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PA23_SCODE
ID   PA23_SCODE              Reviewed;         147 AA.
AC   P0DPT9;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Phospholipase A2 SSD1043 {ECO:0000303|PubMed:23148443};
DE            Short=PLA2;
DE            EC=3.1.1.4 {ECO:0000255|PROSITE-ProRule:PRU10035};
DE   Flags: Precursor;
OS   Scolopendra dehaani (Thai centipede) (Scolopendra subspinipes dehaani).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Scolopendromorpha; Scolopendridae; Scolopendra.
OX   NCBI_TaxID=2609776;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-56, SUBCELLULAR
RP   LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=23148443; DOI=10.1021/pr300881d;
RA   Liu Z.C., Zhang R., Zhao F., Chen Z.M., Liu H.W., Wang Y.J., Jiang P.,
RA   Zhang Y., Wu Y., Ding J.P., Lee W.H., Zhang Y.;
RT   "Venomic and transcriptomic analysis of centipede Scolopendra subspinipes
RT   dehaani.";
RL   J. Proteome Res. 11:6197-6212(2012).
CC   -!- FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl
CC       groups in 3-sn-phosphoglycerides. {ECO:0000250|UniProtKB:C1JAR9}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P14555};
CC       Note=Binds 1 Ca(2+) ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23148443}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:23148443}.
CC   -!- MASS SPECTROMETRY: Mass=13511.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23148443};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR   EMBL; KC145030; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DPT9; -.
DR   SMR; P0DPT9; -.
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..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..28
FT                   /evidence="ECO:0000305|PubMed:23148443"
FT                   /id="PRO_0000446683"
FT   CHAIN           29..147
FT                   /note="Phospholipase A2 SSD1043"
FT                   /evidence="ECO:0000305|PubMed:23148443"
FT                   /id="PRO_0000446684"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000250|UniProtKB:O15496"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000250|UniProtKB:O15496"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        55..71
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        70..130
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        77..123
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        86..116
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
FT   DISULFID        109..121
FT                   /evidence="ECO:0000250|UniProtKB:P14555"
SQ   SEQUENCE   147 AA;  16745 MW;  26F35C7306EAB9DC CRC64;
     MSPKFMFFSI IAVWSCAAVT EALFIQHRSL ANFFFMTLTA AKRSPQEYDG YGNYCGWGGE
     GTPVDSIDRC CQVHDNCYGT VNENECGHYI RNVKLIDYDW HMEGTEIVCD PKDDACGRAL
     CKCDKDIIDC FNENDKDYNP EYNKVIG
 
 
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