PA24F_HUMAN
ID PA24F_HUMAN Reviewed; 849 AA.
AC Q68DD2; Q6ZMC8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytosolic phospholipase A2 zeta;
DE Short=cPLA2-zeta;
DE EC=3.1.1.4 {ECO:0000269|PubMed:29158256};
DE AltName: Full=Phospholipase A2 group IVF;
GN Name=PLA2G4F;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-849 (ISOFORM 3), AND VARIANT
RP VAL-740.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP PROTEIN SEQUENCE OF 1-13; 191-215; 526-543 AND 553-587, IDENTIFICATION BY
RP MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Myocardium;
RX PubMed=29158256; DOI=10.1074/jbc.ra117.000405;
RA Moon S.H., Liu X., Cedars A.M., Yang K., Kiebish M.A., Joseph S.M.,
RA Kelley J., Jenkins C.M., Gross R.W.;
RT "Heart failure-induced activation of phospholipase iPLA2gamma generates
RT hydroxyeicosatetraenoic acids opening the mitochondrial permeability
RT transition pore.";
RL J. Biol. Chem. 293:115-129(2018).
CC -!- FUNCTION: Has calcium-dependent phospholipase and lysophospholipase
CC activities with a potential role in membrane lipid remodeling and
CC biosynthesis of lipid mediators (PubMed:29158256). Preferentially
CC hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC position of phospholipids (phospholipase A2 activity)
CC (PubMed:29158256). Selectively hydrolyzes sn-2 arachidonoyl group from
CC membrane phospholipids, providing the precursor for eicosanoid
CC biosynthesis (PubMed:29158256). In myocardial mitochondria, plays a
CC major role in arachidonate release that is metabolically channeled to
CC the formation of cardioprotective eicosanoids, epoxyeicosatrienoates
CC (EETs) (PubMed:29158256). {ECO:0000269|PubMed:29158256}.
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:29158256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:29158256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001,
CC ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
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:0000250|UniProtKB:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:29158256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:29158256};
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:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
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:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-
CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:77695, ChEBI:CHEBI:77696;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-
CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:55430, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:Q50L41};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q50L41,
CC ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+).
CC {ECO:0000250|UniProtKB:Q50L41}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q50L41}. Cell membrane
CC {ECO:0000250|UniProtKB:Q50L41}; Peripheral membrane protein
CC {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:29158256}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q68DD2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68DD2-2; Sequence=VSP_019888, VSP_019889;
CC Name=3;
CC IsoId=Q68DD2-3; Sequence=VSP_019887;
CC -!- TISSUE SPECIFICITY: Expressed in myocardium (at protein level).
CC {ECO:0000269|PubMed:29158256}.
CC -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes upon
CC calcium binding. It modulates enzyme activity by presenting the active
CC site to its substrate in response to elevations of cytosolic Ca(2+) (By
CC similarity). {ECO:0000250}.
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DR EMBL; AK172836; BAD18801.1; -; mRNA.
DR EMBL; AC036103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR749451; CAH18288.1; -; mRNA.
DR CCDS; CCDS32204.1; -. [Q68DD2-1]
DR RefSeq; NP_998765.3; NM_213600.3. [Q68DD2-1]
DR AlphaFoldDB; Q68DD2; -.
DR SMR; Q68DD2; -.
DR BioGRID; 129083; 9.
DR IntAct; Q68DD2; 10.
DR STRING; 9606.ENSP00000380442; -.
DR iPTMnet; Q68DD2; -.
DR PhosphoSitePlus; Q68DD2; -.
DR BioMuta; PLA2G4F; -.
DR DMDM; 317373489; -.
DR jPOST; Q68DD2; -.
DR MassIVE; Q68DD2; -.
DR MaxQB; Q68DD2; -.
DR PaxDb; Q68DD2; -.
DR PeptideAtlas; Q68DD2; -.
DR PRIDE; Q68DD2; -.
DR ProteomicsDB; 66075; -. [Q68DD2-1]
DR ProteomicsDB; 66076; -. [Q68DD2-2]
DR ProteomicsDB; 66077; -. [Q68DD2-3]
DR Antibodypedia; 42117; 69 antibodies from 25 providers.
DR DNASU; 255189; -.
DR Ensembl; ENST00000397272.7; ENSP00000380442.4; ENSG00000168907.13. [Q68DD2-1]
DR GeneID; 255189; -.
DR KEGG; hsa:255189; -.
DR MANE-Select; ENST00000397272.7; ENSP00000380442.4; NM_213600.4; NP_998765.3.
DR UCSC; uc001zoz.4; human. [Q68DD2-1]
DR CTD; 255189; -.
DR DisGeNET; 255189; -.
DR GeneCards; PLA2G4F; -.
DR HGNC; HGNC:27396; PLA2G4F.
DR HPA; ENSG00000168907; Tissue enriched (skin).
DR neXtProt; NX_Q68DD2; -.
DR OpenTargets; ENSG00000168907; -.
DR PharmGKB; PA142671170; -.
DR VEuPathDB; HostDB:ENSG00000168907; -.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; Q68DD2; -.
DR OMA; WPEPRIC; -.
DR PhylomeDB; Q68DD2; -.
DR TreeFam; TF325228; -.
DR PathwayCommons; Q68DD2; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR Reactome; R-HSA-1482925; Acyl chain remodelling of PG.
DR Reactome; R-HSA-1483115; Hydrolysis of LPC.
DR SignaLink; Q68DD2; -.
DR BioGRID-ORCS; 255189; 6 hits in 1066 CRISPR screens.
DR GenomeRNAi; 255189; -.
DR Pharos; Q68DD2; Tdark.
DR PRO; PR:Q68DD2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q68DD2; protein.
DR Bgee; ENSG00000168907; Expressed in skin of abdomen and 114 other tissues.
DR ExpressionAtlas; Q68DD2; baseline and differential.
DR Genevisible; Q68DD2; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:Ensembl.
DR GO; GO:0008970; F:phospholipase A1 activity; TAS:Reactome.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:Ensembl.
DR CDD; cd04036; C2_cPLA2; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR041847; C2_cPLA2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR040723; cPLA2_C2.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF18695; cPLA2_C2; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Mitochondrion; Phospholipid degradation;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1..849
FT /note="Cytosolic phospholipase A2 zeta"
FT /id="PRO_0000247027"
FT DOMAIN 27..145
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 306..849
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 680
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 352
FT /note="G -> GQV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019887"
FT VAR_SEQ 433..454
FT /note="ALSTERLQYYTQELGVRERSGH -> DVRVSPCQLPRLHSSNLDHSLW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019888"
FT VAR_SEQ 455..849
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019889"
FT VARIANT 30
FT /note="G -> V (in dbSNP:rs636604)"
FT /id="VAR_053553"
FT VARIANT 740
FT /note="M -> V (in dbSNP:rs1356410)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_027054"
FT CONFLICT 203
FT /note="R -> G (in Ref. 1; BAD18801)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> T (in Ref. 1; BAD18801)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="G -> E (in Ref. 3; CAH18288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 849 AA; 95082 MW; B2231EC3A9494598 CRC64;
MLWALWPRWL ADKMLPLLGA VLLQKREKRG PLWRHWRRET YPYYDLQVKV LRATNIRGTD
LLSKADCYVQ LWLPTASPSP AQTRIVANCS DPEWNETFHY QIHGAVKNVL ELTLYDKDIL
GSDQLSLLLF DLRSLKCGQP HKHTFPLNHQ DSQELQVEFV LEKSQVPASE VITNGVLVAH
PCLRIQGTLR GDGTAPREEY GSRQLQLAVP GAYEKPQLLP LQPPTEPGLP PTFTFHVNPV
LSSRLHVELM ELLAAVQSGP SAELEAQTSK LGEGGILLSS LPLGQEEQCS VALGEGQEVA
LSMKVEMSSG DLDLRLGFDL SDGEQEFLDR RKQVVSKALQ QVLGLSEALD SGQVPVVAVL
GSGGGTRAMS SLYGSLAGLQ ELGLLDTVTY LSGVSGSTWC ISTLYRDPAW SQVALQGPIE
RAQVHVCSSK MGALSTERLQ YYTQELGVRE RSGHSVSLID LWGLLVEYLL YQEENPAKLS
DQQEAVRQGQ NPYPIYTSVN VRTNLSGEDF AEWCEFTPYE VGFPKYGAYV PTELFGSELF
MGRLLQLQPE PRICYLQGMW GSAFATSLDE IFLKTAGSGL SFLEWYRGSV NITDDCQKPQ
LHNPSRLRTR LLTPQGPFSQ AVLDIFTSRF TSAQSFNFTR GLCLHKDYVA GREFVAWKDT
HPDAFPNQLT PMRDCLYLVD GGFAINSPFP LALLPQRAVD LILSFDYSLE APFEVLKMTE
KYCLDRGIPF PSIEVGPEDM EEARECYLFA KAEDPRSPIV LHFPLVNRTF RTHLAPGVER
QTAEEKAFGD FVINRPDTPY GMMNFTYEPQ DFYRLVALSR YNVLNNVETL KCALQLALDR
HQARERAGA
