ID PIGG_HUMAN Reviewed; 983 AA. AC Q5H8A4; B4DKC7; Q2TAK5; Q6UX31; Q7L5Y4; Q8N866; Q8NCC9; Q96SY9; AC Q9BVT7; Q9NXG5; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 10-OCT-2018, entry version 117. DE RecName: Full=GPI ethanolamine phosphate transferase 2; DE EC=2.-.-.-; DE AltName: Full=GPI7 homolog; DE Short=hGPI7; DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class G protein; DE Short=PIG-G; GN Name=PIGG; Synonyms=GPI7; ORFNames=UNQ1930/PRO4405; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, AND INTERACTION WITH PIGF. RX PubMed=15632136; DOI=10.1074/jbc.M413755200; RA Shishioh N., Hong Y., Ohishi K., Ashida H., Maeda Y., Kinoshita T.; RT "GPI7 is the second partner of PIG-F and involved in modification of RT glycosylphosphatidylinositol."; RL J. Biol. Chem. 280:9728-9734(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA libraries."; RL DNA Res. 12:117-126(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 367-983 (ISOFORM 1), AND VARIANT RP ILE-699. RC TISSUE=Cervix, Colon mucosa, Teratocarcinoma, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS RP HIS-458; ARG-610 AND ILE-699. RC TISSUE=Lung, and Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP VARIANT MRT53 CYS-669, INVOLVEMENT IN MRT53, AND CHARACTERIZATION OF RP VARIANT MRT53 CYS-669. RX PubMed=26996948; DOI=10.1016/j.ajhg.2016.02.007; RA Makrythanasis P., Kato M., Zaki M.S., Saitsu H., Nakamura K., RA Santoni F.A., Miyatake S., Nakashima M., Issa M.Y., Guipponi M., RA Letourneau A., Logan C.V., Roberts N., Parry D.A., Johnson C.A., RA Matsumoto N., Hamamy H., Sheridan E., Kinoshita T., Antonarakis S.E., RA Murakami Y.; RT "Pathogenic variants in PIGG cause intellectual disability with RT seizures and hypotonia."; RL Am. J. Hum. Genet. 98:615-626(2016). CC -!- FUNCTION: Ethanolamine phosphate transferase involved in CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers CC ethanolamine phosphate to the GPI second mannose. CC {ECO:0000269|PubMed:15632136}. CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol- CC anchor biosynthesis. CC -!- SUBUNIT: Forms a complex with PIGF. PIGF is required to stabilize CC it. Competes with PIGO for the binding of PIGF. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:15632136}; Multi-pass membrane protein CC {ECO:0000269|PubMed:15632136}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q5H8A4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5H8A4-2; Sequence=VSP_019832; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q5H8A4-3; Sequence=VSP_019828; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=Q5H8A4-4; Sequence=VSP_019831, VSP_019833; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=5; CC IsoId=Q5H8A4-5; Sequence=VSP_019827, VSP_019829, VSP_019830; CC Note=No experimental confirmation available.; CC Name=6; CC IsoId=Q5H8A4-6; Sequence=VSP_054387, VSP_054388, VSP_019833; CC Note=No experimental confirmation available.; CC -!- DISEASE: Mental retardation, autosomal recessive 53 (MRT53) CC [MIM:616917]: A form of mental retardation, a disorder CC characterized by significantly below average general intellectual CC functioning associated with impairments in adaptive behavior and CC manifested during the developmental period. Most MRT53 patients CC manifest severely delayed psychomotor development, hypotonia, and CC early-onset seizures. Additional features, such as cerebellar CC hypoplasia and ataxia have been observed in some patients. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. Cells from patients carrying PIGG CC disease-causing mutations show abnormal accumulation of the GPI CC precursors H7 and H7' and absence of mature GPI precursor H8, CC consistent with a loss of function. However, GPI-anchored CC proteins, including CD59, CD55, CD24 and CD16, are normally CC expressed at the cell surface of lymphocytes and granulocytes and CC CD59 exhibits sensitivity to bacterial phosphatidylinositol- CC specific phospholipase C, suggesting a normal structure. The role CC of PIGG in MRT53 etiology is not clear. CC {ECO:0000269|PubMed:26996948}. CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ88902.1; Type=Erroneous termination; Positions=311; Note=Translated as Gln.; Evidence={ECO:0000305}; CC Sequence=BAA91046.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAB55130.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; AB162713; BAD89023.1; -; mRNA. DR EMBL; AY358538; AAQ88902.1; ALT_SEQ; mRNA. DR EMBL; AK074815; BAC11227.1; -; mRNA. DR EMBL; AK000272; BAA91046.1; ALT_INIT; mRNA. DR EMBL; AK027465; BAB55130.1; ALT_INIT; mRNA. DR EMBL; AK097244; BAC04984.1; -; mRNA. DR EMBL; AK296507; BAG59139.1; -; mRNA. DR EMBL; AC092574; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC116565; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000937; AAH00937.2; -; mRNA. DR EMBL; BC001249; AAH01249.2; -; mRNA. DR EMBL; BC110878; AAI10879.1; -; mRNA. DR CCDS; CCDS3336.1; -. [Q5H8A4-2] DR CCDS; CCDS46992.1; -. [Q5H8A4-1] DR CCDS; CCDS75080.1; -. [Q5H8A4-3] DR CCDS; CCDS75083.1; -. [Q5H8A4-5] DR RefSeq; NP_001120650.1; NM_001127178.2. [Q5H8A4-1] DR RefSeq; NP_001275980.1; NM_001289051.1. DR RefSeq; NP_001275981.1; NM_001289052.1. [Q5H8A4-3] DR RefSeq; NP_001275984.1; NM_001289055.1. [Q5H8A4-6] DR RefSeq; NP_001275986.1; NM_001289057.1. [Q5H8A4-5] DR RefSeq; NP_060203.3; NM_017733.4. [Q5H8A4-2] DR UniGene; Hs.7099; -. DR ProteinModelPortal; Q5H8A4; -. DR SMR; Q5H8A4; -. DR BioGrid; 120220; 9. DR IntAct; Q5H8A4; 1. DR MINT; Q5H8A4; -. DR STRING; 9606.ENSP00000415203; -. DR iPTMnet; Q5H8A4; -. DR PhosphoSitePlus; Q5H8A4; -. DR BioMuta; PIGG; -. DR DMDM; 74707851; -. DR EPD; Q5H8A4; -. DR MaxQB; Q5H8A4; -. DR PaxDb; Q5H8A4; -. DR PeptideAtlas; Q5H8A4; -. DR PRIDE; Q5H8A4; -. DR ProteomicsDB; 62844; -. DR ProteomicsDB; 62845; -. [Q5H8A4-2] DR ProteomicsDB; 62846; -. [Q5H8A4-3] DR ProteomicsDB; 62847; -. [Q5H8A4-4] DR ProteomicsDB; 62848; -. [Q5H8A4-5] DR Ensembl; ENST00000310340; ENSP00000311750; ENSG00000174227. [Q5H8A4-2] DR Ensembl; ENST00000383028; ENSP00000372494; ENSG00000174227. [Q5H8A4-3] DR Ensembl; ENST00000453061; ENSP00000415203; ENSG00000174227. [Q5H8A4-1] DR Ensembl; ENST00000503111; ENSP00000426002; ENSG00000174227. [Q5H8A4-5] DR GeneID; 54872; -. DR KEGG; hsa:54872; -. DR UCSC; uc003gaj.6; human. [Q5H8A4-1] DR CTD; 54872; -. DR DisGeNET; 54872; -. DR EuPathDB; HostDB:ENSG00000174227.15; -. DR GeneCards; PIGG; -. DR HGNC; HGNC:25985; PIGG. DR HPA; HPA015997; -. DR MalaCards; PIGG; -. DR MIM; 616917; phenotype. DR MIM; 616918; gene. DR neXtProt; NX_Q5H8A4; -. DR OpenTargets; ENSG00000174227; -. DR PharmGKB; PA143485575; -. DR eggNOG; KOG2125; Eukaryota. DR eggNOG; COG1524; LUCA. DR GeneTree; ENSGT00910000144269; -. DR HOGENOM; HOG000171439; -. DR HOVERGEN; HBG075245; -. DR InParanoid; Q5H8A4; -. DR KO; K05310; -. DR OMA; WYFLVNT; -. DR OrthoDB; EOG091G04HZ; -. DR PhylomeDB; Q5H8A4; -. DR TreeFam; TF300609; -. DR Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI). DR UniPathway; UPA00196; -. DR ChiTaRS; PIGG; human. DR GenomeRNAi; 54872; -. DR PRO; PR:Q5H8A4; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000174227; Expressed in 214 organ(s), highest expression level in lower esophagus muscularis layer. DR CleanEx; HS_PIGG; -. DR ExpressionAtlas; Q5H8A4; baseline and differential. DR Genevisible; Q5H8A4; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IDA:MGI. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; TAS:Reactome. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:MGI. DR GO; GO:0016254; P:preassembly of GPI anchor in ER membrane; TAS:Reactome. DR CDD; cd16024; GPI_EPT_2; 1. DR Gene3D; 3.40.720.10; -; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR002591; Phosphodiest/P_Trfase. DR InterPro; IPR037674; PIG-G_N. DR Pfam; PF01663; Phosphodiest; 1. DR SUPFAM; SSF53649; SSF53649; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Disease mutation; KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; KW Membrane; Mental retardation; Polymorphism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 983 GPI ethanolamine phosphate transferase 2. FT /FTId=PRO_0000246185. FT TOPO_DOM 1 431 Lumenal. {ECO:0000255}. FT TRANSMEM 432 452 Helical. {ECO:0000255}. FT TRANSMEM 471 491 Helical. {ECO:0000255}. FT TRANSMEM 506 526 Helical. {ECO:0000255}. FT TRANSMEM 552 572 Helical. {ECO:0000255}. FT TRANSMEM 699 719 Helical. {ECO:0000255}. FT TRANSMEM 721 741 Helical. {ECO:0000255}. FT TRANSMEM 752 772 Helical. {ECO:0000255}. FT TRANSMEM 789 809 Helical. {ECO:0000255}. FT TRANSMEM 812 832 Helical. {ECO:0000255}. FT TRANSMEM 879 899 Helical. {ECO:0000255}. FT TRANSMEM 919 939 Helical. {ECO:0000255}. FT TRANSMEM 955 975 Helical. {ECO:0000255}. FT CARBOHYD 194 194 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 1 122 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054387. FT VAR_SEQ 1 89 Missing (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_019827. FT VAR_SEQ 120 252 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_019828. FT VAR_SEQ 372 388 DPGFEQFKMSERLHGNW -> GSHPAPAQRPTGTAQKG FT (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_019829. FT VAR_SEQ 389 983 Missing (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_019830. FT VAR_SEQ 430 463 YDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAEL -> FSP FT CSCSASHRHCTERLSWKSHCHLLGFLCSFIW (in FT isoform 4). FT {ECO:0000303|PubMed:12975309}. FT /FTId=VSP_019831. FT VAR_SEQ 430 463 YDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAEL -> FSP FT CSCSASHRHCAERLSWKSHCHLLGFLCSFIW (in FT isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_054388. FT VAR_SEQ 437 444 Missing (in isoform 2). FT {ECO:0000303|PubMed:16303743}. FT /FTId=VSP_019832. FT VAR_SEQ 464 983 Missing (in isoform 4 and isoform 6). FT {ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:14702039}. FT /FTId=VSP_019833. FT VARIANT 55 55 S -> Y (in dbSNP:rs34120878). FT /FTId=VAR_057680. FT VARIANT 458 458 R -> H (in dbSNP:rs13115344). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_027022. FT VARIANT 610 610 C -> R (in dbSNP:rs7666425). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_027023. FT VARIANT 669 669 R -> C (in MRT53; found in a compound FT heterozygote that also carries a FT microdeletion encompassing PIGG; almost FT complete loss of ethanolamine phosphate FT transferase activity, as evidenced by FT abnormal accumulation of the GPI FT precursors H7 and H7' and absence of FT mature GPI precursor H8 in patient FT lymphocytes; does not affect protein FT expression levels in transfected HEK293 FT cells; dbSNP:rs372392424). FT {ECO:0000269|PubMed:26996948}. FT /FTId=VAR_076775. FT VARIANT 699 699 V -> I (in dbSNP:rs13114026). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_027024. FT VARIANT 731 731 V -> I (in dbSNP:rs34916638). FT /FTId=VAR_060086. FT VARIANT 881 881 I -> T (in dbSNP:rs34623004). FT /FTId=VAR_060087. FT VARIANT 932 932 F -> S (in dbSNP:rs1127410). FT /FTId=VAR_027025. FT CONFLICT 624 624 D -> G (in Ref. 3; BAC11227). FT {ECO:0000305}. FT CONFLICT 889 889 F -> L (in Ref. 3; BAC11227). FT {ECO:0000305}. SQ SEQUENCE 983 AA; 108173 MW; 18D5DF737B000D2D CRC64; MRLGSGTFAT CCVAIEVLGI AVFLRGFFPA PVRSSARAEH GAEPPAPEPS AGASSNWTTL PPPLFSKVVI VLIDALRDDF VFGSKGVKFM PYTTYLVEKG ASHSFVAEAK PPTVTMPRIK ALMTGSLPGF VDVIRNLNSP ALLEDSVIRQ AKAAGKRIVF YGDETWVKLF PKHFVEYDGT TSFFVSDYTE VDNNVTRHLD KVLKRGDWDI LILHYLGLDH IGHISGPNSP LIGQKLSEMD SVLMKIHTSL QSKERETPLP NLLVLCGDHG MSETGSHGAS STEEVNTPLI LISSAFERKP GDIRHPKHVQ QTDVAATLAI ALGLPIPKDS VGSLLFPVVE GRPMREQLRF LHLNTVQLSK LLQENVPSYE KDPGFEQFKM SERLHGNWIR LYLEEKHSEV LFNLGSKVLR QYLDALKTLS LSLSAQVAQY DIYSMMVGTV VVLEVLTLLL LSVPQALRRK AELEVPLSSP GFSLLFYLVI LVLSAVHVIV CTSAESSCYF CGLSWLAAGG VMVLASALLC VIVSVLTNVL VGGNTPRKNP MHPSSRWSEL DLLILLGTAG HVLSLGASSF VEEEHQTWYF LVNTLCLALS QETYRNYFLG DDGEPPCGLC VEQGHDGATA AWQDGPGCDV LERDKGHGSP STSEVLRGRE KWMVLASPWL ILACCRLLRS LNQTGVQWAH RPDLGHWLTS SDHKAELSVL AALSLLVVFV LVQRGCSPVS KAALALGLLG VYCYRAAIGS VRFPWRPDSK DISKGIIEAR FVYVFVLGIL FTGTKDLLKS QVIAADFKLK TVGLWEIYSG LVLLAALLFR PHNLPVLAFS LLIQTLMTKF IWKPLRHDAA EITVMHYWFG QAFFYFQGNS NNIATVDISA GFVGLDTYVE IPAVLLTAFG TYAGPVLWAS HLVHFLSSET RSGSALSHAC FCYALICSIP VFTYIVLVTS LRYHLFIWSV FSPKLLYEGM HLLITAAVCV FFTAMDQTRL TQS //