NGFV_NAJAT
ID NGFV_NAJAT Reviewed; 116 AA.
AC P61898; P21377;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Venom nerve growth factor {ECO:0000303|PubMed:1002678, ECO:0000303|PubMed:21801740, ECO:0000303|PubMed:2619756};
DE Short=v-NGF;
DE Short=vNGF;
DE AltName: Full=Cobra nerve growth factor {ECO:0000303|PubMed:22649032};
DE Short=cNGF {ECO:0000303|PubMed:22649032};
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2619756;
RA Oda T., Ohta M., Inoue S., Ikeda K., Furukawa S., Hayashi K.;
RT "Amino acid sequence of nerve growth factor purified from the venom of the
RT Formosan cobra Naja naja atra.";
RL Biochem. Int. 19:909-917(1989).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=1002678; DOI=10.1093/oxfordjournals.jbchem.a131356;
RA Furukawa S., Hayashi K.;
RT "Isolation and characterization of nerve growth factor from the venom of
RT Naja naja atra.";
RL J. Biochem. 80:1001-1009(1976).
RN [3]
RP CHARACTERIZATION.
RC TISSUE=Venom;
RX PubMed=21801740; DOI=10.1016/j.toxicon.2011.07.005;
RA Trummal K., Tonismagi K., Paalme V., Jarvekulg L., Siigur J., Siigur E.;
RT "Molecular diversity of snake venom nerve growth factors.";
RL Toxicon 58:363-368(2011).
RN [4] {ECO:0007744|PDB:4EC7}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF HOMODIMER IN COMPLEX WITH A
RP 1,2-DIACYL-SN-GLYCEROL, INTERACTION WITH NTRK1, FUNCTION, LIPID-BINDING,
RP SUBCELLULAR LOCATION, SUBUNIT, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=22649032; DOI=10.1096/fj.12-207316;
RA Tong Q., Wang F., Zhou H.Z., Sun H.L., Song H., Shu Y.Y., Gong Y.,
RA Zhang W.T., Cai T.X., Yang F.Q., Tang J., Jiang T.;
RT "Structural and functional insights into lipid-bound nerve growth
RT factors.";
RL FASEB J. 26:3811-3821(2012).
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 (PubMed:22649032). {ECO:0000250|UniProtKB:P61899,
CC ECO:0000269|PubMed:22649032}.
CC -!- SUBUNIT: Homodimer; non-covalently linked (PubMed:1002678,
CC PubMed:22649032). Interacts with NTRK1 (PubMed:22649032).
CC {ECO:0000269|PubMed:1002678, ECO:0000269|PubMed:22649032}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1002678}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:1002678}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:21801740}.
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR PIR; A58566; A58566.
DR PDB; 4EC7; X-ray; 2.60 A; A/B=1-116.
DR PDBsum; 4EC7; -.
DR AlphaFoldDB; P61898; -.
DR SMR; P61898; -.
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 PANTHER; PTHR11589; PTHR11589; 1.
DR Pfam; PF00243; NGF; 1.
DR PRINTS; PR00268; NGF.
DR PRINTS; PR01913; NGFBETA.
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 3D-structure; Direct protein sequencing; Disulfide bond; Growth factor;
KW Lipid-binding; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Secreted; Toxin.
FT CHAIN 1..116
FT /note="Venom nerve growth factor"
FT /evidence="ECO:0000269|PubMed:2619756"
FT /id="PRO_0000159605"
FT BINDING 86
FT /ligand="a 1,2-diacyl-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17815"
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EC7"
FT DISULFID 14..78
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EC7"
FT DISULFID 56..106
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EC7"
FT DISULFID 66..108
FT /evidence="ECO:0000269|PubMed:22649032,
FT ECO:0007744|PDB:4EC7"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:4EC7"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 74..91
FT /evidence="ECO:0007829|PDB:4EC7"
FT STRAND 94..112
FT /evidence="ECO:0007829|PDB:4EC7"
SQ SEQUENCE 116 AA; 13064 MW; DAB35421093F3B06 CRC64;
EDHPVHNLGE HSVCDSVSAW VTKTTATDIK GNTVTVMENV NLDNKVYKEY FFETKCKNPN
PEPSGCRGID SSHWNSYCTE TDTFIKALTM EGNQASWRFI RIETACVCVI TKKKGN
