ID   PA2HB_AGKPL             Reviewed;         137 AA.
AC   C0HKC2;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2017, sequence version 1.
DT   11-DEC-2019, entry version 5.
DE   RecName: Full=Basic phospholipase A2 homolog {ECO:0000250|UniProtKB:P04361};
DE            Short=svPLA2 homolog {ECO:0000250|UniProtKB:P04361};
DE   AltName: Full=APL-K49 {ECO:0000303|PubMed:28633930};
DE   AltName: Full=AplP2 {ECO:0000303|PubMed:28633930};
DE   Flags: Precursor;
OS   Agkistrodon piscivorus leucostoma (Western cottonmouth) (Acontias
OS   leucostoma).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Agkistrodon.
OX   NCBI_TaxID=459671 {ECO:0000303|PubMed:28633930};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland {ECO:0000303|PubMed:18502463};
RX   PubMed=18502463; DOI=10.1016/j.toxicon.2008.03.028;
RA   Jia Y., Cantu B.A., Sanchez E.E., Perez J.C.;
RT   "Complementary DNA sequencing and identification of mRNAs from the venomous
RT   gland of Agkistrodon piscivorus leucostoma.";
RL   Toxicon 51:1457-1466(2008).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 17-32, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:28633930};
RX   PubMed=28633930; DOI=10.1016/j.toxicon.2017.06.010;
RA   Jia Y., Ermolinsky B., Garza A., Provenzano D.;
RT   "Phospholipase A2 in the venom of three cottonmouth snakes.";
RL   Toxicon 135:84-92(2017).
CC   -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic
CC       activity. {ECO:0000269|PubMed:28633930}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:28633930}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18502463}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       K49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Does not bind calcium as one of the calcium-binding ligands is
CC       lost (Asp->Lys in position 64, which corresponds to 'Lys-49' in the
CC       current nomenclature). {ECO:0000305}.
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DR   EMBL; EV854871; -; NOT_ANNOTATED_CDS; mRNA.
DR   SMR; C0HKC2; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:28633930"
FT   CHAIN           17..137
FT                   /note="Basic phospholipase A2 homolog"
FT                   /evidence="ECO:0000305|PubMed:28633930"
FT                   /id="PRO_0000442173"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        65..137
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250|UniProtKB:P04361"
SQ   SEQUENCE   137 AA;  15713 MW;  3D8FC7C0E4B5AA8D CRC64;
     MRTLWIVALL LVGVEGSVLE LGKMILQETG KNAITSYGSY GCNCGWGHRG QPKDATDRCC
     FVHKCCYKKL TDCNHKTDRY SYSWKNKAII CEEKNPCLKE MCECDKAVAI CLRENLDTYN
     KKYKAYFKLK CKKPDTC
//