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PA2A2_CERCE
ID   PA2A2_CERCE             Reviewed;         136 AA.
AC   P0CAS0; C3UWD0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Acidic phospholipase A2 CC-PLA2-2;
DE            Short=svPLA2;
DE            EC=3.1.1.4;
DE   AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Flags: Precursor;
OS   Cerastes cerastes (Horned desert viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX   NCBI_TaxID=8697;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=20142800; DOI=10.1038/labinvest.2009.137;
RA   Kessentini-Zouari R., Jebali J., Taboubi S., Srairi-Abid N., Morjen M.,
RA   Kallech-Ziri O., Bezzine S., Marvaldi J., El Ayeb M., Marrakchi N.,
RA   Luis J.;
RT   "CC-PLA2-1 and CC-PLA2-2, two Cerastes cerastes venom-derived
RT   phospholipases A2, inhibit angiogenesis both in vitro and in vivo.";
RL   Lab. Invest. 90:510-519(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-66, FUNCTION, COFACTOR, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RA   Zouari-Kessentini R., Luis J., Karray A., Kallech-Ziri O., Srairi-Abid N.,
RA   Bazaa A., Loret E., Bezzine S., El Ayeb M., Marrakchi N.;
RT   "Two purified and characterized phospholipases A2 from Cerastes cerastes
RT   venom, that inhibit cancerous cell adhesion and migration.";
RL   Toxicon 53:444-453(2009).
CC   -!- FUNCTION: Snake venom phospholipase A2 that inhibits blood coagulation
CC       and platelet aggregation induced by ADP and arachidonic acid. Inhibits
CC       tumor cell adhesion and migration in a dose-dependent manner. Abolishes
CC       the attachment of human brain microvascular endothelial cells (HBMEC)
CC       to fibrinogen (IC(50)=0.2 uM) and dramatically reduces it adhesion to
CC       fibronectin (IC(50)=0.3 uM), whereas no effect is observed on type I
CC       collagen, vitronectin or laminin 1. Also blocks the cell migration
CC       toward fibronectin and fibrinogen. These effects are not dependent of
CC       the catalytic activity, but are mediated by alpha-5/beta-1
CC       (ITGA5/ITGB1) and alpha-v-containing (ITGAV) integrins. Also shows
CC       anti-angiogenic activity in chicken chorioallantoix membrane assay. Has
CC       a relatively high enzymatic activity. PLA2 catalyzes the calcium-
CC       dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
CC       {ECO:0000269|PubMed:20142800, ECO:0000269|Ref.2}.
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};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.2};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000269|Ref.2};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305|Ref.2}.
CC   -!- PTM: Glycosylated (2.5%).
CC   -!- MASS SPECTROMETRY: Mass=13705.63; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.2};
CC   -!- MISCELLANEOUS: Does not show cytotoxic activity on human fibrosarcoma
CC       and melanoma cell lines. {ECO:0000305|PubMed:20142800}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; FJ754187; ACO92623.1; -; mRNA.
DR   AlphaFoldDB; P0CAS0; -.
DR   SMR; P0CAS0; -.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
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; 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   Angiogenesis; Blood coagulation cascade inhibiting toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Metal-binding; Platelet aggregation inhibiting toxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           17..136
FT                   /note="Acidic phospholipase A2 CC-PLA2-2"
FT                   /id="PRO_0000376917"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        103
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..129
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15103 MW;  EA2A65C594F4DBB0 CRC64;
     MRTLWIVAVW LMGVEGNLFQ FGKMIKHKTG KSALLSYSGN PCYCGWGGQG PPQDATDHCC
     FVHDCCYGEE NACYPKTAFT LKFENQIIIC DEDPCNYAVC MCDRVAAICG GENVATSDAK
     YLFYRSMGCE EESVQC
 
 
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