PLA1A_HUMAN
ID PLA1A_HUMAN Reviewed; 456 AA.
AC Q53H76; B2R8V2; B4DXA2; O95991; Q86WX6; Q9UPD2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Phospholipase A1 member A {ECO:0000305};
DE EC=3.1.1.111 {ECO:0000269|PubMed:10196188};
DE AltName: Full=Phosphatidylserine-specific phospholipase A1;
DE Short=PS-PLA1;
DE Flags: Precursor;
GN Name=PLA1A {ECO:0000312|HGNC:HGNC:17661}; Synonyms=NMD, PSPLA1;
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 TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=9074642; DOI=10.1016/s0014-5793(97)00098-7;
RA van Groningen J.J.M., Egmond M.R., Bloemers H.P.J., Swart G.W.M.;
RT "nmd, a novel gene differentially expressed in human melanoma cell lines,
RT encodes a new atypical member of the enzyme family of lipases.";
RL FEBS Lett. 404:82-86(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND CATALYTIC
RP ACTIVITY (ISOFORMS 1 AND 2).
RX PubMed=10196188; DOI=10.1074/jbc.274.16.11053;
RA Nagai Y., Aoki J., Sato T., Amano K., Matsuda Y., Arai H., Inoue K.;
RT "An alternative splicing form of phosphatidylserine-specific phospholipase
RT A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity
RT in humans.";
RL J. Biol. Chem. 274:11053-11059(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Testis;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 [8]
RP VARIANT HIS-110.
RX PubMed=12436198; DOI=10.1007/s100380200093;
RA Wang J., Wen X.-Y., Stewart A.K., Hegele R.A.;
RT "Polymorphisms in the gene encoding phosphatidylserine-specific
RT phospholipase A1 (PSPLA1).";
RL J. Hum. Genet. 47:611-613(2002).
CC -!- FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the
CC sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-
CC acyl-2-lysophosphatidylserines (lysophospholipase activity) in the
CC pathway of phosphatidylserines acyl chain remodeling (PubMed:10196188).
CC Cleaves phosphatidylserines exposed on the outer leaflet of the plasma
CC membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines,
CC which in turn enhance mast cell activation and histamine production (By
CC similarity). Has no activity toward other glycerophospholipids
CC including phosphatidylcholines, phosphatidylethanolamines, phosphatidic
CC acids or phosphatidylinositols, or glycerolipids such as triolein (By
CC similarity). {ECO:0000250|UniProtKB:P97535,
CC ECO:0000269|PubMed:10196188}.
CC -!- FUNCTION: [Isoform 2]: Hydrolyzes lyso-PS but not PS.
CC {ECO:0000269|PubMed:10196188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H2O = a 2-acyl-
CC sn-glycero-3-phospho-L-serine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:42212, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:57262, ChEBI:CHEBI:65214;
CC EC=3.1.1.111; Evidence={ECO:0000269|PubMed:10196188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42213;
CC Evidence={ECO:0000305|PubMed:10196188};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + H(+); Xref=Rhea:RHEA:40491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74905,
CC ChEBI:CHEBI:77342; Evidence={ECO:0000269|PubMed:10196188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40492;
CC Evidence={ECO:0000305|PubMed:10196188};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-L-serine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phospho-L-serine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41187, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75032, ChEBI:CHEBI:77830;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41188;
CC Evidence={ECO:0000250|UniProtKB:P97535};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + H2O = a fatty acid +
CC H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:32979,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:64379, ChEBI:CHEBI:64765; EC=3.1.1.111;
CC Evidence={ECO:0000269|PubMed:10196188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32980;
CC Evidence={ECO:0000305|PubMed:10196188};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:10196188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000305|PubMed:10196188};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:10196188};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000305|PubMed:10196188};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P97535}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q53H76-1; Sequence=Displayed;
CC Name=2; Synonyms=DeltaC;
CC IsoId=Q53H76-2; Sequence=VSP_022508, VSP_022509;
CC Name=3;
CC IsoId=Q53H76-3; Sequence=VSP_022507;
CC Name=4;
CC IsoId=Q53H76-4; Sequence=VSP_044944;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in placenta, prostate
CC and liver. Weakly or not expressed in skin, leukocytes, platelets,
CC colon, spleen, lung, muscle and kidney. {ECO:0000269|PubMed:9074642}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; U37591; AAC99994.1; -; mRNA.
DR EMBL; AF035268; AAC98921.1; -; mRNA.
DR EMBL; AF035269; AAC98922.1; -; mRNA.
DR EMBL; AK301880; BAG63314.1; -; mRNA.
DR EMBL; AK313519; BAG36299.1; -; mRNA.
DR EMBL; AK222705; BAD96425.1; -; mRNA.
DR EMBL; AC073352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79557.1; -; Genomic_DNA.
DR EMBL; BC047703; AAH47703.1; -; mRNA.
DR CCDS; CCDS2991.1; -. [Q53H76-1]
DR CCDS; CCDS56268.1; -. [Q53H76-3]
DR CCDS; CCDS56269.1; -. [Q53H76-4]
DR RefSeq; NP_001193889.1; NM_001206960.1. [Q53H76-3]
DR RefSeq; NP_001193890.1; NM_001206961.1. [Q53H76-4]
DR RefSeq; NP_056984.1; NM_015900.3. [Q53H76-1]
DR RefSeq; XP_016862061.1; XM_017006572.1. [Q53H76-4]
DR AlphaFoldDB; Q53H76; -.
DR SMR; Q53H76; -.
DR BioGRID; 119500; 16.
DR IntAct; Q53H76; 2.
DR STRING; 9606.ENSP00000273371; -.
DR ESTHER; human-PLA1A; Phospholipase.
DR GlyGen; Q53H76; 2 sites.
DR iPTMnet; Q53H76; -.
DR PhosphoSitePlus; Q53H76; -.
DR BioMuta; PLA1A; -.
DR DMDM; 124015212; -.
DR MassIVE; Q53H76; -.
DR PaxDb; Q53H76; -.
DR PeptideAtlas; Q53H76; -.
DR PRIDE; Q53H76; -.
DR ProteomicsDB; 5421; -.
DR ProteomicsDB; 62497; -. [Q53H76-1]
DR ProteomicsDB; 62498; -. [Q53H76-2]
DR ProteomicsDB; 62499; -. [Q53H76-3]
DR Antibodypedia; 32751; 234 antibodies from 28 providers.
DR DNASU; 51365; -.
DR Ensembl; ENST00000273371.9; ENSP00000273371.4; ENSG00000144837.9. [Q53H76-1]
DR Ensembl; ENST00000488919.5; ENSP00000420625.1; ENSG00000144837.9. [Q53H76-4]
DR Ensembl; ENST00000495992.5; ENSP00000417326.1; ENSG00000144837.9. [Q53H76-3]
DR GeneID; 51365; -.
DR KEGG; hsa:51365; -.
DR MANE-Select; ENST00000273371.9; ENSP00000273371.4; NM_015900.4; NP_056984.1.
DR UCSC; uc003ecu.4; human. [Q53H76-1]
DR CTD; 51365; -.
DR DisGeNET; 51365; -.
DR GeneCards; PLA1A; -.
DR HGNC; HGNC:17661; PLA1A.
DR HPA; ENSG00000144837; Tissue enhanced (epididymis, parathyroid gland, seminal vesicle).
DR MIM; 607460; gene.
DR neXtProt; NX_Q53H76; -.
DR OpenTargets; ENSG00000144837; -.
DR PharmGKB; PA134955851; -.
DR VEuPathDB; HostDB:ENSG00000144837; -.
DR eggNOG; ENOG502QQQP; Eukaryota.
DR GeneTree; ENSGT00940000159279; -.
DR HOGENOM; CLU_985272_0_0_1; -.
DR InParanoid; Q53H76; -.
DR OMA; HTDADNF; -.
DR OrthoDB; 534956at2759; -.
DR PhylomeDB; Q53H76; -.
DR TreeFam; TF324997; -.
DR BioCyc; MetaCyc:ENSG00000144837-MON; -.
DR BRENDA; 3.1.1.111; 2681.
DR BRENDA; 3.1.1.32; 2681.
DR PathwayCommons; Q53H76; -.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR SignaLink; Q53H76; -.
DR BioGRID-ORCS; 51365; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; PLA1A; human.
DR GenomeRNAi; 51365; -.
DR Pharos; Q53H76; Tbio.
DR PRO; PR:Q53H76; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q53H76; protein.
DR Bgee; ENSG00000144837; Expressed in corpus epididymis and 132 other tissues.
DR ExpressionAtlas; Q53H76; baseline and differential.
DR Genevisible; Q53H76; HS.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; TAS:Reactome.
DR GO; GO:0008970; F:phospholipase A1 activity; TAS:ProtInc.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; TAS:ProtInc.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00821; TAGLIPASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..456
FT /note="Phospholipase A1 member A"
FT /id="PRO_0000273330"
FT REGION 374..456
FT /note="Involved in the recognition of diacyl-phospholipids"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 260
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..258
FT /evidence="ECO:0000250"
FT DISULFID 282..293
FT /evidence="ECO:0000250"
FT DISULFID 296..304
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..173
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044944"
FT VAR_SEQ 136..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022507"
FT VAR_SEQ 374..376
FT /note="IPK -> MYT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10196188"
FT /id="VSP_022508"
FT VAR_SEQ 377..456
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10196188"
FT /id="VSP_022509"
FT VARIANT 23
FT /note="S -> I (in dbSNP:rs1128293)"
FT /id="VAR_030126"
FT VARIANT 110
FT /note="R -> H (in dbSNP:rs61733987)"
FT /evidence="ECO:0000269|PubMed:12436198"
FT /id="VAR_030127"
FT VARIANT 284
FT /note="S -> N (in dbSNP:rs2692622)"
FT /id="VAR_030128"
FT CONFLICT 213
FT /note="V -> T (in Ref. 4; BAD96425)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49715 MW; CF09D725FD75820B CRC64;
MPPGPWESCF WVGGLILWLS VGSSGDAPPT PQPKCADFQS ANLFEGTDLK VQFLLFVPSN
PSCGQLVEGS SDLQNSGFNA TLGTKLIIHG FRVLGTKPSW IDTFIRTLLR ATNANVIAVD
WIYGSTGVYF SAVKNVIKLS LEISLFLNKL LVLGVSESSI HIIGVSLGAH VGGMVGQLFG
GQLGQITGLD PAGPEYTRAS VEERLDAGDA LFVEAIHTDT DNLGIRIPVG HVDYFVNGGQ
DQPGCPTFFY AGYSYLICDH MRAVHLYISA LENSCPLMAF PCASYKAFLA GRCLDCFNPF
LLSCPRIGLV EQGGVKIEPL PKEVKVYLLT TSSAPYCMHH SLVEFHLKEL RNKDTNIEVT
FLSSNITSSS KITIPKQQRY GKGIIAHATP QCQINQVKFK FQSSNRVWKK DRTTIIGKFC
TALLPVNDRE KMVCLPEPVN LQASVTVSCD LKIACV
