC ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:79208, CC ChEBI:CHEBI:88154; Evidence={ECO:0000269|PubMed:10838196, CC ECO:0000269|PubMed:8804427}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48021; CC Evidence={ECO:0000305|PubMed:10838196, ECO:0000305|PubMed:8804427}; CC -!- ACTIVITY REGULATION: Galactosylgalactosylglucosylceramidase activity is CC stimulated by saposin B and ammonium chloride. CC {ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:8804427}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15003450}. CC -!- INTERACTION: CC P06280; Q2TAA5: ALG11; NbExp=2; IntAct=EBI-2513305, EBI-1048799; CC P06280; Q99767: APBA2; NbExp=2; IntAct=EBI-2513305, EBI-81711; CC P06280; Q12959: DLG1; NbExp=3; IntAct=EBI-2513305, EBI-357481; CC P06280; Q68DX3: FRMPD2; NbExp=2; IntAct=EBI-2513305, EBI-53993476; CC P06280; Q9Y3R0: GRIP1; NbExp=3; IntAct=EBI-2513305, EBI-5349621; CC P06280; Q9C0E4: GRIP2; NbExp=4; IntAct=EBI-2513305, EBI-949557; CC P06280; Q8TBB1: LNX1; NbExp=2; IntAct=EBI-2513305, EBI-739832; CC P06280; Q8N448: LNX2; NbExp=2; IntAct=EBI-2513305, EBI-2340947; CC P06280; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-2513305, EBI-924464; CC P06280; Q86UL8: MAGI2; NbExp=4; IntAct=EBI-2513305, EBI-311035; CC P06280; O75970: MPDZ; NbExp=3; IntAct=EBI-2513305, EBI-821405; CC P06280; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-2513305, EBI-8744528; CC P06280; Q8NI35: PATJ; NbExp=9; IntAct=EBI-2513305, EBI-724390; CC P06280; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-2513305, EBI-349819; CC P06280; Q14160: SCRIB; NbExp=3; IntAct=EBI-2513305, EBI-357345; CC P06280; Q99523: SORT1; NbExp=3; IntAct=EBI-2513305, EBI-1057058; CC P06280; O14907: TAX1BP3; NbExp=2; IntAct=EBI-2513305, EBI-723259; CC P06280; Q9P202: WHRN; NbExp=3; IntAct=EBI-2513305, EBI-310886; CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- RNA EDITING: Modified_positions=396 {ECO:0000269|PubMed:7503918}; CC Note=Partially edited.; CC -!- DISEASE: Fabry disease (FABRYD) [MIM:301500]: An X-linked inborn error CC of glycosphingolipid catabolism due to lysosomal alpha-galactosidase A CC deficiency, leading to systemic accumulation of globotriaosylceramide CC (Gb3) and related glycosphingolipids. Clinical features include CC angiokeratomas over the lower trunk, progressive renal failure, cardiac CC disease, cerebrovascular disease, small-fiber peripheral neuropathy, CC febrile episodes, and burning pain in the extremities. Disease onset is CC usually in childhood or adolescence. Death results from renal failure, CC cardiac or cerebrovascular disease. Heterozygous females may exhibit CC the disorder in an attenuated form. {ECO:0000269|PubMed:10090526, CC ECO:0000269|PubMed:10208848, ECO:0000269|PubMed:10666480, CC ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:10916280, CC ECO:0000269|PubMed:11076046, ECO:0000269|PubMed:11295840, CC ECO:0000269|PubMed:11668641, ECO:0000269|PubMed:11889412, CC ECO:0000269|PubMed:12694230, ECO:0000269|PubMed:12786754, CC ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:15162124, CC ECO:0000269|PubMed:15712228, ECO:0000269|PubMed:16533976, CC ECO:0000269|PubMed:1846223, ECO:0000269|PubMed:19621417, CC ECO:0000269|PubMed:2152885, ECO:0000269|PubMed:2171331, CC ECO:0000269|PubMed:2539398, ECO:0000269|PubMed:26415523, CC ECO:0000269|PubMed:27142856, ECO:0000269|PubMed:27211852, CC ECO:0000269|PubMed:7504405, ECO:0000269|PubMed:7531540, CC ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:7596372, CC ECO:0000269|PubMed:7599642, ECO:0000269|PubMed:7759078, CC ECO:0000269|PubMed:8069316, ECO:0000269|PubMed:8395937, CC ECO:0000269|PubMed:8738659, ECO:0000269|PubMed:8807334, CC ECO:0000269|PubMed:8834244, ECO:0000269|PubMed:8863162, CC ECO:0000269|PubMed:8875188, ECO:0000269|PubMed:8931708, CC ECO:0000269|PubMed:9100224, ECO:0000269|PubMed:9105656, CC ECO:0000269|PubMed:9452068, ECO:0000269|PubMed:9452090, CC ECO:0000269|PubMed:9452111, ECO:0000269|PubMed:9554750}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- PHARMACEUTICAL: Available under the names Replagal (from Shire) and CC Fabrazyme (from Genzyme). Used as a long-term enzyme replacement CC therapy in patients with a confirmed diagnosis of Fabry disease. The CC differences between Replagal (also known as agalsidase alpha) and CC Fabrazyme (also known as agalsidase beta) lies in the glycosylation CC patterns. Agalsidase beta is produced in the hamster CHO cell line CC while agalsidase alpha is produced in human cell lines. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05790; CAA29232.1; -; mRNA. DR EMBL; X14448; CAA32617.1; -; Genomic_DNA. DR EMBL; U78027; AAB64203.1; -; Genomic_DNA. DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002689; AAH02689.1; -; mRNA. DR EMBL; M13571; AAA51676.1; -; Genomic_DNA. DR EMBL; D00039; BAA34059.1; -; mRNA. DR EMBL; M18242; AAA52514.1; -; Genomic_DNA. DR EMBL; X16889; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M20317; AAA52559.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS14484.1; -. DR PIR; S04081; GBHUA. DR RefSeq; NP_000160.1; NM_000169.3. DR PDB; 1R46; X-ray; 3.25 A; A/B=32-429. DR PDB; 1R47; X-ray; 3.45 A; A/B=32-429. DR PDB; 3GXN; X-ray; 3.01 A; A/B=32-429. DR PDB; 3GXP; X-ray; 2.20 A; A/B=32-429. DR PDB; 3GXT; X-ray; 2.70 A; A/B=32-429. DR PDB; 3HG2; X-ray; 2.30 A; A/B=32-429. DR PDB; 3HG3; X-ray; 1.90 A; A/B=32-429. DR PDB; 3HG4; X-ray; 2.30 A; A/B=32-429. DR PDB; 3HG5; X-ray; 2.30 A; A/B=32-429. DR PDB; 3LX9; X-ray; 2.04 A; A/B=32-429. DR PDB; 3LXA; X-ray; 3.04 A; A/B=32-429. DR PDB; 3LXB; X-ray; 2.85 A; A/B=32-429. DR PDB; 3LXC; X-ray; 2.35 A; A/B=32-429. DR PDB; 3S5Y; X-ray; 2.10 A; A/B=32-429. DR PDB; 3S5Z; X-ray; 2.00 A; A/B=32-429. DR PDB; 3TV8; X-ray; 2.64 A; A/B=32-429. DR PDB; 4NXS; X-ray; 2.55 A; A/B=32-429. DR PDB; 6IBK; X-ray; 1.99 A; A/B=32-429. DR PDB; 6IBM; X-ray; 2.07 A; A/B=32-429. DR PDB; 6IBR; X-ray; 2.02 A; A/B=32-429. DR PDB; 6IBT; X-ray; 2.04 A; A/B=32-429. DR PDB; 8K7D; X-ray; 2.61 A; A/B=32-429. DR PDB; 8K7E; X-ray; 2.20 A; A/B=32-429. DR PDB; 8K7F; X-ray; 1.98 A; A/B=32-429. DR PDB; 8K7G; X-ray; 2.32 A; A/B=32-429. DR PDB; 8K7H; X-ray; 2.28 A; A/B=32-429. DR PDB; 8K7I; X-ray; 2.12 A; A/B=32-429. DR PDB; 8K7J; X-ray; 2.01 A; A/B=32-429. DR PDB; 8K7K; X-ray; 2.00 A; A/B=32-429. DR PDB; 8K7L; X-ray; 2.00 A; A/B=32-429. DR PDB; 9AVS; X-ray; 3.53 A; A/B=32-429. DR AlphaFoldDB; P06280; -. DR MDposit; P06280; -. DR MDRepo; P06280; -. DR SMR; P06280; -. DR BioGRID; 108981; 89. DR CORUM; P06280; -. DR FunCoup; P06280; 1248. DR IntAct; P06280; 117. DR NDEx; IQUERY-CP-GLA; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000218516; -. DR BindingDB; P06280; -. DR ChEMBL; CHEMBL2524; -. DR DrugBank; DB15874; Agalsidase alfa. DR DrugBank; DB04658; Calystegine B2. DR DrugBank; DB15236; Fucose. DR DrugBank; DB05018; Migalastat. DR DrugBank; DB14992; Pegunigalsidase alfa. DR DrugCentral; P06280; -. DR SwissLipids; SLP:000001380; -. DR Allergome; 9621; Hom s alpha-Galactosidase. DR CAZy; GH27; Glycoside Hydrolase Family 27. DR GlyConnect; P06280; 19 N-Linked glycans (3 sites). DR GlyCosmos; P06280; 3 sites, 18 glycans. DR GlyGen; P06280; 4 sites, 50 N-linked glycans (3 sites), 1 O-linked glycan (1 site). DR iPTMnet; P06280; -. DR PhosphoSitePlus; P06280; -. DR BioMuta; GLA; -. DR jPOST; P06280; -. DR MassIVE; P06280; -. DR PaxDb; 9606-ENSP00000218516; -. DR PeptideAtlas; P06280; -. DR ProteomicsDB; 51881; -. DR Pumba; P06280; -. DR Antibodypedia; 377; 458 antibodies from 37 providers. DR DNASU; 2717; -. DR Ensembl; ENST00000218516.4; ENSP00000218516.4; ENSG00000102393.15. DR GeneID; 2717; -. DR KEGG; hsa:2717; -. DR MANE-Select; ENST00000218516.4; ENSP00000218516.4; NM_000169.3; NP_000160.1. DR AGR; HGNC:4296; -. DR ClinPGx; PA28707; -. DR CTD; 2717; -. DR DisGeNET; 2717; -. DR GeneCards; GLA; -. DR GeneReviews; GLA; -. DR HGNC; HGNC:4296; GLA. DR HPA; ENSG00000102393; Low tissue specificity. DR MalaCards; GLA; -. DR MIM; 300644; gene. DR MIM; 301500; phenotype. DR OpenTargets; ENSG00000102393; -. DR Orphanet; 324; Fabry disease. DR VEuPathDB; HostDB:ENSG00000102393; -. DR eggNOG; KOG2366; Eukaryota. DR GeneTree; ENSGT00390000008751; -. DR HOGENOM; CLU_013093_0_0_1; -. DR InParanoid; P06280; -. DR OMA; MTPTMGW; -. DR OrthoDB; 5795902at2759; -. DR PAN-GO; P06280; 4 GO annotations based on evolutionary models. DR PhylomeDB; P06280; -. DR BioCyc; MetaCyc:HS02389-MONOMER; -. DR BRENDA; 3.2.1.22; 2681. DR PathwayCommons; P06280; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-9840310; Glycosphingolipid catabolism. DR SABIO-RK; P06280; -. DR SignaLink; P06280; -. DR SIGNOR; P06280; -. DR Agora; ENSG00000102393; -. DR BioGRID-ORCS; 2717; 7 hits in 784 CRISPR screens. DR ChiTaRS; GLA; human. DR EvolutionaryTrace; P06280; -. DR GeneWiki; Alpha-galactosidase; -. DR GenomeRNAi; 2717; -. DR Pharos; P06280; Tclin. DR PRO; PR:P06280; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P06280; protein. DR Bgee; ENSG00000102393; Expressed in pancreatic ductal cell and 177 other cell types or tissues. DR ExpressionAtlas; P06280; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IMP:UniProtKB. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IMP:UniProtKB. DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB. DR GO; GO:0003824; F:catalytic activity; IDA:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; TAS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB. DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central. DR GO; GO:0046479; P:glycosphingolipid catabolic process; IDA:UniProtKB. DR GO; GO:0046477; P:glycosylceramide catabolic process; ISS:UniProtKB. DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB. DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISS:UniProtKB. DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:UniProtKB. DR CDD; cd14792; GH27; 1. DR FunFam; 3.20.20.70:FF:000070; Alpha-galactosidase; 1. DR FunFam; 2.60.40.1180:FF:000017; Alpha-galactosidase A; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR002241; Glyco_hydro_27. DR InterPro; IPR000111; Glyco_hydro_27/36_CS. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR035373; Melibiase/NAGA_C. DR PANTHER; PTHR11452:SF14; ALPHA-GALACTOSIDASE A; 1. DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1. DR Pfam; PF16499; Melibiase_2; 1. DR Pfam; PF17450; Melibiase_2_C; 1. DR PRINTS; PR00740; GLHYDRLASE27. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1. DR PDBsum; 1R46; -. DR PDBsum; 1R47; -. DR PDBsum; 3GXN; -. DR PDBsum; 3GXP; -. DR PDBsum; 3GXT; -. DR PDBsum; 3HG2; -. DR PDBsum; 3HG3; -. DR PDBsum; 3HG4; -. DR PDBsum; 3HG5; -. DR PDBsum; 3LX9; -. DR PDBsum; 3LXA; -. DR PDBsum; 3LXB; -. DR PDBsum; 3LXC; -. DR PDBsum; 3S5Y; -. DR PDBsum; 3S5Z; -. DR PDBsum; 3TV8; -. DR PDBsum; 4NXS; -. DR PDBsum; 6IBK; -. DR PDBsum; 6IBM; -. DR PDBsum; 6IBR; -. DR PDBsum; 6IBT; -. DR PDBsum; 8K7D; -. DR PDBsum; 8K7E; -. DR PDBsum; 8K7F; -. DR PDBsum; 8K7G; -. DR PDBsum; 8K7H; -. DR PDBsum; 8K7I; -. DR PDBsum; 8K7J; -. DR PDBsum; 8K7K; -. DR PDBsum; 8K7L; -. DR PDBsum; 9AVS; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism; Lysosome; KW Pharmaceutical; Proteomics identification; Reference proteome; RNA editing; KW Signal. FT SIGNAL 1..31 FT CHAIN 32..429 FT /note="Alpha-galactosidase A" FT /id="PRO_0000001004" FT ACT_SITE 170 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT ACT_SITE 231 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 203..207 FT /ligand="substrate" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15003450" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15003450" FT CARBOHYD 215 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15003450, FT ECO:0000269|PubMed:19159218" FT DISULFID 52..94 FT DISULFID 56..63 FT DISULFID 142..172 FT DISULFID 202..223 FT DISULFID 378..382 FT VARIANT 3 FT /note="L -> P (does not affect enzyme activity; FT dbSNP:rs150547672)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077365" FT VARIANT 3 FT /note="L -> V (does not affect enzyme activity; FT dbSNP:rs869312133)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077366" FT VARIANT 12..14 FT /note="Missing (in FABRYD; has 4% of wild-type activity)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062550" FT VARIANT 20 FT /note="A -> D (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312134)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077367" FT VARIANT 20 FT /note="A -> P (in FABRYD; atypical; loss of enzyme FT activity; dbSNP:rs104894847)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:9105656" FT /id="VAR_012362" FT VARIANT 21 FT /note="L -> P (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312135)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077368" FT VARIANT 31 FT /note="A -> V (in FABRYD; dbSNP:rs869312448)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012363" FT VARIANT 32 FT /note="L -> P (in FABRYD; dbSNP:rs1569306168)" FT /evidence="ECO:0000269|PubMed:7599642" FT /id="VAR_000431" FT VARIANT 33 FT /note="D -> G (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312136)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077369" FT VARIANT 34 FT /note="N -> S (in FABRYD; dbSNP:rs104894835)" FT /evidence="ECO:0000269|PubMed:7504405, FT ECO:0000269|PubMed:7599642, ECO:0000269|PubMed:8395937" FT /id="VAR_000432" FT VARIANT 35 FT /note="G -> E (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312137)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077370" FT VARIANT 35 FT /note="G -> R (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8069316" FT /id="VAR_000433" FT VARIANT 36 FT /note="L -> W (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312138)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077371" FT VARIANT 40 FT /note="P -> L (in FABRYD; dbSNP:rs398123199)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012364" FT VARIANT 40 FT /note="P -> S (in FABRYD; loss of enzyme activity; FT dbSNP:rs104894831)" FT /evidence="ECO:0000269|PubMed:2152885, FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:9105656, FT ECO:0000269|PubMed:9452111" FT /id="VAR_000434" FT VARIANT 42 FT /note="M -> L (in FABRYD; dbSNP:rs797044613)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062551" FT VARIANT 42 FT /note="M -> T (in FABRYD; loss of enzyme activity; FT dbSNP:rs398123201)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077372" FT VARIANT 42 FT /note="M -> V (in FABRYD; dbSNP:rs797044613)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:8875188" FT /id="VAR_012365" FT VARIANT 43 FT /note="G -> R (in FABRYD; dbSNP:rs886044906)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062552" FT VARIANT 45..46 FT /note="LH -> RS (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012366" FT VARIANT 45 FT /note="L -> P (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077373" FT VARIANT 46 FT /note="H -> P (in FABRYD; has 36% of wild-type activity)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062553" FT VARIANT 46 FT /note="H -> R (in FABRYD; dbSNP:rs398123203)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012367" FT VARIANT 46 FT /note="H -> Y (in FABRYD; dbSNP:rs1928582757)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012368" FT VARIANT 47 FT /note="W -> G (in FABRYD; decreased alpha-galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:27211852" FT /id="VAR_012369" FT VARIANT 47 FT /note="W -> R (in FABRYD; decreased alpha-galactosidase FT activity)" FT /evidence="ECO:0000269|PubMed:27211852" FT /id="VAR_076478" FT VARIANT 48 FT /note="E -> D (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312254)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077374" FT VARIANT 49 FT /note="R -> L (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8069316" FT /id="VAR_000435" FT VARIANT 49 FT /note="R -> P (in FABRYD; dbSNP:rs398123205)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012370" FT VARIANT 49 FT /note="R -> S (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012371" FT VARIANT 52 FT /note="C -> R (in FABRYD; dbSNP:rs1057521047)" FT /evidence="ECO:0000269|PubMed:8807334, FT ECO:0000269|PubMed:8931708" FT /id="VAR_000436" FT VARIANT 52 FT /note="C -> S (in FABRYD; dbSNP:rs869312256)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000437" FT VARIANT 56 FT /note="C -> F (in FABRYD; dbSNP:rs869312258)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000438" FT VARIANT 56 FT /note="C -> G (in FABRYD; dbSNP:rs104894836)" FT /evidence="ECO:0000269|PubMed:7504405" FT /id="VAR_000439" FT VARIANT 56 FT /note="C -> Y (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312258)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:8875188" FT /id="VAR_012372" FT VARIANT 59 FT /note="E -> K (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000440" FT VARIANT 60 FT /note="P -> L (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312262)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077375" FT VARIANT 64 FT /note="I -> F (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312139)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077376" FT VARIANT 65 FT /note="S -> T (in FABRYD; does not affect enzyme function; FT dbSNP:rs104894848)" FT /evidence="ECO:0000269|PubMed:12786754, FT ECO:0000269|PubMed:9554750" FT /id="VAR_032290" FT VARIANT 66 FT /note="E -> Q (in FABRYD; has 52% of wild-type activity; FT dbSNP:rs104894833)" FT /evidence="ECO:0000269|PubMed:1315715, FT ECO:0000269|PubMed:19621417, ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_000441" FT VARIANT 71 FT /note="E -> G (does not affect enzyme activity; FT dbSNP:rs781927744)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077377" FT VARIANT 72 FT /note="M -> V (in FABRYD; atypical)" FT /evidence="ECO:0000269|PubMed:9105656, FT ECO:0000269|PubMed:9452090" FT /id="VAR_000442" FT VARIANT 80 FT /note="G -> D (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs781838005)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077378" FT VARIANT 85 FT /note="G -> D (in FABRYD; dbSNP:rs1569304898)" FT /evidence="ECO:0000269|PubMed:7599642" FT /id="VAR_000443" FT VARIANT 86 FT /note="Y -> C (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012373" FT VARIANT 86 FT /note="Y -> H (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312140)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077379" FT VARIANT 89 FT /note="L -> P (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012374" FT VARIANT 89 FT /note="L -> R (in FABRYD; dbSNP:rs1569304886)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000444" FT VARIANT 91 FT /note="I -> N (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312141)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077380" FT VARIANT 91 FT /note="I -> T (in FABRYD; mild; loss of enzyme activity; FT dbSNP:rs869312141)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012375" FT VARIANT 92 FT /note="D -> H (in FABRYD; dbSNP:rs886041315)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012376" FT VARIANT 92 FT /note="D -> Y (in FABRYD; dbSNP:rs886041315)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012377" FT VARIANT 93 FT /note="D -> G (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012378" FT VARIANT 93 FT /note="D -> N (in FABRYD; has no enzyme activity; FT dbSNP:rs869312270)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:19621417" FT /id="VAR_062554" FT VARIANT 94 FT /note="C -> S (in FABRYD; loss of enzyme activity; FT dbSNP:rs2147480697)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:26415523" FT /id="VAR_012379" FT VARIANT 94 FT /note="C -> Y (in FABRYD; loss of enzyme activity; FT dbSNP:rs113173389)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012380" FT VARIANT 95 FT /note="W -> S (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:11668641" FT /id="VAR_012381" FT VARIANT 97 FT /note="A -> V (in FABRYD; dbSNP:rs1569304867)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012382" FT VARIANT 100 FT /note="R -> K (in FABRYD; dbSNP:rs869312273)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000445" FT VARIANT 100 FT /note="R -> T (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012383" FT VARIANT 112..117 FT /note="Missing (in FABRYD)" FT /id="VAR_000446" FT VARIANT 112 FT /note="R -> C (in FABRYD; dbSNP:rs104894834)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:10916280, ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:9105656" FT /id="VAR_000447" FT VARIANT 112 FT /note="R -> H (in FABRYD; mild; dbSNP:rs372966991)" FT /evidence="ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:15712228, ECO:0000269|PubMed:7531540" FT /id="VAR_000448" FT VARIANT 112 FT /note="R -> S (in FABRYD; dbSNP:rs104894834)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062555" FT VARIANT 113 FT /note="F -> I (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312142)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077381" FT VARIANT 113 FT /note="F -> L (in FABRYD; mild; dbSNP:rs869312142)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012384" FT VARIANT 113 FT /note="F -> S (in FABRYD; dbSNP:rs2147480502)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012385" FT VARIANT 120..121 FT /note="LA -> PT (in FABRYD)" FT /id="VAR_000449" FT VARIANT 120 FT /note="L -> V (in FABRYD; has 42% of wild-type activity)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062556" FT VARIANT 121 FT /note="A -> T (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs782197638)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077382" FT VARIANT 128 FT /note="G -> E (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8807334" FT /id="VAR_000450" FT VARIANT 131 FT /note="L -> P (in FABRYD; dbSNP:rs869312298)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000451" FT VARIANT 134 FT /note="Y -> S (in FABRYD; dbSNP:rs2147477791)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012386" FT VARIANT 135 FT /note="A -> V (in FABRYD; dbSNP:rs1569304221)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062557" FT VARIANT 138 FT /note="G -> R (in FABRYD; dbSNP:rs1928326524)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012387" FT VARIANT 142 FT /note="C -> R (in FABRYD; dbSNP:rs886044845)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012388" FT VARIANT 142 FT /note="C -> Y (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7759078, FT ECO:0000269|PubMed:9105656" FT /id="VAR_000452" FT VARIANT 143 FT /note="A -> P (in FABRYD; dbSNP:rs104894845)" FT /evidence="ECO:0000269|PubMed:11889412, FT ECO:0000269|PubMed:7531540" FT /id="VAR_000453" FT VARIANT 143 FT /note="A -> T (in FABRYD; uncertain significance; FT dbSNP:rs104894845)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:16533976, ECO:0000269|PubMed:27142856, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012389" FT VARIANT 144 FT /note="G -> V (in FABRYD; dbSNP:rs782085638)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000454" FT VARIANT 146 FT /note="P -> S (in FABRYD; mild; dbSNP:rs104894837)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000455" FT VARIANT 148 FT /note="S -> N (in FABRYD; dbSNP:rs1555985829)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012390" FT VARIANT 148 FT /note="S -> R (in FABRYD; dbSNP:rs1569304190)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012391" FT VARIANT 154 FT /note="I -> T (does not affect enzyme activity; FT dbSNP:rs869312143)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077383" FT VARIANT 156 FT /note="A -> T (in FABRYD; dbSNP:rs28935195)" FT /evidence="ECO:0000269|PubMed:7599642" FT /id="VAR_000456" FT VARIANT 156 FT /note="A -> V (in FABRYD; dbSNP:rs869312307)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:9105656" FT /id="VAR_000457" FT VARIANT 162 FT /note="W -> C (in FABRYD; dbSNP:rs869312311)" FT /evidence="ECO:0000269|PubMed:8931708" FT /id="VAR_012392" FT VARIANT 162 FT /note="W -> R (in FABRYD; dbSNP:rs28935196)" FT /evidence="ECO:0000269|PubMed:7504405" FT /id="VAR_000458" FT VARIANT 163 FT /note="G -> V (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012393" FT VARIANT 164 FT /note="V -> G (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077384" FT VARIANT 164 FT /note="V -> L (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312144)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077385" FT VARIANT 165 FT /note="D -> V (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:8069316" FT /id="VAR_000459" FT VARIANT 166 FT /note="L -> V (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:7759078, ECO:0000269|PubMed:9105656" FT /id="VAR_000460" FT VARIANT 167 FT /note="L -> Q (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077386" FT VARIANT 170 FT /note="D -> V (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012394" FT VARIANT 171 FT /note="G -> D (in FABRYD)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062558" FT VARIANT 172 FT /note="C -> R (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012395" FT VARIANT 172 FT /note="C -> Y (in FABRYD; dbSNP:rs869312318)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000461" FT VARIANT 180 FT /note="L -> F (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312145)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077387" FT VARIANT 183 FT /note="G -> D (in FABRYD; dbSNP:rs398123212)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012396" FT VARIANT 187 FT /note="M -> I (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312146)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077388" FT VARIANT 187 FT /note="M -> V (in FABRYD; decreased enzyme activity; FT dbSNP:rs869312340)" FT /evidence="ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:26415523" FT /id="VAR_012397" FT VARIANT 196 FT /note="R -> S (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312147)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077389" FT VARIANT 198 FT /note="I -> T (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs727503950)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077390" FT VARIANT 201 FT /note="S -> F (in FABRYD)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062559" FT VARIANT 202 FT /note="C -> W (in FABRYD; dbSNP:rs104894838)" FT /evidence="ECO:0000269|PubMed:10208848" FT /id="VAR_000462" FT VARIANT 202 FT /note="C -> Y (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312344)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:9100224" FT /id="VAR_012398" FT VARIANT 204 FT /note="W -> R (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312148)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077391" FT VARIANT 205..207 FT /note="Missing (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012399" FT VARIANT 205 FT /note="P -> T (in FABRYD; dbSNP:rs397515870)" FT /evidence="ECO:0000269|PubMed:8807334, FT ECO:0000269|PubMed:8875188" FT /id="VAR_000463" FT VARIANT 213 FT /note="K -> R (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312149)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077392" FT VARIANT 214 FT /note="P -> L (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312150)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077393" FT VARIANT 215 FT /note="N -> S (in FABRYD; mild; dbSNP:rs28935197)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:11668641, ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:8395937, ECO:0000269|PubMed:9452111" FT /id="VAR_000464" FT VARIANT 216 FT /note="Y -> D (in FABRYD; dbSNP:rs1928199003)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012400" FT VARIANT 219 FT /note="I -> M (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312151)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077394" FT VARIANT 219 FT /note="I -> N (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000465" FT VARIANT 219 FT /note="I -> T (in FABRYD; has 46% of wild-type activity; FT dbSNP:rs2147473404)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062560" FT VARIANT 223 FT /note="C -> G (in FABRYD; dbSNP:rs869312381)" FT /evidence="ECO:0000269|PubMed:10208848" FT /id="VAR_012401" FT VARIANT 224 FT /note="N -> D (in FABRYD; dbSNP:rs1555985175)" FT /evidence="ECO:0000269|PubMed:10208848, FT ECO:0000269|PubMed:9452111" FT /id="VAR_000466" FT VARIANT 224 FT /note="N -> S (in FABRYD; dbSNP:rs869312383)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012402" FT VARIANT 226 FT /note="W -> R (in FABRYD; dbSNP:rs1928196393)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012403" FT VARIANT 227 FT /note="R -> P (in FABRYD; loss of enzyme activity; FT dbSNP:rs104894840)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077395" FT VARIANT 227 FT /note="R -> Q (in FABRYD; dbSNP:rs104894840)" FT /evidence="ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:7504405" FT /id="VAR_000467" FT VARIANT 228 FT /note="N -> S (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312152)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077396" FT VARIANT 230 FT /note="A -> T (in FABRYD; dbSNP:rs1928195468)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_012404" FT VARIANT 231 FT /note="D -> N (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8863162" FT /id="VAR_000468" FT VARIANT 234 FT /note="D -> E (in FABRYD)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062561" FT VARIANT 235 FT /note="S -> C (in FABRYD; dbSNP:rs797044746)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012405" FT VARIANT 236 FT /note="W -> C (in FABRYD; dbSNP:rs869312386)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012406" FT VARIANT 236 FT /note="W -> L (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012407" FT VARIANT 242 FT /note="I -> N (in FABRYD)" FT /evidence="ECO:0000269|PubMed:9105656" FT /id="VAR_012408" FT VARIANT 242 FT /note="I -> V (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs397515873)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077397" FT VARIANT 243 FT /note="L -> F (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs397515874)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077398" FT VARIANT 244 FT /note="D -> H (in FABRYD; dbSNP:rs727503948)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012409" FT VARIANT 244 FT /note="D -> N (in FABRYD; dbSNP:rs727503948)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000469" FT VARIANT 247 FT /note="S -> P (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312393)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077399" FT VARIANT 247 FT /note="S -> SWTS (in FABRYD)" FT /id="VAR_000470" FT VARIANT 249 FT /note="N -> K (in FABRYD; uncertain significance; decreased FT enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077400" FT VARIANT 253 FT /note="I -> T (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs727505292)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077401" FT VARIANT 254 FT /note="V -> A (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312153)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077402" FT VARIANT 258 FT /note="G -> R (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012410" FT VARIANT 259 FT /note="P -> L (in FABRYD; dbSNP:rs869312399)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012411" FT VARIANT 259 FT /note="P -> R (in FABRYD; decreased enzyme activity; FT dbSNP:rs869312399)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:26415523" FT /id="VAR_012412" FT VARIANT 260 FT /note="G -> A (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_012413" FT VARIANT 261 FT /note="G -> D (in FABRYD; dbSNP:rs869312401)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:9105656" FT /id="VAR_012414" FT VARIANT 262 FT /note="W -> R (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312154)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077403" FT VARIANT 263 FT /note="N -> S (in FABRYD; dbSNP:rs869312404)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012415" FT VARIANT 264 FT /note="D -> V (in FABRYD; dbSNP:rs28935486)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:7504405" FT /id="VAR_000471" FT VARIANT 264 FT /note="D -> Y (in FABRYD; dbSNP:rs190347120)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062562" FT VARIANT 265 FT /note="P -> R (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8931708" FT /id="VAR_012416" FT VARIANT 266 FT /note="D -> H (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10916280" FT /id="VAR_032291" FT VARIANT 266 FT /note="D -> N (in FABRYD; dbSNP:rs869312407)" FT /evidence="ECO:0000269|PubMed:11076046" FT /id="VAR_012418" FT VARIANT 266 FT /note="D -> V (in FABRYD; dbSNP:rs28935487)" FT /evidence="ECO:0000269|PubMed:7504405" FT /id="VAR_000472" FT VARIANT 267 FT /note="M -> I (in FABRYD; dbSNP:rs730880451)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:11668641" FT /id="VAR_012419" FT VARIANT 269 FT /note="V -> A (in FABRYD; dbSNP:rs28935488)" FT /evidence="ECO:0000269|PubMed:8395937" FT /id="VAR_000473" FT VARIANT 269 FT /note="V -> G (in FABRYD; loss of enzyme activity; FT dbSNP:rs28935488)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077404" FT VARIANT 272 FT /note="N -> K (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000474" FT VARIANT 272 FT /note="N -> S (in FABRYD; dbSNP:rs28935495)" FT /evidence="ECO:0000269|PubMed:15162124" FT /id="VAR_032292" FT VARIANT 276 FT /note="S -> G (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312432)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:26415523" FT /id="VAR_062563" FT VARIANT 279 FT /note="Q -> E (in FABRYD; mild; does not significantly FT affect the enzyme activity but the mutant protein levels FT are decreased presumably in the ER of the cells; FT dbSNP:rs28935485)" FT /evidence="ECO:0000269|PubMed:10838196, FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_000475" FT VARIANT 279 FT /note="Q -> H (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012420" FT VARIANT 280 FT /note="Q -> H (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012421" FT VARIANT 284 FT /note="M -> T (in FABRYD; dbSNP:rs1928171557)" FT /evidence="ECO:0000269|PubMed:8807334" FT /id="VAR_000476" FT VARIANT 285 FT /note="A -> P (in FABRYD)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062564" FT VARIANT 287 FT /note="W -> C (in FABRYD; dbSNP:rs104894839)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012422" FT VARIANT 287 FT /note="W -> G (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012423" FT VARIANT 288 FT /note="A -> D (in FABRYD; dbSNP:rs869312437)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000477" FT VARIANT 289 FT /note="I -> F (in FABRYD; dbSNP:rs140329381)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012424" FT VARIANT 289 FT /note="I -> V (decreased enzyme activity; FT dbSNP:rs140329381)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077405" FT VARIANT 296 FT /note="M -> I (in FABRYD; dbSNP:rs104894846)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:7596372, ECO:0000269|PubMed:9105656" FT /id="VAR_012425" FT VARIANT 296 FT /note="M -> V (in FABRYD; dbSNP:rs104894830)" FT /evidence="ECO:0000269|PubMed:1846223" FT /id="VAR_000478" FT VARIANT 297 FT /note="S -> F (in FABRYD; dbSNP:rs28935489)" FT /evidence="ECO:0000269|PubMed:7504405" FT /id="VAR_000479" FT VARIANT 298 FT /note="N -> H (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:8875188" FT /id="VAR_012426" FT VARIANT 298 FT /note="N -> K (in FABRYD; dbSNP:rs869312444)" FT /evidence="ECO:0000269|PubMed:8807334" FT /id="VAR_000480" FT VARIANT 298 FT /note="N -> S (in FABRYD; dbSNP:rs1569302985)" FT /evidence="ECO:0000269|PubMed:9100224" FT /id="VAR_012427" FT VARIANT 300 FT /note="L -> F (in FABRYD; dbSNP:rs2147472132)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062565" FT VARIANT 301 FT /note="R -> Q (in FABRYD; does not significantly affect the FT enzyme activity but the mutant protein levels are decreased FT presumably in the ER of the cells; dbSNP:rs104894828)" FT /evidence="ECO:0000269|PubMed:10208848, FT ECO:0000269|PubMed:10838196, ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:1315715, ECO:0000269|PubMed:2171331, FT ECO:0000269|PubMed:7575533, ECO:0000269|PubMed:7599642, FT ECO:0000269|PubMed:8738659, ECO:0000269|PubMed:9105656" FT /id="VAR_000481" FT VARIANT 309 FT /note="A -> V (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312155)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077406" FT VARIANT 313 FT /note="D -> N (does not affect enzyme activity; FT dbSNP:rs28935490)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077407" FT VARIANT 313 FT /note="D -> Y (in FABRYD; dbSNP:rs28935490)" FT /evidence="ECO:0000269|PubMed:11668641, FT ECO:0000269|PubMed:7504405, ECO:0000269|PubMed:9452111" FT /id="VAR_000482" FT VARIANT 315 FT /note="D -> N (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312156)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077408" FT VARIANT 316..322 FT /note="Missing (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8931708" FT /id="VAR_012429" FT VARIANT 316 FT /note="V -> A (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312157)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077409" FT VARIANT 316 FT /note="V -> E (in FABRYD)" FT /evidence="ECO:0000269|PubMed:8069316" FT /id="VAR_000483" FT VARIANT 317 FT /note="I -> S (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312158)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077410" FT VARIANT 320 FT /note="N -> K (in FABRYD)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_012430" FT VARIANT 320 FT /note="N -> Y (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:10916280, FT ECO:0000269|PubMed:26415523" FT /id="VAR_012431" FT VARIANT 321 FT /note="Q -> E (in FABRYD; dbSNP:rs730880439)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012432" FT VARIANT 323 FT /note="P -> R (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312159)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077411" FT VARIANT 327 FT /note="Q -> K (in FABRYD; dbSNP:rs28935491)" FT /evidence="ECO:0000269|PubMed:10208848, FT ECO:0000269|PubMed:8395937" FT /id="VAR_000484" FT VARIANT 327 FT /note="Q -> L (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312160)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077412" FT VARIANT 327 FT /note="Q -> R (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312160)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077413" FT VARIANT 328 FT /note="G -> A (in FABRYD; dbSNP:rs28935492)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:7504405" FT /id="VAR_000486" FT VARIANT 328 FT /note="G -> R (in FABRYD; loss of enzyme activity; FT dbSNP:rs104894832)" FT /evidence="ECO:0000269|PubMed:1315715, FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_000485" FT VARIANT 328 FT /note="G -> V (in FABRYD; dbSNP:rs28935492)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062566" FT VARIANT 330 FT /note="Q -> R (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312161)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077414" FT VARIANT 338 FT /note="E -> K (in FABRYD)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062567" FT VARIANT 340 FT /note="W -> R (in FABRYD; dbSNP:rs1555984869)" FT /evidence="ECO:0000269|PubMed:8875188" FT /id="VAR_012433" FT VARIANT 341 FT /note="E -> K (in FABRYD; dbSNP:rs869312214)" FT /evidence="ECO:0000269|PubMed:10090526" FT /id="VAR_012434" FT VARIANT 342 FT /note="R -> P (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077415" FT VARIANT 342 FT /note="R -> Q (in FABRYD; dbSNP:rs28935493)" FT /evidence="ECO:0000269|PubMed:7531540" FT /id="VAR_000487" FT VARIANT 352 FT /note="A -> G (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312162)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077416" FT VARIANT 356 FT /note="R -> P (in FABRYD; loss of enzyme activity; FT dbSNP:rs869312163)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077417" FT VARIANT 356 FT /note="R -> Q (in FABRYD; has 15% of wild-type activity; FT dbSNP:rs869312163)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062568" FT VARIANT 356 FT /note="R -> W (in FABRYD; dbSNP:rs104894827)" FT /evidence="ECO:0000269|PubMed:2539398" FT /id="VAR_000488" FT VARIANT 358 FT /note="E -> A (in FABRYD; dbSNP:rs869312224)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062569" FT VARIANT 358 FT /note="E -> K (in FABRYD; loss of enzyme activity; FT dbSNP:rs797044774)" FT /evidence="ECO:0000269|PubMed:26415523, FT ECO:0000269|PubMed:9452068" FT /id="VAR_000489" FT VARIANT 358 FT /note="Missing (in FABRYD; dbSNP:rs730880453)" FT /evidence="ECO:0000269|PubMed:10666480, FT ECO:0000269|PubMed:15712228, ECO:0000269|PubMed:8807334, FT ECO:0000269|PubMed:9105656" FT /id="VAR_000490" FT VARIANT 360 FT /note="G -> C (in FABRYD; has 6% of wild-type activity; FT dbSNP:rs782598150)" FT /evidence="ECO:0000269|PubMed:19621417" FT /id="VAR_062570" FT VARIANT 360 FT /note="G -> S (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077418" FT VARIANT 361 FT /note="G -> R (in FABRYD; severe; dbSNP:rs28935494)" FT /evidence="ECO:0000269|PubMed:8395937" FT /id="VAR_000491" FT VARIANT 363 FT /note="R -> H (in FABRYD; dbSNP:rs111422676)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012435" FT VARIANT 373 FT /note="G -> D (in FABRYD; dbSNP:rs869312227)" FT /evidence="ECO:0000269|PubMed:11295840" FT /id="VAR_012436" FT VARIANT 373 FT /note="G -> S (in FABRYD; dbSNP:rs727504348)" FT /evidence="ECO:0000269|PubMed:7575533, FT ECO:0000269|PubMed:9105656" FT /id="VAR_012437" FT VARIANT 375 FT /note="G -> A (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312164)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077419" FT VARIANT 377 FT /note="A -> D (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012438" FT VARIANT 378 FT /note="C -> Y (in FABRYD)" FT /evidence="ECO:0000269|PubMed:10666480" FT /id="VAR_012439" FT VARIANT 383 FT /note="Missing (in FABRYD; dbSNP:rs1057519609)" FT /evidence="ECO:0000269|PubMed:8834244" FT /id="VAR_000492" FT VARIANT 392 FT /note="R -> S (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs869312165)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077420" FT VARIANT 396 FT /note="F -> Y (in RNA edited version)" FT /id="VAR_000493" FT VARIANT 399 FT /note="W -> S (in FABRYD; uncertain significance; decreased FT enzyme activity; dbSNP:rs782449839)" FT /evidence="ECO:0000269|PubMed:26415523" FT /id="VAR_077421" FT VARIANT 404 FT /note="Missing (in FABRYD; loss of enzyme activity)" FT /evidence="ECO:0000269|PubMed:15712228, FT ECO:0000269|PubMed:26415523, ECO:0000269|PubMed:7504405, FT ECO:0000269|PubMed:9100224" FT /id="VAR_000494" FT VARIANT 409 FT /note="P -> A (in FABRYD; dbSNP:rs878853698)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012440" FT VARIANT 409 FT /note="P -> T (in FABRYD)" FT /evidence="ECO:0000269|PubMed:11668641" FT /id="VAR_012441" FT VARIANT 410 FT /note="T -> A (in FABRYD; dbSNP:rs104894852)" FT /evidence="ECO:0000269|PubMed:12694230" FT /id="VAR_032293" FT VARIANT 414 FT /note="L -> S (in FABRYD; dbSNP:rs869312246)" FT /evidence="ECO:0000269|PubMed:15712228" FT /id="VAR_062571" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 66..78 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:3GXT" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1R47" FT HELIX 116..126 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 130..140 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 149..151 FT /evidence="ECO:0007829|PDB:6IBT" FT HELIX 152..162 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 177..193 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 216..222 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 236..248 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 272..274 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 305..311 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 314..320 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 329..334 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:8K7F" FT STRAND 349..355 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:3HG3" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 379..390 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 392..398 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 402..407 FT /evidence="ECO:0007829|PDB:3HG3" FT STRAND 412..419 FT /evidence="ECO:0007829|PDB:3HG3" FT HELIX 420..424 FT /evidence="ECO:0007829|PDB:3HG3" SQ SEQUENCE 429 AA; 48767 MW; 613F8BF21B107D7B CRC64; MQLRNPELHL GCALALRFLA LVSWDIPGAR ALDNGLARTP TMGWLHWERF MCNLDCQEEP DSCISEKLFM EMAELMVSEG WKDAGYEYLC IDDCWMAPQR DSEGRLQADP QRFPHGIRQL ANYVHSKGLK LGIYADVGNK TCAGFPGSFG YYDIDAQTFA DWGVDLLKFD GCYCDSLENL ADGYKHMSLA LNRTGRSIVY SCEWPLYMWP FQKPNYTEIR QYCNHWRNFA DIDDSWKSIK SILDWTSFNQ ERIVDVAGPG GWNDPDMLVI GNFGLSWNQQ VTQMALWAIM AAPLFMSNDL RHISPQAKAL LQDKDVIAIN QDPLGKQGYQ LRQGDNFEVW ERPLSGLAWA VAMINRQEIG GPRSYTIAVA SLGKGVACNP ACFITQLLPV KRKLGFYEWT SRLRSHINPT GTVLLQLENT MQMSLKDLL //