ID   A0A1Y1BWD5_9SAUR        Unreviewed;       213 AA.
AC   A0A1Y1BWD5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-NOV-2024, entry version 23.
DE   RecName: Full=Neurotrophin-3 {ECO:0000256|ARBA:ARBA00018014, ECO:0000256|RuleBase:RU365037};
DE            Short=NT-3 {ECO:0000256|RuleBase:RU365037};
DE   Flags: Fragment;
GN   Name=NT3 {ECO:0000313|EMBL:BAX64230.1};
OS   Sinomicrurus iwasakii.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Sinomicrurus.
OX   NCBI_TaxID=34994 {ECO:0000313|EMBL:BAX64230.1};
RN   [1] {ECO:0000313|EMBL:BAX64230.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kaito T., Ota H., Toda M.;
RT   "The evolutionary history and taxonomic reevaluation of the Japanese coral
RT   snake, Sinomicrurus japonicus (Serpentes, Elapidae), endemic to the Ryukyu
RT   Archipelago, Japan, by use of molecular and morphological analyses.";
RL   J. Zool. Syst. Evol. Res. 55:156-166(2017).
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. Binds a lipid between the two protein chains in
CC       the homodimer. The lipid-bound form promotes histamine relase from
CC       mouse mast cells, contrary to the lipid-free form.
CC       {ECO:0000256|ARBA:ARBA00045475}.
CC   -!- FUNCTION: Seems to promote the survival of visceral and proprioceptive
CC       sensory neurons. {ECO:0000256|ARBA:ARBA00003312,
CC       ECO:0000256|RuleBase:RU365037}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU365037}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family.
CC       {ECO:0000256|ARBA:ARBA00010783, ECO:0000256|RuleBase:RU365037}.
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DR   EMBL; LC094132; BAX64230.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1BWD5; -.
DR   GO; GO:0030424; C:axon; IEA:TreeGrafter.
DR   GO; GO:0030425; C:dendrite; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:TreeGrafter.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005163; F:nerve growth factor receptor binding; IEA:TreeGrafter.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0007613; P:memory; IEA:TreeGrafter.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:TreeGrafter.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:TreeGrafter.
DR   GO; GO:0021675; P:nerve development; IEA:TreeGrafter.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; IEA:TreeGrafter.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:TreeGrafter.
DR   GO; GO:0007422; P:peripheral nervous system development; IEA:TreeGrafter.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:TreeGrafter.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IEA:TreeGrafter.
DR   Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR020408; Nerve_growth_factor-like.
DR   InterPro; IPR002072; Nerve_growth_factor-rel.
DR   InterPro; IPR019846; Nerve_growth_factor_CS.
DR   InterPro; IPR045815; NTF3_N.
DR   PANTHER; PTHR11589; NERVE GROWTH FACTOR NGF -RELATED; 1.
DR   PANTHER; PTHR11589:SF4; NEUROTROPHIN-3; 1.
DR   Pfam; PF00243; NGF; 1.
DR   Pfam; PF19338; NTF3_N; 1.
DR   PIRSF; PIRSF001789; NGF; 1.
DR   PRINTS; PR00268; NGF.
DR   SMART; SM00140; NGF; 1.
DR   SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR   PROSITE; PS00248; NGF_1; 1.
DR   PROSITE; PS50270; NGF_2; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685,
KW   ECO:0000256|RuleBase:RU365037};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW   ECO:0000256|RuleBase:RU365037};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU365037};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          131..213
FT                   /note="Nerve growth factor-related"
FT                   /evidence="ECO:0000259|SMART:SM00140"
FT   REGION          37..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAX64230.1"
FT   NON_TER         213
FT                   /evidence="ECO:0000313|EMBL:BAX64230.1"
SQ   SEQUENCE   213 AA;  23924 MW;  9F9FBA2A00E63843 CRC64;
     LAFLSGIQST SMDQRSLSED SMNSFLKTLI QAGIWKNTTP KQGARTKDGV PTAGRKTEAG
     PELTTSQDTK LGLQPVVSLD AEFLRQQRRF SSPRVLLSEN TPLEPPPLYL MEEPLALNRT
     SRRKRYTEGK THRGEYSVCD SESRWVTDKT SAVDIRGHQV TVLGEIRMGP SPVKQYFYET
     RCKQAKPAKS GCRGIDDKHW NSQCKTSQTF VRA
//