NGFV_NAJKA
ID NGFV_NAJKA Reviewed; 116 AA.
AC P61899; P21377;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Venom nerve growth factor;
DE Short=v-NGF;
DE Short=vNGF;
OS Naja kaouthia (Monocled cobra) (Naja siamensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8649;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=1995338; DOI=10.1016/0014-5793(91)80244-w;
RA Inoue S., Oda T., Koyama J., Ikeda K., Hayashi K.;
RT "Amino acid sequences of nerve growth factors derived from cobra venoms.";
RL FEBS Lett. 279:38-40(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-14, FUNCTION AS METALLOPROTEINASE INHIBITOR, AND MASS
RP SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20164177; DOI=10.1074/jbc.m110.100479;
RA Wijeyewickrema L.C., Gardiner E.E., Gladigau E.L., Berndt M.C.,
RA Andrews R.K.;
RT "Nerve growth factor inhibits metalloproteinase-disintegrins and blocks
RT ectodomain shedding of platelet glycoprotein VI.";
RL J. Biol. Chem. 285:11793-11799(2010).
RN [3]
RP CRYSTALLIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=12359255; DOI=10.1016/s0006-291x(02)02323-9;
RA Gu L., Shen Y., Xu S., Shu Y., Jiang T., Lin Z.;
RT "Crystallization and preliminary X-ray diffraction studies of cobra venom
RT beta-nerve growth factor.";
RL Biochem. Biophys. Res. Commun. 297:1008-1010(2002).
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 (PubMed:20164177). 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:0000269|PubMed:20164177}.
CC -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12359255}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:12359255}.
CC -!- MASS SPECTROMETRY: Mass=13049.92; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20164177};
CC -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR AlphaFoldDB; P61899; -.
DR SMR; P61899; -.
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; IDA: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 Direct protein sequencing; Disulfide bond; Growth factor; Lipid-binding;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Secreted; Toxin.
FT CHAIN 1..116
FT /note="Venom nerve growth factor"
FT /id="PRO_0000159606"
FT DISULFID 14..78
FT /evidence="ECO:0000250|UniProtKB:P61898"
FT DISULFID 56..106
FT /evidence="ECO:0000250|UniProtKB:P61898"
FT DISULFID 66..108
FT /evidence="ECO:0000250|UniProtKB:P61898"
SQ SEQUENCE 116 AA; 13064 MW; DAB35421093F3B06 CRC64;
EDHPVHNLGE HSVCDSVSAW VTKTTATDIK GNTVTVMENV NLDNKVYKEY FFETKCKNPN
PEPSGCRGID SSHWNSYCTE TDTFIKALTM EGNQASWRFI RIETACVCVI TKKKGN