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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //