ID   NGFV3_NOTSC             Reviewed;         244 AA.
AC   Q3HXY5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Venom nerve growth factor 3;
DE            Short=v-NGF-3;
DE            Short=vNGF-3;
DE   Flags: Precursor;
OS   Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Notechis.
OX   NCBI_TaxID=70142;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Earl S.T.H., St Pierre L., Birrell G.W., Wallis T.P., Masci P.P.,
RA   de Jersey J., Gorman J.J., Lavin M.F.;
RT   "Identification of nerve growth factor as a ubiquitous component of
RT   Australian elapid snake venoms.";
RL   Submitted (AUG-2005) 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 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; DQ181910; ABA60122.1; -; mRNA.
DR   AlphaFoldDB; Q3HXY5; -.
DR   SMR; Q3HXY5; -.
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; Growth factor;
KW   Lipid-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..125
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043298"
FT   CHAIN           126..244
FT                   /note="Venom nerve growth factor 3"
FT                   /id="PRO_0000043299"
FT   REGION          47..67
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..205
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        181..233
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        193..235
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   244 AA;  27789 MW;  BA39838B30052726 CRC64;
     MSMLCYTLII AFLIGIWAAP KSEDNVPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
     PKKAEDQELG SVANIIVDPK LFQKRRFQSS RVLFSTQPPP LSRDEQSVEF LDNEDTLNRN
     IRAKRENHPV HNQGEHSVCD SVSDWVIKTT ATDIRGNMVT VMVDINRDNE VYKQYFFETK
     CRNPNPNPVQ SECRGIDSRL WNSYCTTTRT FVRALTMEGN QASWRFIRID TACVCVIIRK
     TDNF