ID   NGFV_BOTJR              Reviewed;         241 AA.
AC   Q90W38;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
DE   AltName: Full=Bj-NGF;
DE   Flags: Precursor;
GN   Name=NGF;
OS   Bothrops jararacussu (Jararacussu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND 3D-STRUCTURE MODELING OF 123-241.
RC   TISSUE=Venom gland;
RX   PubMed=12453640; DOI=10.1016/s0300-9084(02)01429-3;
RA   Kashima S., Soares A.M., Roberto P.G., Pereira J.O., Astolfi-Filho S.,
RA   Cintra A.O., Fontes M.R.M., Giglio J.R., de Castro Franca S.;
RT   "cDNA sequence and molecular modeling of a nerve growth factor from
RT   Bothrops jararacussu venomous gland.";
RL   Biochimie 84:675-680(2002).
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:0000250|UniProtKB:P61898}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; AY007318; AAG12169.1; -; mRNA.
DR   AlphaFoldDB; Q90W38; -.
DR   SMR; Q90W38; -.
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; ISS:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR020408; Nerve_growth_factor-like.
DR   InterPro; IPR002072; Nerve_growth_factor-rel.
DR   InterPro; IPR020425; Nerve_growth_factor_bsu.
DR   InterPro; IPR019846; Nerve_growth_factor_CS.
DR   InterPro; IPR020433; Venom_nerve_growth_factor.
DR   PANTHER; PTHR11589; PTHR11589; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PIRSF; PIRSF001789; NGF; 1.
DR   PRINTS; PR00268; NGF.
DR   PRINTS; PR01913; NGFBETA.
DR   PRINTS; PR01917; VENOMNGF.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00248; NGF_1; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Growth factor; Lipid-binding; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043282"
FT   CHAIN           123..241
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_0000043283"
FT   REGION          47..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        136..201
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        179..229
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        189..231
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   241 AA;  27162 MW;  AC57F724A6531A8F CRC64;
     MSMLCYTLII TLLIGIWAAP KSEDNVPLGS PATSDLSVTS CTKTHEALKT SRNTDQHYPA
     PKKEEDQEFG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVDD ANSLNRNIRA
     KREDHPVHNR GEYSVCDSVN VWVANKTTAT DIRGNVVTVM VDVNINNNVY KQYFFETKCR
     NPNPVPTGCR GIDARHWNSY CTTTNTFVKA LTMEGNQASW RFIRIDTACV CVISRKNENF
     G