ID   PA2HA_BOTNI             Reviewed;          41 AA.
AC   C0HJW8;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   02-JUN-2021, entry version 4.
DE   RecName: Full=Phospholipase A2 homolog nigroviriditoxin acidic subunit A {ECO:0000305|PubMed:20590130};
DE   Flags: Fragments;
OS   Bothriechis nigroviridis (Black-speckled palm pit viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothriechis.
OX   NCBI_TaxID=88079;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:20590130};
RX   PubMed=20590130; DOI=10.1021/pr100545d;
RA   Fernandez J., Lomonte B., Sanz L., Angulo Y., Gutierrez J.M., Calvete J.J.;
RT   "Snake venomics of Bothriechis nigroviridis reveals extreme variability
RT   among palm pitviper venoms: different evolutionary solutions for the same
RT   trophic purpose.";
RL   J. Proteome Res. 9:4234-4241(2010).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:25434534};
RX   PubMed=25434534; DOI=10.1016/j.toxicon.2014.11.235;
RA   Lomonte B., Mora-Obando D., Fernandez J., Sanz L., Pla D., Gutierrez J.M.,
RA   Calvete J.J.;
RT   "First crotoxin-like phospholipase A(2) complex from a New World non-
RT   rattlesnake species: nigroviriditoxin, from the arboreal Neotropical snake
RT   Bothriechis nigroviridis.";
RL   Toxicon 93:144-154(2015).
CC   -!- FUNCTION: Heterodimer A-B: Nigroviriditoxin possesses phospholipase A2
CC       (PLA2) activity. It consists of a non-covalent association of a basic
CC       PLA2 subunit B with a non-enzymatic subunit A.
CC       {ECO:0000269|PubMed:25434534}.
CC   -!- FUNCTION: Subunit A: The acidic subunit of nigroviriditoxin probably is
CC       a heterotrimer of three disulfide-linked chains generated by post-
CC       translational maturation of a PLA2-like precursor (PubMed:20590130). It
CC       appears to have no PLA2 activity of its own, instead inhibiting the
CC       catalytic activity of subunit B (PubMed:25434534). It is not toxic to
CC       mice by itself but increases toxicity of subunit B (PubMed:25434534).
CC       {ECO:0000269|PubMed:20590130, ECO:0000269|PubMed:25434534}.
CC   -!- SUBUNIT: Nigroviriditoxin is a heterodimer of an acidic subunit A and a
CC       basic subunit B. {ECO:0000269|PubMed:25434534}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20590130,
CC       ECO:0000269|PubMed:25434534}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:25434534}.
CC   -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC       D49 sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: The order of the peptides is unknown. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted.
FT   CHAIN           1..41
FT                   /note="Phospholipase A2 homolog nigroviriditoxin acidic
FT                   subunit A"
FT                   /id="PRO_0000434986"
FT   REGION          19..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000303|PubMed:20590130"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:20590130"
FT   NON_TER         41
FT                   /evidence="ECO:0000303|PubMed:20590130"
SQ   SEQUENCE   41 AA;  4319 MW;  FCCE97013DDB8FDB CRC64;
     SPENCQGESQ PCGCYCDAEG QGWPQDAEEN GDIVCGEXTP C