ID V9I1A1_BUNFA Unreviewed; 243 AA.
AC V9I1A1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Venom nerve growth factor {ECO:0000313|EMBL:AEH59578.1};
OS Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8613 {ECO:0000313|EMBL:AEH59578.1};
RN [1] {ECO:0000313|EMBL:AEH59578.1}
RP NUCLEOTIDE SEQUENCE.
RA Yu S.-H., Wang Y.-M., Tsai I.-H., Utkin Y.;
RT "Sequences and phylogenetic analysis of nerve growth factors from Vipera
RT ursinii, Daboia russelii, Bungarus fasiatus and Walterinnesia aegyptia
RT snake venom.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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
CC form. {ECO:0000256|ARBA:ARBA00025325}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the NGF-beta family.
CC {ECO:0000256|ARBA:ARBA00010783}.
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DR EMBL; HM590742; AEH59578.1; -; mRNA.
DR AlphaFoldDB; V9I1A1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 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:SF10; BETA-NERVE GROWTH FACTOR; 1.
DR PANTHER; PTHR11589; NERVE GROWTH FACTOR NGF -RELATED; 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; Cystine-knot cytokines; 1.
DR PROSITE; PS00248; NGF_1; 1.
DR PROSITE; PS50270; NGF_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001789-1};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..243
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004777346"
FT DOMAIN 131..235
FT /note="Nerve growth factor-related"
FT /evidence="ECO:0000259|SMART:SM00140"
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 DISULFID 139..204
FT /evidence="ECO:0000256|PIRSR:PIRSR001789-1"
FT DISULFID 182..232
FT /evidence="ECO:0000256|PIRSR:PIRSR001789-1"
FT DISULFID 192..234
FT /evidence="ECO:0000256|PIRSR:PIRSR001789-1"
SQ SEQUENCE 243 AA; 27346 MW; 2B9754F1654A9C98 CRC64;
MSMLCYTLII AFLIGIWAAP KSEDNVPLGS PATSDLSDAS CAQTHEGLKT SRNTDQRHPA
SKKAEDQELG SAANIIVDPK LFEKRQFQSP RVLFSTQSPP LSRDEQSVEF LDNEDALNRN
IWAKNENHPV HNQGEHSVCD SISAWVTNKT EAIDVKGNTV TVMVDVNLNN EVYKQYFFET
KCRNPNPVPS GCRGIDSRHW NSYCTTRDTF VKALTMEGNR ASWRFIRIDT ACVCVISRKT
ENF
//