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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
 
 
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