BDNF_AILFU
ID BDNF_AILFU Reviewed; 247 AA.
AC O97759;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 60.
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 Ailurus fulgens (Lesser panda) (Red panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ailuridae; Ailurus.
OX NCBI_TaxID=9649;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Feng L.;
RT "Giant panda (GP) and lesser panda (LP) BDNF gene sequences and their
RT deduced amino acid sequences.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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; U56639; AAD10843.1; -; Genomic_DNA.
DR AlphaFoldDB; O97759; -.
DR SMR; O97759; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Growth factor; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..247
FT /note="BDNF precursor form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447526"
FT PROPEP 19..128
FT /evidence="ECO:0000250|UniProtKB:P21237"
FT /id="PRO_0000042896"
FT CHAIN 129..247
FT /note="Brain-derived neurotrophic factor"
FT /id="PRO_0000042897"
FT SITE 57..58
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250|UniProtKB:P23560"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..208
FT /evidence="ECO:0000250|UniProtKB:P23560"
FT DISULFID 186..237
FT /evidence="ECO:0000250|UniProtKB:P23560"
FT DISULFID 196..239
FT /evidence="ECO:0000250|UniProtKB:P23560"
SQ SEQUENCE 247 AA; 27870 MW; FE8C62CF1A6C03EE CRC64;
MTILFLTMVI SYFGCMKAAP MKEANVRGQG SLAYTGVRTH GTLESMNGPK AGSRGLTSLA
DTFEHVIEEL LDEDQKVRPN EENNKDADLY TSRVMLSSQV PLEPPLLFLL EEYKNYLDAA
NMSMRVRRHS DPARRGELSV CDSISEWVTA ADKKTAVDMS GGTVTVLEKV PVSKGQLKQY
FYETKCNPMG YTKEGCRGID KRHWNSQCRT TQSYVRALTM DSKKRIGWRF IRIDTSCVCT
LTIKRGR
