ID   PA2H_VIPAP              Reviewed;         138 AA.
AC   Q8JFG1; Q6A3P3;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Acidic phospholipase A2 inhibitor vaspin A chain;
DE            Short=svPLA2 homolog;
DE   AltName: Full=Vaspin non-toxic component;
DE   Flags: Precursor;
OS   Vipera aspis aspis (Aspic viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=194601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=12220671; DOI=10.1016/s0014-5793(02)03205-2;
RA   Jan V., Maroun R.C., Robbe-Vincent A., De Haro L., Choumet V.;
RT   "Toxicity evolution of Vipera aspis aspis venom: identification and
RT   molecular modeling of a novel phospholipase A(2) heterodimer neurotoxin.";
RL   FEBS Lett. 527:263-268(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17904178; DOI=10.1016/j.toxicon.2007.07.024;
RA   Jan V.M., Guillemin I., Robbe-Vincent A., Choumet V.;
RT   "Phospholipase A2 diversity and polymorphism in European viper venoms:
RT   paradoxical molecular evolution in Viperinae.";
RL   Toxicon 50:1140-1161(2007).
CC   -!- FUNCTION: Heterodimer: postsynaptic neurotoxin. {ECO:0000250}.
CC   -!- FUNCTION: Monomer: the acidic chain inhibits the basic phospholipase A2
CC       of the complex. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a toxic basic protein having phospholipase A2
CC       activity (B chain (AC Q8JFG0)) and a non-toxic acidic protein
CC       functioning as its inhibitor (A chain).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AJ459806; CAD30849.1; -; mRNA.
DR   EMBL; AJ580096; CAE47101.1; -; mRNA.
DR   EMBL; AJ580097; CAE47102.1; -; mRNA.
DR   EMBL; AJ580099; CAE47104.1; -; mRNA.
DR   EMBL; AJ580106; CAE47111.1; -; mRNA.
DR   AlphaFoldDB; Q8JFG1; -.
DR   SMR; Q8JFG1; -.
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:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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   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.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Neurotoxin; Phospholipase A2 inhibitor;
KW   Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000250"
FT   CHAIN           17..138
FT                   /note="Acidic phospholipase A2 inhibitor vaspin A chain"
FT                   /id="PRO_0000022969"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15411 MW;  3FD0BF5796FC9FE2 CRC64;
     MRTLWIVAVC LIGVEGNLFQ FGDMILQKTG KEAVHSYAIY GCYCGWGGQG RAQDATDRCC
     FAQDCCYGRV NDCNPKMATY TYSFENGDIV CGDNDLCLRA VCECDRAAAI CLGENVNTYD
     KNYEYYSISH CTEESEQC