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BDNF_MOUSE
ID   BDNF_MOUSE              Reviewed;         249 AA.
AC   P21237; A2AII2; Q8CCH9;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Brain-derived neurotrophic factor {ECO:0000303|PubMed:2369898};
DE            Short=BDNF {ECO:0000303|PubMed:2369898};
DE   Contains:
DE     RecName: Full=BDNF precursor form {ECO:0000305};
DE              Short=ProBDNF {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Bdnf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=2369898; DOI=10.1002/j.1460-2075.1990.tb07423.x;
RA   Hofer M., Pagliusi S.R., Hohn A., Leibrock J., Barde Y.-A.;
RT   "Regional distribution of brain-derived neurotrophic factor mRNA in the
RT   adult mouse brain.";
RL   EMBO J. 9:2459-2464(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28164.1};
RC   TISSUE=Testis {ECO:0000312|EMBL:BAC28164.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 112-121 AND 131-135, SUBUNIT, AND MUTAGENESIS OF
RP   ARG-130.
RX   PubMed=7957235; DOI=10.1111/j.1432-1033.1994.0995b.x;
RA   Kolbeck R., Jungbluth S., Barde Y.-A.;
RT   "Characterisation of neurotrophin dimers and monomers.";
RL   Eur. J. Biochem. 225:995-1003(1994).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8139657; DOI=10.1038/368147a0;
RA   Ernfors P., Lee K.F., Jaenisch R.;
RT   "Mice lacking brain-derived neurotrophic factor develop with sensory
RT   deficits.";
RL   Nature 368:147-150(1994).
RN   [7]
RP   FUNCTION, AND ACTIVATION BY PLG.
RX   PubMed=15486301; DOI=10.1126/science.1100135;
RA   Pang P.T., Teng H.K., Zaitsev E., Woo N.T., Sakata K., Zhen S., Teng K.K.,
RA   Yung W.-H., Hempstead B.L., Lu B.;
RT   "Cleavage of proBDNF by tPA/plasmin is essential for long-term hippocampal
RT   plasticity.";
RL   Science 306:487-491(2004).
RN   [8]
RP   FUNCTION (BDNF PRECURSOR FORM), AND MUTAGENESIS OF VAL-68.
RX   PubMed=17023662; DOI=10.1126/science.1129663;
RA   Chen Z.-Y., Jing D., Bath K.G., Ieraci A., Khan T., Siao C.-J.,
RA   Herrera D.G., Toth M., Yang C., McEwen B.S., Hempstead B.L., Lee F.S.;
RT   "Genetic variant BDNF (Val66Met) polymorphism alters anxiety-related
RT   behavior.";
RL   Science 314:140-143(2006).
RN   [9]
RP   INDUCTION.
RX   PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013;
RA   Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
RA   Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
RT   "p75 neurotrophin receptor is a clock gene that regulates oscillatory
RT   components of circadian and metabolic networks.";
RL   J. Neurosci. 33:10221-10234(2013).
RN   [10]
RP   INTERACTION WITH SORCS2 AND NGFR, AND FUNCTION (BDNF PRECURSOR FORM).
RX   PubMed=24908487; DOI=10.1016/j.neuron.2014.04.022;
RA   Glerup S., Olsen D., Vaegter C.B., Gustafsen C., Sjoegaard S.S., Hermey G.,
RA   Kjolby M., Molgaard S., Ulrichsen M., Boggild S., Skeldal S.,
RA   Fjorback A.N., Nyengaard J.R., Jacobsen J., Bender D., Bjarkam C.R.,
RA   Soerensen E.S., Fuechtbauer E.M., Eichele G., Madsen P., Willnow T.E.,
RA   Petersen C.M., Nykjaer A.;
RT   "SorCS2 regulates dopaminergic wiring and is processed into an apoptotic
RT   two-chain receptor in peripheral glia.";
RL   Neuron 82:1074-1087(2014).
RN   [11]
RP   FUNCTION (BDNF PRECURSOR FORM).
RX   PubMed=27457814; DOI=10.1038/mp.2016.108;
RA   Glerup S., Bolcho U., Moelgaard S., Boeggild S., Vaegter C.B., Smith A.H.,
RA   Nieto-Gonzalez J.L., Ovesen P.L., Pedersen L.F., Fjorback A.N., Kjolby M.,
RA   Login H., Holm M.M., Andersen O.M., Nyengaard J.R., Willnow T.E.,
RA   Jensen K., Nykjaer A.;
RT   "SorCS2 is required for BDNF-dependent plasticity in the hippocampus.";
RL   Mol. Psychiatry 21:1740-1751(2016).
RN   [12]
RP   TISSUE SPECIFICITY, AND INDUCTION BY NERVE INJURY.
RX   PubMed=28111162; DOI=10.1016/j.brainres.2017.01.019;
RA   Sanna M.D., Ghelardini C., Galeotti N.;
RT   "HuD-mediated distinct BDNF regulatory pathways promote regeneration after
RT   nerve injury.";
RL   Brain Res. 1659:55-63(2017).
RN   [13]
RP   FUNCTION (BDNF PRECURSOR FORM), AND MUTAGENESIS OF VAL-68.
RX   PubMed=29909994; DOI=10.1016/j.neuron.2018.05.024;
RA   Giza J.I., Kim J., Meyer H.C., Anastasia A., Dincheva I., Zheng C.I.,
RA   Lopez K., Bains H., Yang J., Bracken C., Liston C., Jing D.,
RA   Hempstead B.L., Lee F.S.;
RT   "The BDNF Val66Met Prodomain Disassembles Dendritic Spines Altering Fear
RT   Extinction Circuitry and Behavior.";
RL   Neuron 99:163-178(2018).
CC   -!- FUNCTION: Important signaling molecule that activates signaling
CC       cascades downstream of NTRK2 (PubMed:27457814). 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
CC       (PubMed:8139657, PubMed:15486301, PubMed:17023662, PubMed:27457814,
CC       PubMed:29909994). {ECO:0000269|PubMed:15486301,
CC       ECO:0000269|PubMed:17023662, ECO:0000269|PubMed:27457814,
CC       ECO:0000269|PubMed:29909994, ECO:0000269|PubMed:8139657}.
CC   -!- FUNCTION: [BDNF precursor form]: Important signaling molecule that
CC       activates signaling cascades downstream of NTRK2 (PubMed:27457814).
CC       Activates signaling cascades via the heterodimeric receptor formed by
CC       NGFR and SORCS2 (PubMed:24908487, PubMed:29909994). Signaling via NGFR
CC       and SORCS2 plays a role in synaptic plasticity and long-term depression
CC       (LTD) (PubMed:27457814). Binding to NGFR and SORCS2 promotes neuronal
CC       apoptosis (PubMed:24908487). Promotes neuronal growth cone collapse
CC       (PubMed:24908487, PubMed:27457814). {ECO:0000269|PubMed:24908487,
CC       ECO:0000269|PubMed:27457814, ECO:0000269|PubMed:29909994}.
CC   -!- SUBUNIT: Monomers and homodimers (PubMed:7957235). Binds to NTRK2/TRKB
CC       (By similarity). Can form heterodimers with other neurotrophin family
CC       members, such as NTF3 and NTF4 (in vitro), but the physiological
CC       relevance of this is not clear (By similarity). BDNF precursor form:
CC       interacts with the heterodimer formed by NGFR and SORCS2. Mature BDNF
CC       has much lower affinity for the heterodimer formed by NGFR and SORCS2
CC       (PubMed:24908487). {ECO:0000250|UniProtKB:P23560,
CC       ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:7957235}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P21237-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P21237-2; Sequence=VSP_060202;
CC   -!- TISSUE SPECIFICITY: Expressed in the dorsal root ganglion and the
CC       spinal cord (at protein level) (PubMed:28111162). Detected in brain,
CC       especially in brain cortex, hippocampus, midbrain and cerebellum
CC       (PubMed:2369898, PubMed:8139657). {ECO:0000269|PubMed:2369898,
CC       ECO:0000269|PubMed:28111162, ECO:0000269|PubMed:8139657}.
CC   -!- INDUCTION: Expression oscillates in a circadian manner in the
CC       suprachiasmatic nucleus (SCN) of the brain (PubMed:23785138). Expressed
CC       at higher levels during the dark period and at lower levels during the
CC       light period (PubMed:23785138). Up-regulated after sciatic nerve injury
CC       (PubMed:28111162). {ECO:0000269|PubMed:23785138,
CC       ECO:0000269|PubMed:28111162}.
CC   -!- PTM: Contrary to mature BDNF, the propeptide is N-glycosylated and
CC       glycosulfated. {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 (By
CC       similarity). Can be converted into mature BDNF by plasmin (PLG)
CC       (PubMed:15486301). {ECO:0000250|UniProtKB:P23560,
CC       ECO:0000269|PubMed:15486301}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice are smaller than wild-type
CC       littermates, and most die during the second week after birth. They
CC       exhibit impaired motor coordination and balance, head bobbing and
CC       tilting, and spinning during perionds of hyperactivity. Mutant mice
CC       display a strongly reduced number of neurons in the dorsal root
CC       ganglion, trigeminal ganglion, mesencephalic trigeminal nucleus,
CC       vestibular ganglion and nodose ganglion. Cell death of vestibular
CC       ganglion neurons is strongly increased 14 days after birth. The number
CC       of facial motor neurons and sympathetic superior cervical ganglion
CC       neurons are not decreased. Mutant mice display defects in the
CC       innervation of the inner ear, but respond to auditory stimuli. Tne
CC       inner ear from mutant mice has fewer nerve fibers that enter the
CC       sacculus, utricle and ampulla of the semicircular ducts, and axons fail
CC       to contact their target cells and terminate in the connective tissue
CC       adjacent to the sensory epithelia of the sacculus.
CC       {ECO:0000269|PubMed:8139657}.
CC   -!- SIMILARITY: Belongs to the NGF-beta family. {ECO:0000305}.
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DR   EMBL; X55573; CAA39159.1; -; mRNA.
DR   EMBL; AK033127; BAC28164.1; -; mRNA.
DR   EMBL; AL732477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034862; AAH34862.1; -; mRNA.
DR   CCDS; CCDS38193.1; -. [P21237-2]
DR   CCDS; CCDS38194.1; -. [P21237-1]
DR   PIR; S12555; S12555.
DR   RefSeq; NP_001041604.1; NM_001048139.1. [P21237-1]
DR   RefSeq; NP_001041606.1; NM_001048141.1. [P21237-1]
DR   RefSeq; NP_001041607.1; NM_001048142.1. [P21237-1]
DR   RefSeq; NP_001272345.1; NM_001285416.1. [P21237-1]
DR   RefSeq; NP_001272346.1; NM_001285417.1. [P21237-1]
DR   RefSeq; NP_001272347.1; NM_001285418.1. [P21237-1]
DR   RefSeq; NP_001272348.1; NM_001285419.1. [P21237-1]
DR   RefSeq; NP_001272349.1; NM_001285420.1. [P21237-1]
DR   RefSeq; NP_001272350.1; NM_001285421.1. [P21237-1]
DR   RefSeq; NP_001272351.1; NM_001285422.1. [P21237-1]
DR   RefSeq; NP_001303239.1; NM_001316310.1. [P21237-1]
DR   AlphaFoldDB; P21237; -.
DR   SMR; P21237; -.
DR   BioGRID; 198334; 3.
DR   DIP; DIP-5724N; -.
DR   IntAct; P21237; 2.
DR   STRING; 10090.ENSMUSP00000057989; -.
DR   GlyGen; P21237; 1 site.
DR   iPTMnet; P21237; -.
DR   PhosphoSitePlus; P21237; -.
DR   PaxDb; P21237; -.
DR   PRIDE; P21237; -.
DR   ProteomicsDB; 265206; -. [P21237-1]
DR   ProteomicsDB; 328451; -.
DR   ABCD; P21237; 2 sequenced antibodies.
DR   Antibodypedia; 4032; 1196 antibodies from 50 providers.
DR   DNASU; 12064; -.
DR   Ensembl; ENSMUST00000053317; ENSMUSP00000057989; ENSMUSG00000048482. [P21237-2]
DR   Ensembl; ENSMUST00000111043; ENSMUSP00000106672; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111044; ENSMUSP00000106673; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111045; ENSMUSP00000106674; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111046; ENSMUSP00000106675; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111047; ENSMUSP00000106676; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111049; ENSMUSP00000106678; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111050; ENSMUSP00000106679; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000111051; ENSMUSP00000106680; ENSMUSG00000048482. [P21237-1]
DR   Ensembl; ENSMUST00000176893; ENSMUSP00000135762; ENSMUSG00000048482. [P21237-1]
DR   GeneID; 12064; -.
DR   KEGG; mmu:12064; -.
DR   UCSC; uc008lme.1; mouse. [P21237-1]
DR   CTD; 627; -.
DR   MGI; MGI:88145; Bdnf.
DR   VEuPathDB; HostDB:ENSMUSG00000048482; -.
DR   eggNOG; ENOG502QRU8; Eukaryota.
DR   GeneTree; ENSGT00390000007725; -.
DR   HOGENOM; CLU_059942_0_0_1; -.
DR   InParanoid; P21237; -.
DR   OMA; YPGMRTH; -.
DR   OrthoDB; 1156054at2759; -.
DR   TreeFam; TF106463; -.
DR   Reactome; R-MMU-9026527; Activated NTRK2 signals through PLCG1.
DR   Reactome; R-MMU-9028731; Activated NTRK2 signals through FRS2 and FRS3.
DR   Reactome; R-MMU-9032759; NTRK2 activates RAC1.
DR   BioGRID-ORCS; 12064; 3 hits in 76 CRISPR screens.
DR   PRO; PR:P21237; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P21237; protein.
DR   Bgee; ENSMUSG00000048482; Expressed in lumbar dorsal root ganglion and 160 other tissues.
DR   ExpressionAtlas; P21237; baseline and differential.
DR   Genevisible; P21237; MM.
DR   GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:SynGO-UCL.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR   GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0043195; C:terminal bouton; ISO:MGI.
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:0005169; F:neurotrophin TRKB receptor binding; ISO:MGI.
DR   GO; GO:0048675; P:axon extension; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0007412; P:axon target recognition; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0048668; P:collateral sprouting; ISO:MGI.
DR   GO; GO:1990708; P:conditioned place preference; ISO:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0097484; P:dendrite extension; IDA:MGI.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; ISO:MGI.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
DR   GO; GO:0014047; P:glutamate secretion; IPI:MGI.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
DR   GO; GO:0048839; P:inner ear development; IMP:MGI.
DR   GO; GO:0007612; P:learning; ISO:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0042490; P:mechanoreceptor differentiation; IGI:MGI.
DR   GO; GO:0007613; P:memory; IBA:GO_Central.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IGI:ARUK-UCL.
DR   GO; GO:0060548; P:negative regulation of cell death; IMP:MGI.
DR   GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:MGI.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IDA:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISO:MGI.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:MGI.
DR   GO; GO:0021675; P:nerve development; IMP:MGI.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; ISO:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:1990138; P:neuron projection extension; ISO:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0008038; P:neuron recognition; IMP:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; IDA:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:2000324; P:positive regulation of glucocorticoid receptor signaling pathway; ISO:MGI.
DR   GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IGI:ARUK-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR   GO; GO:1900122; P:positive regulation of receptor binding; ISO:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI.
DR   GO; GO:0031099; P:regeneration; ISO:MGI.
DR   GO; GO:0030516; P:regulation of axon extension; ISO:MGI.
DR   GO; GO:0048670; P:regulation of collateral sprouting; IGI:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:MGI.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR   GO; GO:0046668; P:regulation of retinal cell programmed cell death; IDA:MGI.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISO:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IDA:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR   GO; GO:0099083; P:retrograde trans-synaptic signaling by neuropeptide, modulating synaptic transmission; IMP:SynGO.
DR   GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR   GO; GO:0061193; P:taste bud development; IMP:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0001657; P:ureteric bud development; IDA:MGI.
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   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..249
FT                   /note="BDNF precursor form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000447536"
FT   PROPEP          19..130
FT                   /evidence="ECO:0000305|PubMed:7957235"
FT                   /id="PRO_0000019635"
FT   CHAIN           131..249
FT                   /note="Brain-derived neurotrophic factor"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000019636"
FT   SITE            59..60
FT                   /note="Cleavage; by MBTPS1"
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        143..210
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        188..239
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   DISULFID        198..241
FT                   /evidence="ECO:0000250|UniProtKB:P23560"
FT   VAR_SEQ         1
FT                   /note="M -> MFHQVRRVM (in isoform 2)"
FT                   /id="VSP_060202"
FT   MUTAGEN         68
FT                   /note="V->M: Reduced hippocampal volume, dendritic
FT                   complexity and context-dependent memory. Decreased density
FT                   of dendritic mushroom spines and synapses. Impaired fear
FT                   extinction. Increased anxiety-related behaviors."
FT                   /evidence="ECO:0000269|PubMed:17023662,
FT                   ECO:0000269|PubMed:29909994"
FT   MUTAGEN         130
FT                   /note="R->K: Forms homodimers processed at L-112 that seem
FT                   more stable than the wild-type."
FT                   /evidence="ECO:0000269|PubMed:7957235"
FT   CONFLICT        232
FT                   /note="F -> L (in Ref. 2; BAC28164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  28123 MW;  90CE1F16BB235C97 CRC64;
     MTILFLTMVI SYFGCMKAAP MKEVNVHGQG NLAYPGVRTH GTLESVNGPR AGSRGLTTTS
     LADTFEHVIE ELLDEDQKVR PNEENHKDAD LYTSRVMLSS QVPLEPPLLF LLEEYKNYLD
     AANMSMRVRR HSDPARRGEL SVCDSISEWV TAADKKTAVD MSGGTVTVLE KVPVSKGQLK
     QYFYETKCNP MGYTKEGCRG IDKRHWNSQC RTTQSYVRAL TMDSKKRIGW RFIRIDTSCV
     CTLTIKRGR
 
 
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