ID   NGFV_NAJNA              Reviewed;         116 AA.
AC   P01140;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   02-SEP-2026, entry version 107.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
OS   Naja naja (Indian cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=35670;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=1995338; DOI=10.1016/0014-5793(91)80244-w;
RA   Inoue S., Oda T., Koyama J., Ikeda K., Hayashi K.;
RT   "Amino acid sequences of nerve growth factors derived from cobra venoms.";
RL   FEBS Lett. 279:38-40(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-26, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA   Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA   Athauda S.B., Moriyama A.;
RT   "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT   russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL   Biomed. Res. 31:71-81(2010).
RN   [3]
RP   PRELIMINARY PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=1247508; DOI=10.1021/bi00646a005;
RA   Hogue-Angeletti R.A., Frazier W.A., Jacobs J.W., Niall H.D., Bradshaw R.A.;
RT   "Purification, characterization, and partial amino acid sequence of nerve
RT   growth factor from cobra venom.";
RL   Biochemistry 15:26-34(1976).
RN   [4]
RP   CHARACTERIZATION.
RC   TISSUE=Venom;
RX   PubMed=21801740; DOI=10.1016/j.toxicon.2011.07.005;
RA   Trummal K., Tonismagi K., Paalme V., Jarvekulg L., Siigur J., Siigur E.;
RT   "Molecular diversity of snake venom nerve growth factors.";
RL   Toxicon 58:363-368(2011).
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:0000269|PubMed:1247508}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20203422}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:21801740}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   PIR; S13927; NGNJXI.
DR   AlphaFoldDB; P01140; -.
DR   SMR; P01140; -.
DR   Proteomes; UP000694559; Unplaced.
DR   GO; GO:0030424; C:axon; IEA:TreeGrafter.
DR   GO; GO:0030425; C:dendrite; IEA:TreeGrafter.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:TreeGrafter.
DR   GO; GO:0008083; F:growth factor activity; IEA:TreeGrafter.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0005163; F:nerve growth factor receptor binding; IEA:TreeGrafter.
DR   GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:TreeGrafter.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:TreeGrafter.
DR   GO; GO:0021675; P:nerve development; IEA:TreeGrafter.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:TreeGrafter.
DR   FunFam; 2.10.90.10:FF:000002; Brain-derived neurotrophic factor; 1.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 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   PANTHER; PTHR11589:SF10; BETA-NERVE GROWTH FACTOR; 1.
DR   PANTHER; PTHR11589; NERVE GROWTH FACTOR NGF -RELATED; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PRINTS; PR00268; NGF.
DR   PRINTS; PR01913; NGFBETA.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00248; NGF_1; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Growth factor; Lipid-binding;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Reference proteome; Secreted; Toxin.
FT   CHAIN           1..116
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_0000159607"
FT   DISULFID        14..78
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        56..106
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        66..108
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   116 AA;  13023 MW;  DAB346B1093E7E06 CRC64;
     EDHPVHNLGE HSVCDSVSAW VTKTTATDIK GNTVTVMENV NLDNKVYKEY FFETKCKNPN
     PEPSGCRGID SSHWNSYCTE TDTFIKALTM EGNQASWRFI RIDTACVCVI TKKTGN
//