NGFV_BUNMU
ID NGFV_BUNMU Reviewed; 243 AA.
AC P34128;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Venom nerve growth factor;
DE Short=v-NGF;
DE Short=vNGF;
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=7916740; DOI=10.3109/08977199309029136;
RA Danse J.-M., Garnier J.-M.;
RT "Molecular cloning of a cDNA encoding a nerve growth factor precursor from
RT the krait, Bungarus multicinctus.";
RL Growth Factors 8:77-86(1993).
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).
RN [3]
RP SUBUNIT.
RX PubMed=417735; DOI=10.1016/0005-2795(78)90384-7;
RA Furukawa S., Hayashi K.;
RT "Purification and characterization of nerve growth factor from the venom of
RT Bungarus multicinctus.";
RL Biochim. Biophys. Acta 533:383-395(1978).
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. {ECO:0000269|PubMed:417735}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR EMBL; S56212; AAB25729.1; -; mRNA.
DR PIR; I51193; I51193.
DR AlphaFoldDB; P34128; -.
DR SMR; P34128; -.
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 Disulfide bond; Glycoprotein; Growth factor; Lipid-binding;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..125
FT /evidence="ECO:0000250"
FT /id="PRO_0000019613"
FT CHAIN 126..243
FT /note="Venom nerve growth factor"
FT /id="PRO_0000019614"
FT REGION 47..70
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; 27514 MW; E33F64B142179A08 CRC64;
MSMLCYTLII AFLIGIWAAP KSEDNVPLGS PAKSDFSDTN CAQTHEGLKT SRNTDQHHPT
PKKSEDQELG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVKF LDTEDTLNRN
IWANNENHPV HNQGEHSVCD SISVWVTNKT KATDIKGNTV TVMVDVNLNN EVYKQYFFET
KCRNPNPVPS GCRGIDSRHW NSYCTTTDTF VKALTMEGNR ASWRFIRIDT ACVCVISRKT
ENF
