NGFV_MACLB
ID NGFV_MACLB Reviewed; 244 AA.
AC P25428; Q5S8C5;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Venom nerve growth factor;
DE Short=v-NGF;
DE Short=vNGF;
DE Contains:
DE RecName: Full=Truncated venom nerve growth factor;
DE Flags: Precursor;
OS Macrovipera lebetina (Levantine viper) (Vipera lebetina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Macrovipera.
OX NCBI_TaxID=8709;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING
RP OF N-TERMINUS, AND GLYCOSYLATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19463841; DOI=10.1016/j.toxicon.2009.05.001;
RA Paalme V., Trummal K., Samel M., Tonismagi K., Jarvekulg L., Vija H.,
RA Subbi J., Siigur J., Siigur E.;
RT "Nerve growth factor from Vipera lebetina venom.";
RL Toxicon 54:329-336(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-222.
RX PubMed=2025430; DOI=10.1016/0896-6273(91)90180-8;
RA Hallboeoek F., Ibanez C.F., Persson H.;
RT "Evolutionary studies of the nerve growth factor family reveal a novel
RT member abundantly expressed in Xenopus ovary.";
RL Neuron 6:845-858(1991).
RN [3]
RP CHARACTERIZATION, AND GLYCOSYLATION.
RC TISSUE=Venom;
RX PubMed=4017541; DOI=10.1016/0305-0491(85)90185-3;
RA Siigur E., Neuman T., Jarve V., Tara A., Siigur J.;
RT "Isolation and characterization of nerve growth factor from Vipera lebetina
RT (snake) venom.";
RL Comp. Biochem. Physiol. 81:211-215(1985).
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). It promotes neurite outgrowth in rat PC12
CC pheochromocytoma cells (PubMed:19463841).
CC {ECO:0000250|UniProtKB:P61898, ECO:0000250|UniProtKB:P61899,
CC ECO:0000269|PubMed:19463841}.
CC -!- SUBUNIT: Homodimer; non-covalently linked.
CC {ECO:0000269|PubMed:19463841}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19463841}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:19463841}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19463841,
CC ECO:0000269|PubMed:4017541}.
CC -!- MASS SPECTROMETRY: [Venom nerve growth factor]: Mass=14380;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:19463841};
CC -!- MISCELLANEOUS: On the 2D-gel the determined MW of this protein is: 17.5
CC kDa.
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY740013; AAV64846.1; -; mRNA.
DR AlphaFoldDB; P25428; -.
DR SMR; P25428; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
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 1: Evidence at protein 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_0000019615"
FT CHAIN 126..244
FT /note="Venom nerve growth factor"
FT /id="PRO_0000019616"
FT CHAIN 128..244
FT /note="Truncated venom nerve growth factor"
FT /id="PRO_0000397243"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
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"
FT CONFLICT 190
FT /note="S -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 27318 MW; 2230DE4C49D94A51 CRC64;
MSMLCYTLII AFLIGIWAAP KSEDNVSLGS PATPDLSDTS CAKTHEALKT SRNTDQHYPA
PKKAEDQEFG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNADSLNRN
IRAKRATHPV HNRGEFSVCD SVSVWVANKT TATDIRGNVV TVMVDVKLNN NVYRQYFFET
KCKNPSPVSS GCRGIDAKHW NSYCTTTDTF VRALTMEGNQ ASWRFIRIDT ACVCVISRKN
DNFG
