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