位置:首页 > 蛋白库 > PA2N2_VIPAA
PA2N2_VIPAA
ID   PA2N2_VIPAA             Reviewed;         137 AA.
AC   P34180; Q9I967;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Neutral phospholipase A2 ammodytin I2 {ECO:0000303|PubMed:1551386, ECO:0000303|PubMed:16156665};
DE            Short=AmI2 {ECO:0000250|UniProtKB:Q910A1};
DE            Short=AmdI1;
DE            Short=AtnI2 {ECO:0000303|PubMed:16156665};
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Vipera ammodytes ammodytes (Western sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=8705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-137, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=1551386; DOI=10.1111/j.1432-1033.1992.tb16728.x;
RA   Krizaj I., Liang N.-S., Pungercar J., Strukelj B., Ritonja A., Gubensek F.;
RT   "Amino acid and cDNA sequences of a neutral phospholipase A2 from the long-
RT   nosed viper (Vipera ammodytes ammodytes) venom.";
RL   Eur. J. Biochem. 204:1057-1062(1992).
RN   [2]
RP   SEQUENCE REVISION TO 132.
RA   Pungercar J.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kordis D., Gubensek F.;
RT   "Molecular evolution of phospholipase A2 multigene family in Vipera
RT   ammodytes.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   TISSUE=Venom;
RX   PubMed=16156665; DOI=10.1021/bi051024r;
RA   Petan T., Krizaj I., Gelb M.H., Pungercar J.;
RT   "Ammodytoxins, potent presynaptic neurotoxins, are also highly efficient
RT   phospholipase A2 enzymes.";
RL   Biochemistry 44:12535-12545(2005).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that has enzymatic
CC       activity but is non-toxic. Displays low binding affinity and enzymatic
CC       activity on phosphatidylserine-containing vesicles and HEK-293 plasma
CC       membranes, in contrast to ammodytoxins that have high activity on these
CC       phospholipids. PLA2 catalyzes the calcium-dependent hydrolysis of the
CC       2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:16156665}.
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:16156665};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:16156665};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1551386}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:1551386}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {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; X56878; CAA40200.2; -; mRNA.
DR   EMBL; X84018; CAA58840.1; -; Genomic_DNA.
DR   PIR; S22388; S22388.
DR   AlphaFoldDB; P34180; -.
DR   SMR; P34180; -.
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; Metal-binding; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:1551386"
FT   CHAIN           17..137
FT                   /note="Neutral phospholipase A2 ammodytin I2"
FT                   /id="PRO_0000022973"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
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                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   137 AA;  15309 MW;  BDEC100B7F524431 CRC64;
     MRTLWIVAVC LIGVEGNLYQ FGNMIFKMTK KSALLSYSNY GCYCGWGGKG KPQDATDRCC
     FVHDCCYGRV NGCDPKLSIY SYSFENGDIV CGGDDPCLRA VCECDRVAAI CFGENLNTYD
     KKYKNYPSSH CTETEQC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024