PA2GA_RAT
ID PA2GA_RAT Reviewed; 146 AA.
AC P14423;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Phospholipase A2, membrane associated;
DE EC=3.1.1.4 {ECO:0000269|PubMed:3356705};
DE AltName: Full=GIIC sPLA2;
DE AltName: Full=Group IIA phospholipase A2;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2A;
DE Flags: Precursor;
GN Name=Pla2g2a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Platelet;
RX PubMed=2606907; DOI=10.1093/oxfordjournals.jbchem.a122890;
RA Komada M., Kudo I., Mizushima H., Kitamura N., Inoue K.;
RT "Structure of cDNA coding for rat platelet phospholipase A2.";
RL J. Biochem. 106:545-547(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=2346480; DOI=10.1016/0006-291x(90)91137-h;
RA Komada M., Kudo I., Inoue K.;
RT "Structure of gene coding for rat group II phospholipase A2.";
RL Biochem. Biophys. Res. Commun. 168:1059-1065(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2764915; DOI=10.1016/0006-291x(89)90777-8;
RA Ishizaki J., Ohara O., Nakamura E., Tamaki M., Ono T., Kanda A.,
RA Yoshida N., Teraoka H., Tojo H., Okamoto M.;
RT "cDNA cloning and sequence determination of rat membrane-associated
RT phospholipase A2.";
RL Biochem. Biophys. Res. Commun. 162:1030-1036(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2400792; DOI=10.1016/0167-4781(90)90127-n;
RA Kusunoki C., Satoh S., Kobayashi M., Niwa M.;
RT "Structure of genomic DNA for rat platelet phospholipase A2.";
RL Biochim. Biophys. Acta 1087:95-97(1990).
RN [5]
RP PROTEIN SEQUENCE OF 22-146.
RC STRAIN=Wistar; TISSUE=Platelet;
RX PubMed=3235451; DOI=10.1093/oxfordjournals.jbchem.a122547;
RA Hayakawa M., Kudo I., Tomita M., Nojima S., Inoue K.;
RT "The primary structure of rat platelet phospholipase A2.";
RL J. Biochem. 104:767-772(1988).
RN [6]
RP PROTEIN SEQUENCE OF 22-57, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Spleen;
RX PubMed=3356705; DOI=10.1016/s0021-9258(18)60626-x;
RA Ono T., Tojo H., Kuramitsu S., Kagamiyama H., Okamoto M.;
RT "Purification and characterization of a membrane-associated phospholipase
RT A2 from rat spleen. Its comparison with a cytosolic phospholipase A2 S-1.";
RL J. Biol. Chem. 263:5732-5738(1988).
RN [7]
RP PROTEIN SEQUENCE OF 22-46.
RC TISSUE=Platelet;
RX PubMed=3654593; DOI=10.1093/oxfordjournals.jbchem.a121996;
RA Hayakawa M., Horigome K., Kudo I., Tomita M., Nojima S., Inoue K.;
RT "Amino acid composition and NH2-terminal amino acid sequence of rat
RT platelet secretory phospholipase A2.";
RL J. Biochem. 101:1311-1314(1987).
RN [8]
RP PROTEIN SEQUENCE OF 22-45, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=2722857; DOI=10.1016/s0021-9258(18)81760-4;
RA Aarsman A.J., de Jong J.G.N., Arnoldussen E., Neys F.W.,
RA van Wassenaar P.D., van den Bosch H.;
RT "Immunoaffinity purification, partial sequence, and subcellular
RT localization of rat liver phospholipase A2.";
RL J. Biol. Chem. 264:10008-10014(1989).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids with implications in host
CC antimicrobial defense, inflammatory response and tissue regeneration
CC (By similarity). Hydrolyzes the ester bond of the fatty acyl group
CC attached at sn-2 position of phospholipids (phospholipase A2 activity)
CC with preference for phosphatidylethanolamines and phosphatidylglycerols
CC over phosphatidylcholines (PubMed:3356705). Contributes to lipid
CC remodeling of cellular membranes and generation of lipid mediators
CC involved in pathogen clearance. Displays bactericidal activity against
CC Gram-positive bacteria by directly hydrolyzing phospholipids of the
CC bacterial membrane. Upon sterile inflammation, targets membrane
CC phospholipids of extracellular mitochondria released from activated
CC platelets, generating free unsaturated fatty acids such as arachidonate
CC that is used by neighboring leukocytes to synthesize inflammatory
CC eicosanoids such as leukotrienes. Simultaneously, by compromising
CC mitochondrial membrane integrity, promotes the release in circulation
CC of potent damage-associated molecular pattern molecules that activate
CC the innate immune response (By similarity). Plays a stem cell regulator
CC role in the intestinal crypt. Within intracellular compartment mediates
CC Paneth cell differentiation and its stem cell supporting functions by
CC inhibiting Wnt signaling pathway in intestinal stem cell (ICS).
CC Secreted in the intestinal lumen upon inflammation, acts in an
CC autocrine way and promotes prostaglandin E2 synthesis that stimulates
CC Wnt signaling pathway in ICS cells and tissue regeneration (By
CC similarity). May play a role in the biosynthesis of N-acyl
CC ethanolamines that regulate energy metabolism and inflammation.
CC Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl
CC lysophosphatidylethanolamines, which are further cleaved by a
CC lysophospholipase D to release N-acyl ethanolamines. Independent of its
CC catalytic activity, acts as a ligand for integrins. Binds to and
CC activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to
CC a site (site 2) which is distinct from the classical ligand-binding
CC site (site 1) and induces integrin conformational changes and enhanced
CC ligand binding to site 1. Induces cell proliferation in an integrin-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:P14555,
CC ECO:0000250|UniProtKB:P31482, ECO:0000269|PubMed:3356705}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC Evidence={ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC Evidence={ECO:0000305|PubMed:3356705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000305|PubMed:3356705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = (9Z)-octadecenoate + H(+) + N-hexadecanoyl-1-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:45424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:78097, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45425;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O
CC = 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:45472, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72829,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-
CC glycerol + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phospho-glycerol + H(+); Xref=Rhea:RHEA:44524, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:84472,
CC ChEBI:CHEBI:84475; Evidence={ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:P14555};
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:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-
CC ProRule:PRU10036, ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:3356705};
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:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:3356705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:3356705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:3356705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = (4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:41231, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:74963, ChEBI:CHEBI:77016;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000250|UniProtKB:P14555};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:3356705};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14555};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9.5. {ECO:0000269|PubMed:3356705};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2722857}. Cell
CC membrane {ECO:0000269|PubMed:2722857}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14555}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P14555}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P14555}.
CC -!- MISCELLANEOUS: Group II phospholipase A2 is found in many cells and
CC also extracellularly. The membrane-bound and secreted forms are
CC identical and are encoded by a single gene.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; D00523; BAA00410.1; -; mRNA.
DR EMBL; M37127; AAA41223.1; -; Genomic_DNA.
DR EMBL; M25148; AAA41920.1; -; mRNA.
DR EMBL; X51529; CAA35909.1; -; Genomic_DNA.
DR PIR; A33394; A33394.
DR PIR; A35493; A35493.
DR PIR; JU0283; JU0283.
DR PIR; JX0052; JX0052.
DR RefSeq; NP_113786.3; NM_031598.3.
DR RefSeq; XP_006239208.1; XM_006239146.2.
DR AlphaFoldDB; P14423; -.
DR SMR; P14423; -.
DR CORUM; P14423; -.
DR STRING; 10116.ENSRNOP00000022827; -.
DR BindingDB; P14423; -.
DR ChEMBL; CHEMBL3686; -.
DR PaxDb; P14423; -.
DR Ensembl; ENSRNOT00000022827; ENSRNOP00000022827; ENSRNOG00000016945.
DR GeneID; 29692; -.
DR KEGG; rno:29692; -.
DR UCSC; RGD:620857; rat.
DR CTD; 5320; -.
DR RGD; 620857; Pla2g2a.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000155096; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; P14423; -.
DR OMA; CQCDKAA; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; P14423; -.
DR TreeFam; TF319283; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR Reactome; R-RNO-1482922; Acyl chain remodelling of PI.
DR Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR Reactome; R-RNO-6803157; Antimicrobial peptides.
DR PRO; PR:P14423; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016945; Expressed in jejunum and 18 other tissues.
DR Genevisible; P14423; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; TAS:RGD.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:1902563; P:regulation of neutrophil activation; ISS:UniProtKB.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Calcium; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Hydrolase;
KW Inflammatory response; Lipid degradation; Lipid metabolism; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2722857,
FT ECO:0000269|PubMed:3235451, ECO:0000269|PubMed:3356705,
FT ECO:0000269|PubMed:3654593"
FT CHAIN 22..146
FT /note="Phospholipase A2, membrane associated"
FT /id="PRO_0000022752"
FT ACT_SITE 68
FT /evidence="ECO:0000250"
FT ACT_SITE 113
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT SITE 122
FT /note="Important for integrin binding"
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 47..139
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 49..65
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 64..119
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 70..146
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 71..112
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 80..105
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT DISULFID 98..110
FT /evidence="ECO:0000250|UniProtKB:P14555"
FT VARIANT 135
FT /note="P -> L"
FT CONFLICT 22
FT /note="S -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="W -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="D -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="R -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="L -> V (in Ref. 3; AAA41920)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="A -> S (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16294 MW; 60DDC9E79BF109F7 CRC64;
MKVLLLLAVV IMAFGSIQVQ GSLLEFGQMI LFKTGKRADV SYGFYGCHCG VGGRGSPKDA
TDWCCVTHDC CYNRLEKRGC GTKFLTYKFS YRGGQISCST NQDSCRKQLC QCDKAAAECF
ARNKKSYSLK YQFYPNKFCK GKTPSC
