PLAT1_HUMAN
ID PLAT1_HUMAN Reviewed; 168 AA.
AC Q9HDD0; D2KX19; Q6X7C0; Q86WS9; X6R3D1;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phospholipase A and acyltransferase 1 {ECO:0000312|HGNC:HGNC:14922};
DE EC=2.3.1.- {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847};
DE EC=3.1.1.32 {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847};
DE EC=3.1.1.4 {ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847};
DE AltName: Full=HRAS-like suppressor 1;
DE Short=HRSL1;
DE AltName: Full=Phospholipid-metabolizing enzyme A-C1 {ECO:0000303|PubMed:21880860};
GN Name=PLAAT1 {ECO:0000312|HGNC:HGNC:14922}; Synonyms=HRASLS;
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).
RA Kato S.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RA Wu N., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT "A new spermatogenesis-related gene.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), TISSUE
RP SPECIFICITY (ISOFORM 1), AND CATALYTIC ACTIVITY (ISOFORM 1).
RX PubMed=21880860; DOI=10.1194/jlr.m015081;
RA Shinohara N., Uyama T., Jin X.H., Tsuboi K., Tonai T., Houchi H., Ueda N.;
RT "Enzymological analysis of the tumor suppressor A-C1 reveals a novel group
RT of phospholipid-metabolizing enzymes.";
RL J. Lipid Res. 52:1927-1935(2011).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY (ISOFORM 1).
RX PubMed=22825852; DOI=10.1074/jbc.m112.368712;
RA Uyama T., Ikematsu N., Inoue M., Shinohara N., Jin X.H., Tsuboi K.,
RA Tonai T., Tokumura A., Ueda N.;
RT "Generation of N-acylphosphatidylethanolamine by members of the
RT phospholipase A/acyltransferase (PLA/AT) family.";
RL J. Biol. Chem. 287:31905-31919(2012).
RN [8]
RP REVIEW.
RX PubMed=26503625; DOI=10.1186/s12929-015-0210-7;
RA Mardian E.B., Bradley R.M., Duncan R.E.;
RT "The HRASLS (PLA/AT) subfamily of enzymes.";
RL J. Biomed. Sci. 22:99-99(2015).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION (ISOFORMS 1 AND 2),
RP CATALYTIC ACTIVITY (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND
RP 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=27623847; DOI=10.1194/jlr.m071290;
RA Hussain Z., Uyama T., Kawai K., Rahman I.A., Tsuboi K., Araki N., Ueda N.;
RT "Comparative analyses of isoforms of the calcium-independent
RT phosphatidylethanolamine N-acyltransferase PLAAT-1 in humans and mice.";
RL J. Lipid Res. 57:2051-2060(2016).
CC -!- FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase
CC activities (PubMed:21880860, PubMed:26503625). Shows phospholipase A1
CC (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent
CC release of fatty acids from the sn-1 or sn-2 position of
CC glycerophospholipids (PubMed:21880860, PubMed:22825852,
CC PubMed:27623847). Shows O-acyltransferase activity, catalyzing the
CC transfer of a fatty acyl group from glycerophospholipid to the hydroxyl
CC group of lysophospholipid (PubMed:21880860). Shows N-acyltransferase
CC activity, catalyzing the calcium-independent transfer of a fatty acyl
CC group at the sn-1 position of phosphatidylcholine (PC) and other
CC glycerophospholipids to the primary amine of phosphatidylethanolamine
CC (PE), forming N-acylphosphatidylethanolamine (NAPE) which serves as
CC precursor for N-acylethanolamines (NAEs) (PubMed:21880860,
CC PubMed:22825852, PubMed:27623847). {ECO:0000269|PubMed:21880860,
CC ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:27623847,
CC ECO:0000303|PubMed:26503625}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852,
CC ECO:0000269|PubMed:27623847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852,
CC ECO:0000269|PubMed:27623847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078;
CC Evidence={ECO:0000269|PubMed:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091;
CC Evidence={ECO:0000269|PubMed:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-
CC sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:74986, ChEBI:CHEBI:78097;
CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361;
CC Evidence={ECO:0000269|PubMed:21880860, ECO:0000269|PubMed:22825852};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-
CC phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999,
CC ChEBI:CHEBI:76078, ChEBI:CHEBI:77369;
CC Evidence={ECO:0000269|PubMed:21880860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365;
CC Evidence={ECO:0000269|PubMed:21880860};
CC -!- INTERACTION:
CC Q9HDD0; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-12387058, EBI-10261970;
CC Q9HDD0; O95872: GPANK1; NbExp=3; IntAct=EBI-12387058, EBI-751540;
CC Q9HDD0; O14964: HGS; NbExp=3; IntAct=EBI-12387058, EBI-740220;
CC Q9HDD0; P78424: POU6F2; NbExp=3; IntAct=EBI-12387058, EBI-12029004;
CC Q9HDD0; O43711: TLX3; NbExp=3; IntAct=EBI-12387058, EBI-3939165;
CC Q9HDD0; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12387058, EBI-741480;
CC Q9HDD0; Q15915: ZIC1; NbExp=3; IntAct=EBI-12387058, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000255}; Single-pass
CC membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:27623847}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:27623847}. Cytoplasm {ECO:0000269|PubMed:27623847}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PLAAT-1S {ECO:0000303|PubMed:27623847};
CC IsoId=Q9HDD0-1; Sequence=Displayed;
CC Name=2; Synonyms=PLAAT-1L {ECO:0000303|PubMed:27623847};
CC IsoId=Q9HDD0-2; Sequence=VSP_060190;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Abundantly expressed in testis,
CC skeletal muscle, brain, and heart. {ECO:0000269|PubMed:21880860}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Highly expressed in the testis,
CC skeletal muscle, brain, heart, and thyroid.
CC {ECO:0000269|PubMed:27623847}.
CC -!- SIMILARITY: Belongs to the H-rev107 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; AB030816; BAB08110.1; -; mRNA.
DR EMBL; AY251533; AAP20056.1; -; mRNA.
DR EMBL; AB510981; BAI63210.1; -; mRNA.
DR EMBL; AC105057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78078.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78079.1; -; Genomic_DNA.
DR EMBL; BC048095; AAH48095.1; -; mRNA.
DR CCDS; CCDS3303.2; -. [Q9HDD0-1]
DR RefSeq; NP_065119.2; NM_020386.4. [Q9HDD0-1]
DR RefSeq; XP_016862412.1; XM_017006923.1.
DR AlphaFoldDB; Q9HDD0; -.
DR SMR; Q9HDD0; -.
DR IntAct; Q9HDD0; 7.
DR STRING; 9606.ENSP00000264735; -.
DR SwissLipids; SLP:000000688; -.
DR PhosphoSitePlus; Q9HDD0; -.
DR BioMuta; HRASLS; -.
DR DMDM; 20138344; -.
DR PaxDb; Q9HDD0; -.
DR PRIDE; Q9HDD0; -.
DR Antibodypedia; 33880; 43 antibodies from 15 providers.
DR DNASU; 57110; -.
DR Ensembl; ENST00000264735.4; ENSP00000264735.4; ENSG00000127252.7. [Q9HDD0-1]
DR Ensembl; ENST00000650797.1; ENSP00000498228.1; ENSG00000127252.7. [Q9HDD0-2]
DR GeneID; 57110; -.
DR KEGG; hsa:57110; -.
DR MANE-Select; ENST00000264735.4; ENSP00000264735.4; NM_020386.5; NP_065119.3.
DR UCSC; uc003fta.5; human.
DR CTD; 57110; -.
DR DisGeNET; 57110; -.
DR GeneCards; PLAAT1; -.
DR HGNC; HGNC:14922; PLAAT1.
DR HPA; ENSG00000127252; Group enriched (skeletal muscle, testis, tongue).
DR MIM; 606487; gene.
DR neXtProt; NX_Q9HDD0; -.
DR OpenTargets; ENSG00000127252; -.
DR PharmGKB; PA29445; -.
DR VEuPathDB; HostDB:ENSG00000127252; -.
DR eggNOG; ENOG502QU0S; Eukaryota.
DR GeneTree; ENSGT00940000156634; -.
DR HOGENOM; CLU_1019273_0_0_1; -.
DR InParanoid; Q9HDD0; -.
DR OrthoDB; 1602481at2759; -.
DR PhylomeDB; Q9HDD0; -.
DR TreeFam; TF330836; -.
DR BioCyc; MetaCyc:ENSG00000127252-MON; -.
DR PathwayCommons; Q9HDD0; -.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q9HDD0; -.
DR BioGRID-ORCS; 57110; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; HRASLS; human.
DR GenomeRNAi; 57110; -.
DR Pharos; Q9HDD0; Tbio.
DR PRO; PR:Q9HDD0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HDD0; protein.
DR Bgee; ENSG00000127252; Expressed in sperm and 160 other tissues.
DR ExpressionAtlas; Q9HDD0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005641; C:nuclear envelope lumen; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070292; P:N-acylphosphatidylethanolamine metabolic process; IDA:UniProtKB.
DR GO; GO:1903008; P:organelle disassembly; ISS:UniProtKB.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR InterPro; IPR007053; LRAT_dom.
DR Pfam; PF04970; LRAT; 1.
DR PROSITE; PS51934; LRAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Nucleus; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..168
FT /note="Phospholipase A and acyltransferase 1"
FT /id="PRO_0000152481"
FT TOPO_DOM 1..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 20..135
FT /note="LRAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01283"
FT ACT_SITE 30
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT ACT_SITE 119
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P53816"
FT VAR_SEQ 1
FT /note="M -> MVRASCRLGSARTPSPARRPPGVRASQSRGGAAGTVSAWRRWCWRWP
FT WRTAPSDGWRLPPGCLPGTDGVVPRPPAARSAAARPRETPGHTQLPPGARRRPRLESEM
FT (in isoform 2)"
FT /id="VSP_060190"
FT CONFLICT 58
FT /note="S -> P (in Ref. 2; AAP20056)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="N -> D (in Ref. 6; AAH48095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18750 MW; 11844F8B5963D39B CRC64;
MAFNDCFSLN YPGNPCPGDL IEVFRPGYQH WALYLGDGYV INIAPVDGIP ASFTSAKSVF
SSKALVKMQL LKDVVGNDTY RINNKYDETY PPLPVEEIIK RSEFVIGQEV AYNLLVNNCE
HFVTLLRYGE GVSEQANRAI STVEFVTAAV GVFSFLGLFP KGQRAKYY
