ID   NGFV_ECHOC              Reviewed;         168 AA.
AC   P0DMD1;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Venom nerve growth factor;
DE            Short=v-NGF;
DE            Short=vNGF;
DE   Flags: Precursor; Fragment;
OS   Echis ocellatus (Ocellated saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=99586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16713134; DOI=10.1016/j.gene.2006.03.008;
RA   Wagstaff S.C., Harrison R.A.;
RT   "Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals
RT   novel alpha9beta1 integrin-binding motifs in venom metalloproteinases and a
RT   new group of putative toxins, renin-like aspartic proteases.";
RL   Gene 377:21-32(2006).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Venom;
RX   PubMed=21801740; DOI=10.1016/j.toxicon.2011.07.005;
RA   Trummal K., Tonismagi K., Paalme V., Jarvekulg L., Siigur J., Siigur E.;
RT   "Molecular diversity of snake venom nerve growth factors.";
RL   Toxicon 58:363-368(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). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; non-covalently linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: On reduced SDS-PAGE, the determined MW of this protein
CC       is 18.5 kDa. {ECO:0000305|PubMed:21801740}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; DW361587; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DMD1; -.
DR   SMR; P0DMD1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; 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; IPR020433; Venom_nerve_growth_factor.
DR   PANTHER; PTHR11589; PTHR11589; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PIRSF; PIRSF001789; NGF; 1.
DR   PRINTS; PR01917; VENOMNGF.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Growth factor; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW   Protease inhibitor; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000425458"
FT   CHAIN           126..168
FT                   /note="Venom nerve growth factor"
FT                   /id="PRO_0000425459"
FT   REGION          48..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        25
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..?
FT                   /evidence="ECO:0000250"
FT   NON_TER         168
SQ   SEQUENCE   168 AA;  18478 MW;  CAC4795C577AFEB2 CRC64;
     MSMLCYTLII AFLIGIWAAP KSEDNVSLGS PATPDISDTS CAKTHEALKT SQNTDQHSPA
     PKKAEDQEFG SAANIIVDPK LFQKRRFQSP RVLFSTQPPP LSRDEQSVEF LDNADSLNRN
     IRAKRGIHPV HNQGEFSVCD SVNVWVANKT TATDIKGNEV TVMVNVKP