ID   NGFV_DABRR              Reviewed;         117 AA.
AC   P30894;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
OS   Daboia russelii (Russel's viper) (Vipera russelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX   NCBI_TaxID=8707;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-21.
RC   TISSUE=Venom;
RX   PubMed=1477101; DOI=10.1016/0167-4838(92)90090-z;
RA   Koyama J., Inoue S., Ikeda K., Hayashi K.;
RT   "Purification and amino-acid sequence of a nerve growth factor from the
RT   venom of Vipera russelli russelli.";
RL   Biochim. Biophys. Acta 1160:287-292(1992).
RN   [2]
RP   CHARACTERIZATION, AND GLYCOSYLATION.
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:0000250|UniProtKB:P61898}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21801740}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:21801740}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   AlphaFoldDB; P30894; -.
DR   SMR; P30894; -.
DR   iPTMnet; P30894; -.
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   PANTHER; PTHR11589; PTHR11589; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PRINTS; PR00268; NGF.
DR   PRINTS; PR01913; NGFBETA.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 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; Glycoprotein; Growth factor;
KW   Lipid-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Secreted; Toxin.
FT   CHAIN           1..117
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_0000159604"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1477101"
FT   DISULFID        12..77
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        55..105
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        65..107
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   117 AA;  13283 MW;  A64559C5FEC11F66 CRC64;
     HPVHNQGEFS VCDSVSVWVA NKTTATDMRG NVVTVMVDVN LNNNVYKQYF FETKCKNPNP
     VPSGCRGIDA KHWNSYCTTT DTFVRALTME RNQASWRFIR INTACVCVIS RKNDNFG