ID   NGFV_CRYNI              Reviewed;         243 AA.
AC   Q1W7Q6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
DE   Flags: Precursor;
OS   Cryptophis nigrescens (Eastern small-eyed snake) (Rhinoplocephalus
OS   nigrescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Cryptophis.
OX   NCBI_TaxID=292442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=17109379; DOI=10.1002/pmic.200600263;
RA   Earl S.T.H., Birrell G.W., Wallis T.P., St Pierre L., Masci P.P.,
RA   de Jersey J., Gorman J.J., Lavin M.F.;
RT   "Post-translational modification accounts for the presence of varied forms
RT   of nerve growth factor in Australian elapid snake venoms.";
RL   Proteomics 6:6554-6565(2006).
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; DQ422727; ABD85370.1; -; mRNA.
DR   AlphaFoldDB; Q1W7Q6; -.
DR   SMR; Q1W7Q6; -.
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..125
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_5000141488"
FT   CHAIN           126..243
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_5000141489"
FT   REGION          45..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..204
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        182..232
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        192..234
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   243 AA;  27576 MW;  DD77D2906811859D CRC64;
     MSMLCYTLII AFLIGIWAAP KSEDNVPLGS PTTSDLSDTS CAQTHEGLKT SRNTDQRHLA
     PKKAEDQELG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNEDTLNRN
     IRTKRETHPV HNLGEHSVCD SISVWVTNKT KATDIKDNMV TVMVDINLNN EVYKQYFFET
     KCRNPNPVPS GCRGTDSRHW NSYCTTTQTF VKALTMEGNR ASWRFIRIDT ACVCVISRKT
     DNF