ID   NGFV2_PSEAU             Reviewed;         242 AA.
AC   Q3HXY2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Venom nerve growth factor 2;
DE            Short=v-NGF-2;
DE            Short=vNGF-2;
DE   Flags: Precursor;
OS   Pseudechis australis (Mulga snake) (King brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Pseudechis.
OX   NCBI_TaxID=8670;
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; DQ181913; ABA60125.1; -; mRNA.
DR   AlphaFoldDB; Q3HXY2; -.
DR   SMR; Q3HXY2; -.
DR   PRIDE; Q3HXY2; -.
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_0000043306"
FT   CHAIN           126..242
FT                   /note="Venom nerve growth factor 2"
FT                   /id="PRO_0000043307"
FT   REGION          47..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        139..203
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        181..231
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
FT   DISULFID        191..233
FT                   /evidence="ECO:0000250|UniProtKB:P61898"
SQ   SEQUENCE   242 AA;  27207 MW;  CBCC718A82CF51AA CRC64;
     MSMLCYTLII AFLIGIWAAP QSEDNVPLGS PATSDLSDTS CAQTHEDLKT SRNTDQRHPA
     PKKADDQELG SAANIIVDPK LFQKRQFQSS RVLFSTQPPP LSRDEQSVEF LDNEDALNRN
     IQAKRQNHPV HDLGEHSVCD SISEWVTKTT ATDIKGNTVT VKVDVNLNNH VYKQYFFETK
     CRNPNPVPSG CRGIDSRLWT SYCTKTQTFV RALTMEGNQA SWRFIRIDTA CVCVITKKTD
     NL