ID   PA2H_GLOHA              Reviewed;         122 AA.
AC   O42188;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Basic phospholipase A2 homolog;
DE            Short=svPLA2 homolog;
OS   Gloydius halys (Chinese water mocassin) (Agkistrodon halys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=8714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=9690782; DOI=10.1016/s0041-0101(98)00013-0;
RA   Pan H., Liu X.-L., Ou-Yang L.-L., Yang G.-Z., Zhou Y.-C., Li Z.-P.,
RA   Wu X.-F.;
RT   "Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas
RT   venom, and its expression in E. coli.";
RL   Toxicon 36:1155-1163(1998).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9690782}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:9690782}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       N49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding sites is
CC       lost (Asp->Asn in position 48, which corresponds to 'Asn-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   EMBL; AF015243; AAB71845.1; -; mRNA.
DR   AlphaFoldDB; O42188; -.
DR   SMR; O42188; -.
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:InterPro.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond; Secreted.
FT   CHAIN           1..122
FT                   /note="Basic phospholipase A2 homolog"
FT                   /evidence="ECO:0000303|PubMed:9690782"
FT                   /id="PRO_0000161604"
FT   REGION          105..117
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        26..115
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        28..44
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        43..95
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        49..122
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        50..88
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        57..81
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        75..86
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   122 AA;  13876 MW;  877B271DE312EF6A CRC64;
     NLIQFKKMIK KMTGKEPVVS YAFYGCYCGS GGRGKPKDAT DRCCFVHNCC YEKVTGCDPK
     WDDYTYSWKN GTIVCGGDDP CKKEVCECDK AAAICFRDNL KTYKKRYMTY PNILCSSKSE
     KC