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Database: UniProt
Entry: V9I1A1_BUNFA
LinkDB: V9I1A1_BUNFA
Original site: V9I1A1_BUNFA 
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
//
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