ID PHLD_HUMAN Reviewed; 840 AA. AC P80108; Q15127; Q15128; Q2M2F2; Q5T3Y0; Q7Z6T8; Q8TCV0; Q8WW82; Q96ID6; AC Q9H167; Q9H4M1; Q9UJC9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 3. DT 04-NOV-2026, entry version 193. DE RecName: Full=Phosphatidylinositol-glycan-specific phospholipase D {ECO:0000305|PubMed:17720976}; DE Short=PI-G PLD; DE EC=3.1.4.50 {ECO:0000269|PubMed:17720976}; DE AltName: Full=Glycoprotein phospholipase D; DE AltName: Full=Glycosyl-phosphatidylinositol-specific phospholipase D {ECO:0000303|PubMed:2760042}; DE Short=GPI-PLD {ECO:0000303|Ref.1}; DE Short=GPI-specific phospholipase D {ECO:0000303|PubMed:2760042}; DE Flags: Precursor; GN Name=GPLD1 {ECO:0000312|HGNC:HGNC:4459}; Synonyms=PIGPLD1; 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] (ISOFORM 1), AND VARIANTS ILE-30; VAL-350; RP MET-461 AND ILE-698. RC TISSUE=Liver, and Pancreas; RA Tsang T.C., Fung W.-J.C., Levine J., Metz C.N., Davitz M.A., Burns D.K., RA Huang K.-S., Kochan J.P.; RT "Isolation and expression of two human glycosylphosphatidylinositol RT phospholipase D (GPI-PLD) cDNAs."; RL FASEB J. 6:A1922-A1922(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA] RP OF 384-840, AND VARIANTS ILE-30; VAL-694 AND ILE-698. RC TISSUE=Liver; RX PubMed=11072085; DOI=10.1016/s0167-4781(00)00194-9; RA Schofield J.N., Rademacher T.W.; RT "Structure and expression of the human glycosylphosphatidylinositol RT phospholipase D1 (GPLD1) gene."; RL Biochim. Biophys. Acta 1494:189-194(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-698. RC TISSUE=Bone marrow; RA Tang J.H., Gu S.L., Zhang X.J.; RT "Preliminary study of the gene structure of human RT glycosylphosphatidylinositol specific phospholipase D."; RL Hunan Yi Ke Da Xue Xue Bao 26:96-97(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 266-840 (ISOFORM 1), AND VARIANTS VAL-17; ILE-30 AND RP ILE-698. RC TISSUE=Eye, and Liver; 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 PARTIAL PROTEIN SEQUENCE. RC TISSUE=Serum; RX PubMed=1606959; DOI=10.1111/j.1432-1033.1992.tb16981.x; RA Hoener M.C., Brodbeck U.; RT "Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic RT glycoprotein that in serum is associated with high-density lipoproteins."; RL Eur. J. Biochem. 206:747-757(1992). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=2760042; DOI=10.1016/s0021-9258(18)80065-5; RA Davitz M.A., Hom J., Schenkman S.; RT "Purification of a glycosyl-phosphatidylinositol-specific phospholipase D RT from human plasma."; RL J. Biol. Chem. 264:13760-13764(1989). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-94. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [9] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17720976; DOI=10.1074/jbc.m702713200; RA Watanabe K., Bianco C., Strizzi L., Hamada S., Mancino M., Bailly V., RA Mo W., Wen D., Miatkowski K., Gonzales M., Sanicola M., Seno M., RA Salomon D.S.; RT "Growth factor induction of Cripto-1 shedding by RT glycosylphosphatidylinositol-phospholipase D and enhancement of endothelial RT cell migration."; RL J. Biol. Chem. 282:31643-31655(2007). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-659. 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). CC -!- FUNCTION: Hydrolyzes the inositol phosphate linkage of CC glycosylphosphatidylinositol (GPI)-anchored membrane proteins, thereby CC releasing them from the cell surface. Cleaves on the inositol side of CC the anchor, leaving the phosphate group attached to the membrane CC (PubMed:17720976, PubMed:2760042). This release of GPI-anchored CC proteins can modulate diverse biological processes, including the CC activation of signaling pathways (PubMed:17720976). CC {ECO:0000269|PubMed:17720976, ECO:0000269|PubMed:2760042}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-C-terminal carboxyl phosphoethanolamide-(1-radyl-2- CC octadecanoyl)-GPI(deacylinositol-H7) + H2O = [protein]-C-terminal CC carboxyl phosphoethanolamide-glycosylinositol (deacylinositol-H7) + CC 1-radyl-2-octadecanoyl-sn-glycero-3-phosphate + H(+); CC Xref=Rhea:RHEA:86263, Rhea:RHEA-COMP:20747, Rhea:RHEA-COMP:20748, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:235441, CC ChEBI:CHEBI:235464, ChEBI:CHEBI:235465; EC=3.1.4.50; CC Evidence={ECO:0000269|PubMed:17720976, ECO:0000269|PubMed:2760042}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:86264; CC Evidence={ECO:0000269|PubMed:17720976}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 4.5-8.0. {ECO:0000269|PubMed:2760042}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2760042}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2760042}. CC Note=Associated with the High-Density Lipoproteins (HDL). CC {ECO:0000250|UniProtKB:P80109}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P80108-1; Sequence=Displayed; CC Name=2; CC IsoId=P80108-2; Sequence=VSP_023261, VSP_023262; CC -!- SIMILARITY: Belongs to the GPLD1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA36444.1; Type=Miscellaneous discrepancy; Note=This sequence has numerous of conflicts with the human genome.; 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; L11701; AAA36444.1; ALT_SEQ; mRNA. DR EMBL; L11702; AAA36445.1; -; mRNA. DR EMBL; AJ308108; CAC87068.1; -; mRNA. DR EMBL; AJ400872; CAC14844.1; -; Genomic_DNA. DR EMBL; AJ400873; CAC14844.1; JOINED; Genomic_DNA. DR EMBL; AJ400874; CAC14844.1; JOINED; Genomic_DNA. DR EMBL; AJ400875; CAC14844.1; JOINED; Genomic_DNA. DR EMBL; AJ400876; CAC14844.1; JOINED; Genomic_DNA. DR EMBL; AY007546; AAG16627.2; -; mRNA. DR EMBL; AL359713; CAI17103.1; -; Genomic_DNA. DR EMBL; AL031230; CAI17103.1; JOINED; Genomic_DNA. DR EMBL; AL031230; CAI22602.1; -; Genomic_DNA. DR EMBL; AL359713; CAI22602.1; JOINED; Genomic_DNA. DR EMBL; AL031230; CAD92520.1; -; Genomic_DNA. DR EMBL; BC007614; AAH07614.1; -; mRNA. DR EMBL; BC020748; AAH20748.1; -; mRNA. DR EMBL; BC093645; AAH93645.1; -; mRNA. DR EMBL; BC112001; AAI12002.1; -; mRNA. DR CCDS; CCDS4553.1; -. [P80108-1] DR RefSeq; NP_001494.2; NM_001503.4. [P80108-1] DR AlphaFoldDB; P80108; -. DR BioGRID; 109083; 9. DR FunCoup; P80108; 125. DR IntAct; P80108; 2. DR NDEx; IQUERY-CP-GPLD1; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000230036; -. DR GlyConnect; P80108; 19 N-Linked glycans (4 sites). DR GlyCosmos; P80108; 10 sites, 39 glycans. DR GlyGen; P80108; 10 sites, 39 N-linked glycans (4 sites). DR iPTMnet; P80108; -. DR PhosphoSitePlus; P80108; -. DR BioMuta; GPLD1; -. DR DMDM; 126302583; -. DR CPTAC; CPTAC-2231; -. DR MassIVE; P80108; -. DR PaxDb; 9606-ENSP00000230036; -. DR PeptideAtlas; P80108; -. DR ProteomicsDB; 57666; -. [P80108-1] DR ProteomicsDB; 57667; -. [P80108-2] DR Antibodypedia; 1368; 301 antibodies from 31 providers. DR DNASU; 2822; -. DR Ensembl; ENST00000230036.2; ENSP00000230036.1; ENSG00000112293.16. [P80108-1] DR GeneID; 2822; -. DR KEGG; hsa:2822; -. DR MANE-Select; ENST00000230036.2; ENSP00000230036.1; NM_001503.4; NP_001494.2. DR UCSC; uc003ned.3; human. [P80108-1] DR AGR; HGNC:4459; -. DR ClinPGx; PA28842; -. DR CTD; 2822; -. DR DisGeNET; 2822; -. DR GeneCards; GPLD1; -. DR HGNC; HGNC:4459; GPLD1. DR HPA; ENSG00000112293; Tissue enriched (liver). DR MalaCards; GPLD1; -. DR MIM; 602515; gene. DR OpenTargets; ENSG00000112293; -. DR VEuPathDB; HostDB:ENSG00000112293; -. DR eggNOG; KOG3637; Eukaryota. DR GeneTree; ENSGT00390000013522; -. DR HOGENOM; CLU_011756_0_0_1; -. DR InParanoid; P80108; -. DR OMA; AADWFMS; -. DR OrthoDB; 5317514at2759; -. DR PAN-GO; P80108; 3 GO annotations based on evolutionary models. DR PhylomeDB; P80108; -. DR BRENDA; 3.1.4.50; 2681. DR PathwayCommons; P80108; -. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR SignaLink; P80108; -. DR Agora; ENSG00000112293; -. DR BioGRID-ORCS; 2822; 6 hits in 1150 CRISPR screens. DR ChiTaRS; GPLD1; human. DR GeneWiki; GPLD1; -. DR GenomeRNAi; 2822; -. DR Pharos; P80108; Tbio. DR PRO; PR:P80108; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P80108; protein. DR Bgee; ENSG00000112293; Expressed in secondary oocyte and 153 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0004630; F:D-type glycerophospholipase activity; IDA:UniProtKB. DR GO; GO:0004621; F:GPI anchor phospholipase D activity; IDA:UniProtKB. DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB. DR GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome. DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:UniProtKB. DR GO; GO:0071397; P:cellular response to cholesterol; IMP:UniProtKB. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB. DR GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB. DR GO; GO:0071401; P:cellular response to triglyceride; IMP:UniProtKB. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB. DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB. DR GO; GO:0002430; P:complement receptor mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0035701; P:hematopoietic stem cell migration; TAS:UniProtKB. DR GO; GO:0097241; P:hematopoietic stem cell migration to bone marrow; TAS:UniProtKB. DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; ISS:UniProtKB. DR GO; GO:0001503; P:ossification; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB. DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB. DR GO; GO:0010983; P:positive regulation of high-density lipoprotein particle clearance; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB. DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB. DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IDA:UniProtKB. DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB. DR GO; GO:0070633; P:transepithelial transport; ISS:UniProtKB. DR FunFam; 2.130.10.130:FF:000010; Glycosylphosphatidylinositol specific phospholipase D1; 1. DR FunFam; 2.130.10.130:FF:000011; Glycosylphosphatidylinositol specific phospholipase D1; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR001028; Gprt_PLipase_D. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR029002; PLPC/GPLD1. DR PANTHER; PTHR23221; GLYCOSYLPHOSPHATIDYLINOSITOL PHOSPHOLIPASE D; 1. DR PANTHER; PTHR23221:SF7; PHOSPHATIDYLINOSITOL-GLYCAN-SPECIFIC PHOSPHOLIPASE D; 1. DR Pfam; PF01839; FG-GAP; 3. DR Pfam; PF00882; Zn_dep_PLPC; 1. DR PRINTS; PR00718; PHPHLIPASED. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR PROSITE; PS51470; FG_GAP; 7. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Glycoprotein; Hydrolase; KW Lipid metabolism; Proteomics identification; Reference proteome; Repeat; KW Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:1606959" FT CHAIN 24..840 FT /note="Phosphatidylinositol-glycan-specific phospholipase FT D" FT /id="PRO_0000022047" FT REPEAT 367..428 FT /note="FG-GAP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 436..497 FT /note="FG-GAP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 499..559 FT /note="FG-GAP 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 563..623 FT /note="FG-GAP 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 633..693 FT /note="FG-GAP 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 704..770 FT /note="FG-GAP 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT REPEAT 788..840 FT /note="FG-GAP 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 271 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 292 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 307 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 321 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 501 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 568 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 591 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 604 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 659 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT VAR_SEQ 165..176 FT /note="GDVLSQFEFNFN -> TVYLHLLNFLVV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023261" FT VAR_SEQ 177..840 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023262" FT VARIANT 17 FT /note="L -> V (in dbSNP:rs2235501)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_030743" FT VARIANT 30 FT /note="V -> I (in dbSNP:rs1126617)" FT /evidence="ECO:0000269|PubMed:11072085, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_030744" FT VARIANT 275 FT /note="D -> E (in dbSNP:rs17300770)" FT /id="VAR_030745" FT VARIANT 350 FT /note="I -> V (in dbSNP:rs1062496)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_051278" FT VARIANT 396 FT /note="G -> S (in dbSNP:rs6924628)" FT /id="VAR_030746" FT VARIANT 461 FT /note="V -> M (in dbSNP:rs1062505)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_030747" FT VARIANT 694 FT /note="M -> V (in dbSNP:rs1042303)" FT /evidence="ECO:0000269|PubMed:11072085" FT /id="VAR_030748" FT VARIANT 698 FT /note="T -> I (in dbSNP:rs1772256)" FT /evidence="ECO:0000269|PubMed:11072085, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1, FT ECO:0000269|Ref.3" FT /id="VAR_030749" FT CONFLICT 531..534 FT /note="VIGS -> MLGT (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 840 AA; 92336 MW; 11369BAFEC3D6D38 CRC64; MSAFRLWPGL LIMLGSLCHR GSPCGLSTHV EIGHRALEFL QLHNGRVNYR ELLLEHQDAY QAGIVFPDCF YPSICKGGKF HDVSESTHWT PFLNASVHYI RENYPLPWEK DTEKLVAFLF GITSHMAADV SWHSLGLEQG FLRTMGAIDF HGSYSEAHSA GDFGGDVLSQ FEFNFNYLAR RWYVPVKDLL GIYEKLYGRK VITENVIVDC SHIQFLEMYG EMLAVSKLYP TYSTKSPFLV EQFQEYFLGG LDDMAFWSTN IYHLTSFMLE NGTSDCNLPE NPLFIACGGQ QNHTQGSKMQ KNDFHRNLTT SLTESVDRNI NYTERGVFFS VNSWTPDSMS FIYKALERNI RTMFIGGSQL SQKHVSSPLA SYFLSFPYAR LGWAMTSADL NQDGHGDLVV GAPGYSRPGH IHIGRVYLIY GNDLGLPPVD LDLDKEAHRI LEGFQPSGRF GSALAVLDFN VDGVPDLAVG APSVGSEQLT YKGAVYVYFG SKQGGMSSSP NITISCQDIY CNLGWTLLAA DVNGDSEPDL VIGSPFAPGG GKQKGIVAAF YSGPSLSDKE KLNVEAANWT VRGEEDFSWF GYSLHGVTVD NRTLLLVGSP TWKNASRLGH LLHIRDEKKS LGRVYGYFPP NGQSWFTISG DKAMGKLGTS LSSGHVLMNG TLKQVLLVGA PTYDDVSKVA FLTVTLHQGG ATRMYALTSD AQPLLLSTFS GDRRFSRFGG VLHLSDLDDD GLDEIIMAAP LRIADVTSGL IGGEDGRVYV YNGKETTLGD MTGKCKSWIT PCPEEKAQYV LISPEASSRF GSSLITVRSK AKNQVVIAAG RSSLGARLSG ALHVYSLGSD //