ID   PA2H_VIPBN              Reviewed;         138 AA.
AC   A4VBF0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Acidic phospholipase A2 inhibitor chain HPD-1I;
DE            Short=svPLA2 homolog;
DE   AltName: Full=Heterodimeric neurotoxic phospholipases A2 acidic subunit;
DE   Flags: Precursor;
OS   Vipera berus nikolskii (Nikolsky's adder) (Vipera nikolskii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Vipera.
OX   NCBI_TaxID=1808362;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-27, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=18083205; DOI=10.1016/j.toxicon.2007.11.001;
RA   Ramazanova A.S., Zavada L.L., Starkov V.G., Kovyazina I.V., Subbotina T.F.,
RA   Kostyukhina E.E., Dementieva I.N., Ovchinnikova T.V., Utkin Y.N.;
RT   "Heterodimeric neurotoxic phospholipases A2 -- the first proteins from
RT   venom of recently established species Vipera nikolskii: implication of
RT   venom composition in viper systematics.";
RL   Toxicon 51:524-537(2008).
CC   -!- FUNCTION: Heterodimer: slightly affects neuromuscular transmission
CC       acting presynaptically. It has a low catalytic activity, a low
CC       anticoagulant activity and weakly inhibits ADP-induced platelet
CC       aggregation. {ECO:0000269|PubMed:18083205}.
CC   -!- FUNCTION: Monomer: has no activity (neurotoxic, catalytic,
CC       anticoagulant and a ADP-induced platelet aggregation), but inhibits
CC       phospholipase A2. {ECO:0000269|PubMed:18083205}.
CC   -!- SUBUNIT: Heterodimer of an acidic and a basic chain; non-covalently
CC       linked. The basic chain is toxic and has phospholipase A2 activity
CC       (chain HDP-1P (AC Q1RP79) or HDP-2P (AC Q1RP78)) and the acidic chain
CC       is non-toxic and functions as its inhibitor (chain HPD-1I).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MASS SPECTROMETRY: Mass=13624; Mass_error=1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18083205};
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other phospholipases, it lacks the typical His
CC       active site (His->Gln in position 63). {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; AM707023; CAM92310.1; -; mRNA.
DR   AlphaFoldDB; A4VBF0; -.
DR   SMR; A4VBF0; -.
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   Blood coagulation cascade inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin; Neurotoxin;
KW   Phospholipase A2 inhibitor; Platelet aggregation inhibiting toxin;
KW   Presynaptic neurotoxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:18083205"
FT   CHAIN           17..138
FT                   /note="Acidic phospholipase A2 inhibitor chain HPD-1I"
FT                   /id="PRO_5000237460"
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;  15381 MW;  28F78F5796E586E2 CRC64;
     MRTLWIVAVC LIGVEGNLFQ FGDMILQKTG KEAVHSYAIY GCYCGWGGQG RAQDATDRCC
     FAQDCCYGRV NDCNPKTATY TYSFENGDIV CGDNDLCLRA VCECDRAAAI CLGENVNTYD
     KNYEYYSISH CTEESEQC