NGFV_OXYSC
ID NGFV_OXYSC Reviewed; 243 AA.
AC Q3I5F4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Venom nerve growth factor;
DE Short=v-NGF;
DE Short=vNGF;
DE Flags: Precursor;
OS Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=8667;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16261251; DOI=10.1007/s00018-005-5384-9;
RA St Pierre L., Woods R., Earl S.T.H., Masci P.P., Lavin M.F.;
RT "Identification and analysis of venom gland-specific genes from the coastal
RT taipan (Oxyuranus scutellatus) and related species.";
RL Cell. Mol. Life Sci. 62:2679-2693(2005).
RN [2]
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).
RN [3]
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}.
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; DQ084064; AAZ39009.1; -; mRNA.
DR AlphaFoldDB; Q3I5F4; -.
DR SMR; Q3I5F4; -.
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 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_0000346650"
FT CHAIN 126..243
FT /note="Venom nerve growth factor"
FT /id="PRO_0000346651"
FT REGION 47..69
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; 27382 MW; CEF6D7A2B78FF0F1 CRC64;
MSMLCYTLII VFLIGIWAAP KSEDNVPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
PKKAEDQELG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNEDTLNRN
IRAKRETHPV HNLGEYSVCD SISVWVANKT EAMDIKGKPV TVMVDVNLNN HVFKQYFFET
KCRNPNPVPS GCRGIDSGHW NSYCTTTQTF VRALTMEGNQ ASWRFIRIDT ACVCVISRKT
ENF
