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BDNF_BOVIN
ID   BDNF_BOVIN              Reviewed;         250 AA.
AC   Q95106; Q32KY2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Brain-derived neurotrophic factor;
DE            Short=BDNF;
DE   Contains:
DE     RecName: Full=BDNF precursor form {ECO:0000305};
DE              Short=ProBDNF {ECO:0000305};
DE   Flags: Precursor;
GN   Name=BDNF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-250.
RX   PubMed=9034318; DOI=10.1016/s0378-1119(96)00635-x;
RA   Arab S.F., Krohn K., Lachmund A., Unsicker K., Suter-Crazzolara C.;
RT   "The gene encoding bovine brain-derived neurotrophic factor (BDNF).";
RL   Gene 185:95-98(1997).
CC   -!- FUNCTION: Important signaling molecule that activates signaling
CC       cascades downstream of NTRK2 (By similarity). During development,
CC       promotes the survival and differentiation of selected neuronal
CC       populations of the peripheral and central nervous systems. Participates
CC       in axonal growth, pathfinding and in the modulation of dendritic growth
CC       and morphology. Major regulator of synaptic transmission and plasticity
CC       at adult synapses in many regions of the CNS. The versatility of BDNF
CC       is emphasized by its contribution to a range of adaptive neuronal
CC       responses including long-term potentiation (LTP), long-term depression
CC       (LTD), certain forms of short-term synaptic plasticity, as well as
CC       homeostatic regulation of intrinsic neuronal excitability (By
CC       similarity). {ECO:0000250|UniProtKB:P21237,
CC       ECO:0000250|UniProtKB:P23560}.
CC   -!- FUNCTION: [BDNF precursor form]: Important signaling molecule that
CC       activates signaling cascades downstream of NTRK2. Activates signaling
CC       cascades via the heterodimeric receptor formed by NGFR and SORCS2.
CC       Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and
CC       long-term depression (LTD). Binding to NGFR and SORCS2 promotes
CC       neuronal apoptosis. Promotes neuronal growth cone collapse.
CC       {ECO:0000250|UniProtKB:P21237}.
CC   -!- SUBUNIT: Monomers and homodimers (By similarity). Binds to NTRK2/TRKB.
CC       Can form heterodimers with other neurotrophin family members, such as
CC       NTF3 and NTF4 (in vitro), but the physiological relevance of this is
CC       not clear (By similarity). BDNF precursor form: interacts with the
CC       heterodimer formed by NGFR and SORCS2. Mature BDNF has much lower
CC       affinity for the heterodimer formed by NGFR and SORCS2 (By similarity).
CC       {ECO:0000250|UniProtKB:P21237, ECO:0000250|UniProtKB:P23560}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23560}.
CC   -!- SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted
CC       {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted
CC       as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}.
CC   -!- PTM: [BDNF precursor form]: N-glycosylated and glycosulfated, contrary
CC       to mature BDNF. {ECO:0000250|UniProtKB:P23560}.
CC   -!- PTM: Mature BDNF is produced by proteolytic removal of the propeptide,
CC       catalyzed by a FURIN family member. In addition, the precursor form is
CC       proteolytically cleaved within the propeptide, but this is not an
CC       obligatory intermediate for the production of mature BDNF. Can be
CC       converted into mature BDNF by plasmin (PLG).
CC       {ECO:0000250|UniProtKB:P23560}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; BC109860; AAI09861.1; -; mRNA.
DR   EMBL; X97914; CAA66488.1; -; Genomic_DNA.
DR   PIR; JC6183; JC6183.
DR   RefSeq; NP_001040072.1; NM_001046607.2.
DR   RefSeq; XP_005216392.1; XM_005216335.3.
DR   RefSeq; XP_005216393.1; XM_005216336.3.
DR   AlphaFoldDB; Q95106; -.
DR   SMR; Q95106; -.
DR   STRING; 9913.ENSBTAP00000010694; -.
DR   PaxDb; Q95106; -.
DR   Ensembl; ENSBTAT00000010694; ENSBTAP00000010694; ENSBTAG00000008134.
DR   GeneID; 617701; -.
DR   KEGG; bta:617701; -.
DR   CTD; 627; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008134; -.
DR   VGNC; VGNC:26461; BDNF.
DR   eggNOG; ENOG502QRU8; Eukaryota.
DR   GeneTree; ENSGT00390000007725; -.
DR   HOGENOM; CLU_059942_0_0_1; -.
DR   InParanoid; Q95106; -.
DR   OMA; YPGMRTH; -.
DR   OrthoDB; 1156054at2759; -.
DR   TreeFam; TF106463; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000008134; Expressed in oocyte and 68 other tissues.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005163; F:nerve growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR   GO; GO:0007613; P:memory; IBA:GO_Central.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
DR   GO; GO:0021675; P:nerve development; IBA:GO_Central.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; IBA:GO_Central.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; IBA:GO_Central.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:1900122; P:positive regulation of receptor binding; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR020430; Brain-der_neurotrophic_factor.
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   PANTHER; PTHR11589; PTHR11589; 1.
DR   PANTHER; PTHR11589:SF3; PTHR11589:SF3; 1.
DR   Pfam; PF00243; NGF; 1.
DR   PIRSF; PIRSF001789; NGF; 1.
DR   PRINTS; PR01912; BDNFACTOR.
DR   PRINTS; PR00268; NGF.
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   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..250
FT                   /note="BDNF precursor form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000447528"
FT   PROPEP          19..131
FT                   /evidence="ECO:0000250|UniProtKB:P21237"
FT                   /id="PRO_0000019625"
FT   CHAIN           132..250
FT                   /note="Brain-derived neurotrophic factor"
FT                   /id="PRO_0000019626"
FT   SITE            57..58
FT                   /note="Cleavage; by MBTPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        144..211
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        189..240
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        199..242
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   CONFLICT        33
FT                   /note="A -> T (in Ref. 2; CAA66488)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157..158
FT                   /note="KT -> RL (in Ref. 2; CAA66488)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   250 AA;  28174 MW;  08C15E90F0BD4FE1 CRC64;
     MTILFLTMVI SYFGCMKAAP MKEANLRAQG SLAYPGVRTH GTLESMNGPK VGSRGLTSSS
     SLADTFEHVI EELLDEDQKV RPSEENNKDA DMYTSRVMLS SQVPLEPPLL FLLEEYKNYL
     DAANMSMRVR RHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL
     KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC
     VCTLTIKRGR
 
 
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