PA21_SCODE
ID PA21_SCODE Reviewed; 147 AA.
AC P0DPT7;
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 SSD387 {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, MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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:0000269|PubMed:23148443}.
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:0000269|PubMed:23148443};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=110 uM/min/mg enzyme for egg yolk {ECO:0000269|PubMed:23148443};
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=13440.8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23148443};
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. {ECO:0000305}.
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DR EMBL; KC144387; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0DPT7; -.
DR SMR; P0DPT7; -.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..28
FT /evidence="ECO:0000305|PubMed:23148443"
FT /id="PRO_0000446680"
FT CHAIN 29..147
FT /note="Phospholipase A2 SSD387"
FT /evidence="ECO:0000305|PubMed:23148443"
FT /id="PRO_0000446681"
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; 16543 MW; 9824A0D96329146F CRC64;
MSPKFLLFSI IAVWSCAAAI EALFIQPRSL ANFLSMTLTA AKRSPQEYDG YGNYCGWGGE
GTPVDSIDRC CQVHDNCYGT VNENECGHYI RNVKLIDYDW HMEGTEIVCD PKDDACGRAL
CKCDKDIIDC FNENDKDYNP EYNKVIG
