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NGFV2_NAJSP
ID   NGFV2_NAJSP             Reviewed;         241 AA.
AC   Q5YF89;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Venom nerve growth factor 2;
DE            Short=v-NGF-2;
DE            Short=vNGF-2;
DE   AltName: Full=Nerve growth factor II;
DE   Flags: Precursor;
OS   Naja sputatrix (Malayan spitting cobra) (Naja naja sputatrix).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=33626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=15225125; DOI=10.1042/bj20040569;
RA   Koh D.C.-I., Armugam A., Jeyaseelan K.;
RT   "Sputa nerve growth factor forms a preferable substitute to mouse 7S-beta
RT   nerve growth factor.";
RL   Biochem. J. 383:149-158(2004).
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; AY527216; AAS94269.1; -; mRNA.
DR   AlphaFoldDB; Q5YF89; -.
DR   SMR; Q5YF89; -.
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_0000043292"
FT   CHAIN           126..241
FT                   /note="Venom nerve growth factor 2"
FT                   /id="PRO_0000043293"
FT   REGION          47..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..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   241 AA;  27030 MW;  72132B0EEF4020A7 CRC64;
     MSMLCYTLIT AFLIGIWAAP KSEDNVPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
     PQKAEDQELR TAANIIVDPK LFQKRQFQSP RVLFSTQPPL LSRDEESVEF LDNEDSLNRN
     IRAKREDHPV HNLGEHSVCD SVSAWVTKTT ATDIKGNTVT VMENVNLDNK VYKQYFFETK
     CKNPNPVPSG CRGIDSSHWN SYCTETDTFI KALTMEGNQA SWRFIRIDTA CVCVITKKTG
     N
 
 
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