ID   NGFV1_NAJSP             Reviewed;         243 AA.
AC   Q5YF90;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Venom nerve growth factor 1;
DE            Short=v-NGF-1;
DE            Short=vNGF-1;
DE   AltName: Full=Nerve growth factor I;
DE   Flags: Precursor;
OS   Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=33626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 126-138.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15225125; DOI=10.1042/bj20040569;
RA   Koh D.C.-I., Armugam A., Jeyaseelan K.;
RT   "Sputa nerve growth factor forms a preferable substitute to mouse 7S-beta
RT   nerve growth factor.";
RL   Biochem. J. 383:149-158(2004).
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; AY527215; AAS94268.1; -; mRNA.
DR   AlphaFoldDB; Q5YF90; -.
DR   SMR; Q5YF90; -.
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; Direct protein sequencing;
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:0000269|PubMed:15225125"
FT                   /id="PRO_0000043290"
FT   CHAIN           126..243
FT                   /note="Venom nerve growth factor 1"
FT                   /id="PRO_0000043291"
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;  27551 MW;  2BFB1928CDD81258 CRC64;
     MSMLCYTLII AFLIGIWAVP KSEDNAPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
     PRSQRIKQFG SASNIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNEDALNRN
     IRAKRETHPV HNRGEYSVCD SISVWVANKT TATDIKGKPV TVMVDVNLNN HVYKQYFFET
     KCRNPNPVPS GCRGIDSRHW NSYCTTTHTF VKALTMEGNR ASWRFIRIDT ACVCVISRKT
     ENF