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PA2B1_AGKPC
ID   PA2B1_AGKPC             Reviewed;         123 AA.
AC   C0HKC4;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Basic phospholipase A2 APC-D49 {ECO:0000303|PubMed:28633930};
DE            Short=svPLA2 {ECO:0000250|UniProtKB:P51972};
DE            EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035};
DE   AltName: Full=ApcP3 {ECO:0000303|PubMed:28633930};
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase {ECO:0000250|UniProtKB:P51972};
OS   Agkistrodon piscivorus conanti (Florida cottonmouth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=2782195 {ECO:0000303|PubMed:28633930};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR
RP   LOCATION, MASS SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom {ECO:0000303|PubMed:28633930};
RX   PubMed=28633930; DOI=10.1016/j.toxicon.2017.06.010;
RA   Jia Y., Ermolinsky B., Garza A., Provenzano D.;
RT   "Phospholipase A2 in the venom of three cottonmouth snakes.";
RL   Toxicon 135:84-92(2017).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:28633930}.
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:28633930};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P14418};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P14418};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28633930}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:28633930}.
CC   -!- MASS SPECTROMETRY: Mass=13967.25; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:28633930};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKC4; -.
DR   SMR; C0HKC4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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   Calcium; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipoprotein; Metal-binding; Palmitate;
KW   Secreted.
FT   CHAIN           1..123
FT                   /note="Basic phospholipase A2 APC-D49"
FT                   /evidence="ECO:0000269|PubMed:28633930"
FT                   /id="PRO_0000439086"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10036"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   BINDING         29
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   BINDING         31
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   BINDING         48
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14418"
FT   LIPID           7
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   LIPID           10
FT                   /note="N6-palmitoyl lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        26..116
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        49..123
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P51972"
SQ   SEQUENCE   123 AA;  13989 MW;  C39986552D990D72 CRC64;
     NLFQFEKLIK KMTGKSGMLW YSAYGCYCGW GGQGRPKDAT DRCCFVHDCC YGKVTGCNPK
     MDIYTYSVDN GNIVCGGTNP CKKQICECDR AAAICFRDNL KTYDSKTYWK YPKKNCKEES
     EPC
 
 
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