ID   NGFV_DRYCN              Reviewed;         242 AA.
AC   F8RKW5;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
DE   Flags: Precursor;
OS   Drysdalia coronoides (White-lipped snake) (Hoplocephalus coronoides).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Notechinae; Drysdalia.
OX   NCBI_TaxID=66186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21133350; DOI=10.1021/pr1008916;
RA   Chatrath S.T., Chapeaurouge A., Lin Q., Lim T.K., Dunstan N., Mirtschin P.,
RA   Kumar P.P., Kini R.M.;
RT   "Identification of novel proteins from the venom of a cryptic snake
RT   Drysdalia coronoides by a combined transcriptomics and proteomics
RT   approach.";
RL   J. Proteome Res. 10:739-750(2011).
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   -!- MISCELLANEOUS: The presence of this protein in the venom could not be
CC       confirmed. {ECO:0000305|PubMed:21133350}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; HM627208; AEH95535.1; -; mRNA.
DR   AlphaFoldDB; F8RKW5; -.
DR   SMR; F8RKW5; -.
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; IEA:UniProtKB-KW.
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; Glycoprotein;
KW   Growth factor; Lipid-binding; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..125
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425462"
FT   CHAIN           126..242
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_0000425463"
FT   REGION          47..70
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   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   242 AA;  27282 MW;  B0BEE77CF46A15C7 CRC64;
     MSMMCYTLII AFLIGIWAAP KSEDNVPLGS PATSDLSDTS CAQTHEGLKT SRNTDQRHPA
     PKKAEDQELG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNEDTLNRN
     IRAKRENHPV HNQGEHSVCD SVSDWVIKTT ATDIHGNMVT VMGDINFTNE VYKQYFFETK
     CRNPNPVPSG CRGIDSKVWN SYCTTTQTFV KALTMEGSRA SWRFIRIDTA CVCVISRKTE
     NF