ID   NGFV_BOTCO              Reviewed;          21 AA.
AC   P0DMG7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Venom nerve growth factor Bco12;
DE            Short=v-NGF;
DE            Short=vNGF;
DE   Flags: Fragment;
OS   Bothrops cotiara (Cotiara) (Rhinocerophis cotiara).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8727;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=18760386; DOI=10.1016/j.jprot.2008.07.007;
RA   Tashima A.K., Sanz L., Camargo A.C., Serrano S.M., Calvete J.J.;
RT   "Snake venomics of the Brazilian pitvipers Bothrops cotiara and Bothrops
RT   fonsecai. Identification of taxonomy markers.";
RL   J. Proteomics 71:473-485(2008).
CC   -!- FUNCTION: Nerve growth factor is important for the development and
CC       maintenance of the sympathetic and sensory nervous systems. It
CC       stimulates division and differentiation of sympathetic and embryonic
CC       sensory neurons as well as basal forebrain cholinergic neurons in the
CC       brain. Its relevance in the snake venom is not clear. However, it has
CC       been shown to inhibit metalloproteinase-dependent proteolysis of
CC       platelet glycoprotein Ib alpha, suggesting a metalloproteinase
CC       inhibition to prevent metalloprotease autodigestion and/or protection
CC       against prey proteases (By similarity). Binds a lipid between the two
CC       protein chains in the homodimer. The lipid-bound form promotes
CC       histamine relase from mouse mast cells, contrary to the lipid-free form
CC       (By similarity). {ECO:0000250|UniProtKB:P61898,
CC       ECO:0000250|UniProtKB:P61899}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked.
CC       {ECO:0000250|UniProtKB:P61898}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18760386}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18760386}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   AlphaFoldDB; P0DMG7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   PROSITE; PS50270; NGF_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW   Lipid-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Secreted; Toxin.
FT   CHAIN           1..>21
FT                   /note="Venom nerve growth factor Bco12"
FT                   /id="PRO_0000428807"
FT   DISULFID        14..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2442 MW;  A740C09A55A3CC03 CRC64;
     EDHPVHNRGE YSVCDSVNVW V