ID   PA2H_VIPAZ              Reviewed;         138 AA.
AC   Q10754; Q6A3N8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Acidic phospholipase A2 inhibitor vaspin A chain;
DE            Short=VaspA;
DE            Short=svPLA2 homolog;
DE   AltName: Full=PLA2-I complex chain A;
DE   Flags: Precursor;
OS   Vipera aspis zinnikeri (Viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=55427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12823540; DOI=10.1046/j.1432-1033.2003.03629.x;
RA   Guillemin I., Bouchier C., Garrigues T., Wisner A., Choumet V.;
RT   "Sequences and structural organization of phospholipase A2 genes from
RT   Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom.
RT   Identification of the origin of a new viper population based on ammodytin
RT   I1 heterogeneity.";
RL   Eur. J. Biochem. 270:2697-2706(2003).
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 17-138, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=8619619; DOI=10.1006/abbi.1996.0126;
RA   Komori Y., Masuda K., Nikai T., Sugihara H.;
RT   "Complete primary structure of the subunits of heterodimeric phospholipase
RT   A2 from Vipera a. zinnikeri venom.";
RL   Arch. Biochem. Biophys. 327:303-307(1996).
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 weakly toxic basic protein having
CC       phospholipase A2 activity (B chain) and a non-toxic acidic protein
CC       functioning as its inhibitor but which potentiates its lethal potency
CC       and neurotoxicity (A chain).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8619619}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8619619}.
CC   -!- MASS SPECTROMETRY: Mass=13654; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8619619};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY152843; AAN59979.1; -; Genomic_DNA.
DR   EMBL; AJ580101; CAE47106.1; -; mRNA.
DR   EMBL; AJ580104; CAE47109.1; -; mRNA.
DR   EMBL; AJ580105; CAE47110.1; -; mRNA.
DR   PIR; S62780; S62780.
DR   AlphaFoldDB; Q10754; -.
DR   SMR; Q10754; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin;
KW   Phospholipase A2 inhibitor; Postsynaptic neurotoxin; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..138
FT                   /note="Acidic phospholipase A2 inhibitor vaspin A chain"
FT                   /id="PRO_0000022976"
FT   REGION          121..133
FT                   /note="Important for membrane-damaging activities in
FT                   eukaryotes and bacteria; heparin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        42..131
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        59..111
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        65..138
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        66..104
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        73..97
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
FT   DISULFID        91..102
FT                   /evidence="ECO:0000250|UniProtKB:P24605"
SQ   SEQUENCE   138 AA;  15411 MW;  3FD0BF5796FC9FE2 CRC64;
     MRTLWIVAVC LIGVEGNLFQ FGDMILQKTG KEAVHSYAIY GCYCGWGGQG RAQDATDRCC
     FAQDCCYGRV NDCNPKMATY TYSFENGDIV CGDNDLCLRA VCECDRAAAI CLGENVNTYD
     KNYEYYSISH CTEESEQC