PA2GE_MOUSE
ID PA2GE_MOUSE Reviewed; 142 AA.
AC Q9QUL3;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Group IIE secretory phospholipase A2;
DE Short=GIIE sPLA2;
DE Short=sPLA2-IIE;
DE EC=3.1.1.4 {ECO:0000269|PubMed:10531313};
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase 2E;
DE Flags: Precursor;
GN Name=Pla2g2e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10531313; DOI=10.1074/jbc.274.44.31195;
RA Valentin E., Ghomashchi F., Gelb M.H., Lazdunski M., Lambeau G.;
RT "On the diversity of secreted phospholipases A2. Cloning, tissue
RT distribution, and functional expression of two novel mouse group II
RT enzymes.";
RL J. Biol. Chem. 274:31195-31202(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP LIPOPOLYSACCHARIDE.
RC STRAIN=BALB/cJ;
RX PubMed=10681567; DOI=10.1074/jbc.275.8.5785;
RA Suzuki N., Ishizaki J., Yokota Y., Higashino K., Ono T., Ikeda M.,
RA Fujii N., Kawamoto K., Hanasaki K.;
RT "Structures, enzymatic properties, and expression of novel human and mouse
RT secretory phospholipase A(2)s.";
RL J. Biol. Chem. 275:5785-5793(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY
RP LIPOPOLYSACCHARIDE, AND SUBCELLULAR LOCATION.
RX PubMed=11922621; DOI=10.1006/bbrc.2002.6716;
RA Murakami M., Yoshihara K., Shimbara S., Lambeau G., Singer A., Gelb M.H.,
RA Sawada M., Inagaki N., Nagai H., Kudo I.;
RT "Arachidonate release and eicosanoid generation by group IIE phospholipase
RT A(2).";
RL Biochem. Biophys. Res. Commun. 292:689-696(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP HIGH-FAT DIET.
RX PubMed=24910243; DOI=10.1016/j.cmet.2014.05.002;
RA Sato H., Taketomi Y., Ushida A., Isogai Y., Kojima T., Hirabayashi T.,
RA Miki Y., Yamamoto K., Nishito Y., Kobayashi T., Ikeda K., Taguchi R.,
RA Hara S., Ida S., Miyamoto Y., Watanabe M., Baba H., Miyata K., Oike Y.,
RA Gelb M.H., Murakami M.;
RT "The adipocyte-inducible secreted phospholipases PLA2G5 and PLA2G2E play
RT distinct roles in obesity.";
RL Cell Metab. 20:119-132(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=27226633; DOI=10.1074/jbc.m116.734657;
RA Yamamoto K., Miki Y., Sato H., Nishito Y., Gelb M.H., Taketomi Y.,
RA Murakami M.;
RT "Expression and Function of Group IIE Phospholipase A2 in Mouse Skin.";
RL J. Biol. Chem. 291:15602-15613(2016).
CC -!- FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily
CC targets extracellular phospholipids (PubMed:11922621, PubMed:10531313).
CC Hydrolyzes the ester bond of the fatty acyl group attached at sn-2
CC position of phospholipids (phospholipase A2 activity), releasing
CC various unsaturated fatty acids including oleoate, linoleoate,
CC arachidonate, docosahexaenoate and lysophosphatidylethanolamines in
CC preference to lysophosphatidylcholines (By similarity). In response to
CC high-fat diet, hydrolyzes minor lipoprotein phospholipids including
CC phosphatidylserines, phosphatidylinositols and phosphatidylglycerols,
CC altering lipoprotein composition and fat storage in adipose tissue and
CC liver (PubMed:24910243). May act in an autocrine and paracrine manner
CC (By similarity). Contributes to lipid remodeling of cellular membranes
CC and generation of lipid mediators involved in pathogen clearance.
CC Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and
CC phosphatidylethanolamines, which are major components of membrane
CC phospholipids in bacteria (By similarity). Acts as a hair follicle
CC phospholipase A2. Selectively releases lysophosphatidylethanolamines
CC (LPE) and various unsaturated fatty acids in skin to regulate hair
CC follicle homeostasis (PubMed:27226633). May regulate the inflammatory
CC response by releasing arachidonate, a precursor of prostaglandins and
CC leukotrienes. Upon allergen exposure, may participate in allergic
CC inflammatory response by enhancing leukotriene C4 synthesis and
CC degranulation in mast cells (PubMed:11922621).
CC {ECO:0000250|UniProtKB:Q9NZK7, ECO:0000269|PubMed:10531313,
CC ECO:0000269|PubMed:11922621, ECO:0000269|PubMed:24910243,
CC ECO:0000269|PubMed:27226633}.
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:0000250|UniProtKB:Q9NZK7};
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:0000250|UniProtKB:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
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:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
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:11922621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:11922621};
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:0000269|PubMed:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45473;
CC Evidence={ECO:0000305|PubMed:10531313};
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:0000250|UniProtKB:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44525;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
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,
CC ECO:0000269|PubMed:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:10531313};
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:10531313};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:10531313};
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:0000250|UniProtKB:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
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:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
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:Q9NZK7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41232;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9NZK7};
CC Note=Binds 2 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9NZK7};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11922621}. Cytoplasm
CC {ECO:0000269|PubMed:11922621}. Note=Through binding to heparan sulfate
CC proteoglycan, may be localized to cytoplasmic compartments enriched in
CC anionic phospholipids. {ECO:0000250|UniProtKB:Q9NZK7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skin and uterus, and at lower
CC levels in various other tissues (PubMed:27226633, PubMed:10531313,
CC PubMed:10681567, PubMed:11922621). Expressed in hair follicles,
CC specifically localized in companion cells of the outer root sheath and
CC cuticular cells of the inner root sheath in hair follicles during
CC anagen (PubMed:27226633). Expressed in white and brown adipose tisue
CC (PubMed:24910243). {ECO:0000269|PubMed:10531313,
CC ECO:0000269|PubMed:10681567, ECO:0000269|PubMed:11922621,
CC ECO:0000269|PubMed:24910243, ECO:0000269|PubMed:27226633}.
CC -!- DEVELOPMENTAL STAGE: Expressed abundantly in hair follicles during the
CC anagen phase. Low expression is observed before birth, then follows
CC hair cycle progression: up-regulated markedly during P5-P15 (anagen
CC phase), declining to nearly the basal level during P20-P25 (catagen and
CC telogen) and then increasing again at P30 (next anagen).
CC {ECO:0000269|PubMed:27226633}.
CC -!- INDUCTION: Up-regulated in thymus, small intestine, brain, heart,
CC testis, kidney and lung upon endotoxin challenge (PubMed:10681567,
CC PubMed:11922621). Detected in alveolar macrophage-like cells upon
CC endotoxin challenge (PubMed:10681567). Up-regulated in white and brown
CC adipocytes upon high-fat diet (PubMed:24910243). Up-regulated in ear
CC epidermis in response to topical dermatitis agent 2,4-dinitrobenzene
CC (DNFB) (PubMed:11922621). {ECO:0000269|PubMed:10681567,
CC ECO:0000269|PubMed:11922621, ECO:0000269|PubMed:24910243}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show abnormal hair follicle
CC ultrastructure characterized by defects in the companion layer, the
CC inner root sheath (IRS) and hair shaft. Mutant IRS cells have large
CC cytoplasmic cysts and pyknotic nuclei and are devoid of keratohyalin
CC granules, whereas the cuticle is abnormally dissociated from the hair
CC cortex and medulla, indicative of impaired hair follicle development
CC (PubMed:27226633). Mutant mice are protected from obesity and
CC hyperlipidemia in response to high-fat diet (PubMed:24910243).
CC {ECO:0000269|PubMed:24910243, ECO:0000269|PubMed:27226633}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; AF166098; AAF04499.1; -; mRNA.
DR EMBL; AF112984; AAF22290.1; -; mRNA.
DR EMBL; BC027524; AAH27524.1; -; mRNA.
DR CCDS; CCDS18835.1; -.
DR RefSeq; NP_036174.1; NM_012044.2.
DR AlphaFoldDB; Q9QUL3; -.
DR SMR; Q9QUL3; -.
DR BioGRID; 205090; 2.
DR STRING; 10090.ENSMUSP00000030531; -.
DR BindingDB; Q9QUL3; -.
DR ChEMBL; CHEMBL4201; -.
DR PhosphoSitePlus; Q9QUL3; -.
DR PaxDb; Q9QUL3; -.
DR PRIDE; Q9QUL3; -.
DR Antibodypedia; 29744; 35 antibodies from 12 providers.
DR DNASU; 26970; -.
DR Ensembl; ENSMUST00000030531; ENSMUSP00000030531; ENSMUSG00000028751.
DR Ensembl; ENSMUST00000105804; ENSMUSP00000101430; ENSMUSG00000028751.
DR GeneID; 26970; -.
DR KEGG; mmu:26970; -.
DR UCSC; uc008vll.1; mouse.
DR CTD; 30814; -.
DR MGI; MGI:1349660; Pla2g2e.
DR VEuPathDB; HostDB:ENSMUSG00000028751; -.
DR eggNOG; KOG4087; Eukaryota.
DR GeneTree; ENSGT00940000161504; -.
DR HOGENOM; CLU_090683_3_0_1; -.
DR InParanoid; Q9QUL3; -.
DR OMA; IGGSHWP; -.
DR OrthoDB; 1422829at2759; -.
DR PhylomeDB; Q9QUL3; -.
DR TreeFam; TF319283; -.
DR BRENDA; 3.1.1.4; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 26970; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9QUL3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QUL3; protein.
DR Bgee; ENSMUSG00000028751; Expressed in lip and 35 other tissues.
DR ExpressionAtlas; Q9QUL3; baseline and differential.
DR Genevisible; Q9QUL3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:MGI.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
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; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Disulfide bond; Hydrolase; Inflammatory response;
KW Lipid metabolism; Metal-binding; Phospholipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..142
FT /note="Group IIE secretory phospholipase A2"
FT /id="PRO_0000022758"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT ACT_SITE 109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 44..135
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 46..62
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 61..115
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 67..142
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 68..108
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 77..101
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
FT DISULFID 95..106
FT /evidence="ECO:0000250|UniProtKB:Q9NZK7"
SQ SEQUENCE 142 AA; 15943 MW; 8B0E3CC710A1F946 CRC64;
MKPPIALACL CLLVPLAGGN LVQFGVMIER MTGKPALQYN DYGCYCGVGG SHWPVDETDW
CCHAHDCCYG RLEKLGCDPK LEKYLFSITR DNIFCAGRTA CQRHTCECDK RAALCFRHNL
NTYNRKYAHY PNKLCTGPTP PC
