NGFV1_PSEAU
ID NGFV1_PSEAU Reviewed; 242 AA.
AC Q3HXY3;
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 1;
DE Short=v-NGF-1;
DE Short=vNGF-1;
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; DQ181912; ABA60124.1; -; mRNA.
DR AlphaFoldDB; Q3HXY3; -.
DR SMR; Q3HXY3; -.
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_0000043304"
FT CHAIN 126..242
FT /note="Venom nerve growth factor 1"
FT /id="PRO_0000043305"
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; 27156 MW; A6A034BCD6B57EBE CRC64;
MSMLCYTLII AFLIGIWAAP QSEDNVPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
PKKVDDQELG SVANIIVDPK LFQKRQFQSS RVLFSTQPPP LSRDEQSVEF LDNEDALNRN
IQAKRQNHPV HDLGEHSVCD SISEWVTKTT ATDIKGNTVT VEVDVNLNNE VYKQYFFETK
CRNPNPVPSG CRGIDSRLWN SYCTTTQTFV KALTMEGNQA SWRFIRIDTA CVCVITKKTD
NL