NGFV1_DEMVE
ID NGFV1_DEMVE Reviewed; 242 AA.
AC A6MFL5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Venom nerve growth factor 1;
DE Short=v-NGF-1;
DE Short=vNGF-1;
DE Flags: Precursor;
OS Demansia vestigiata (Lesser black whip snake) (Demansia atra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Notechinae; Demansia.
OX NCBI_TaxID=412038;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=17608513; DOI=10.1021/pr0701613;
RA St Pierre L., Birrell G.W., Earl S.T.H., Wallis T.P., Gorman J.J.,
RA de Jersey J., Masci P.P., Lavin M.F.;
RT "Diversity of toxic components from the venom of the evolutionarily
RT distinct black whip snake, Demansia vestigiata.";
RL J. Proteome Res. 6:3093-3107(2007).
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; DQ917526; ABK63555.1; -; mRNA.
DR AlphaFoldDB; A6MFL5; -.
DR SMR; A6MFL5; -.
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_5000254119"
FT CHAIN 126..242
FT /note="Venom nerve growth factor 1"
FT /id="PRO_5000254120"
FT REGION 26..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..49
FT /note="Polar residues"
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 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..203
FT /evidence="ECO:0000250|UniProtKB:P61898"
FT DISULFID 181..231
FT /evidence="ECO:0000250|UniProtKB:P61898"
FT DISULFID 191..233
FT /evidence="ECO:0000250|UniProtKB:P61898"
SQ SEQUENCE 242 AA; 27209 MW; 77C19A23B21F9E35 CRC64;
MSMLCYTLII AFLIGIWAAP KSEDNVPLGS PATSDLSDTS CAQTHKALKT SRNTDQRHPA
PKKAEDQELG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LENEDALNRN
IRSKRENHPV NDHGEYSVCD SVSVWVNKTT ATDIKGKPVT VMVDVNLNNH VYKQYFFETK
CKNPNPVPSG CRGIDSRHWN SYCTTTQSFV KALTKEGNQA SWRFIRIDTA CVCVISRKTG
NF
