DREB_RAT
ID DREB_RAT Reviewed; 707 AA.
AC Q07266; A5D6R1; O70205;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Drebrin;
DE AltName: Full=Developmentally-regulated brain protein;
GN Name=Dbn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Wistar; TISSUE=Brain, and Hippocampus;
RX PubMed=1611026; DOI=10.1097/00001756-199201000-00029;
RA Shirao T., Obata N., Obata K.;
RT "Cloning of drebrin A and induction of neurite-like processes in drebrin-
RT transfected cells.";
RL NeuroReport 3:109-112(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E1).
RA Ren Y., Kawai-Hirai R., Xue Y., Shirao T.;
RT "Study of processes formation in drebrin cDNA transfected fibroblast
RT cells.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E1).
RC TISSUE=Embryonic brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-342 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Actin cytoskeleton-organizing protein that plays a role in
CC the formation of cell projections (By similarity). Required for actin
CC polymerization at immunological synapses (IS) and for the recruitment
CC of the chemokine receptor CXCR4 to IS (By similarity). Plays a role in
CC dendritic spine morphogenesis and organization, including the
CC localization of the dopamine receptor DRD1 to the dendritic spines (By
CC similarity). Involved in memory-related synaptic plasticity in the
CC hippocampus (By similarity). {ECO:0000250|UniProtKB:Q16643,
CC ECO:0000250|UniProtKB:Q9QXS6}.
CC -!- SUBUNIT: Interacts with RUFY (By similarity). Interacts with CXCR4;
CC this interaction is enhanced by antigenic stimulation (By similarity).
CC Interacts (via ADF-H domain) with ZMYND8 (via PHD-type Zinc finger,
CC Bromo and PWWP domains); the interaction leads to sequestering of
CC ZMYND8 in the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q16643,
CC ECO:0000250|UniProtKB:Q9QXS6}.
CC -!- INTERACTION:
CC Q07266; O54857: Pten; NbExp=3; IntAct=EBI-918187, EBI-8074312;
CC Q07266; A8C4G9: Zmynd8; NbExp=9; IntAct=EBI-918187, EBI-9004258;
CC Q07266-1; P61073: CXCR4; Xeno; NbExp=3; IntAct=EBI-8786792, EBI-489411;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16643}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:Q16643}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:Q16643}. Cell junction
CC {ECO:0000250|UniProtKB:Q16643}. Cell projection
CC {ECO:0000250|UniProtKB:Q9QXS6}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9QXS6}. Note=In the absence of antigen, evenly
CC distributed throughout subcortical regions of the T-cell membrane and
CC cytoplasm. In the presence of antigen, distributes to the immunological
CC synapse forming at the T-cell-APC contact area, where it localizes at
CC the peripheral and distal supramolecular activation clusters (SMAC).
CC Colocalized with RUFY3 and F-actin at the transitional domain of the
CC axonal growth cone. {ECO:0000250|UniProtKB:Q16643,
CC ECO:0000250|UniProtKB:Q9QXS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q07266-1; Sequence=Displayed;
CC Name=E1;
CC IsoId=Q07266-2; Sequence=VSP_004201;
CC Name=E2;
CC IsoId=Q07266-3; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Brain neurons.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Drebrins are classified into two forms of the embryonic
CC type (E1 and E2) and one form of the adult type (A). The time course of
CC their appearance are different from each other. Their structures are
CC closely related. Adult rat brain expresses only drebrin A while drebrin
CC E1 or E2 is observed in immature animals.
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DR EMBL; X59267; CAA41957.1; -; mRNA.
DR EMBL; AB015042; BAA28746.1; -; mRNA.
DR EMBL; BC139847; AAI39848.1; -; mRNA.
DR PIR; S60588; S60588.
DR RefSeq; NP_112286.1; NM_031024.1. [Q07266-1]
DR RefSeq; XP_006253719.1; XM_006253657.3.
DR AlphaFoldDB; Q07266; -.
DR SMR; Q07266; -.
DR BioGRID; 249553; 9.
DR IntAct; Q07266; 6.
DR MINT; Q07266; -.
DR STRING; 10116.ENSRNOP00000019569; -.
DR iPTMnet; Q07266; -.
DR PhosphoSitePlus; Q07266; -.
DR SwissPalm; Q07266; -.
DR jPOST; Q07266; -.
DR PaxDb; Q07266; -.
DR PRIDE; Q07266; -.
DR Ensembl; ENSRNOT00000019393; ENSRNOP00000019393; ENSRNOG00000014170. [Q07266-2]
DR GeneID; 81653; -.
DR KEGG; rno:81653; -.
DR UCSC; RGD:70885; rat. [Q07266-1]
DR CTD; 1627; -.
DR RGD; 70885; Dbn1.
DR VEuPathDB; HostDB:ENSRNOG00000014170; -.
DR eggNOG; KOG3655; Eukaryota.
DR GeneTree; ENSGT00940000159431; -.
DR HOGENOM; CLU_013085_3_0_1; -.
DR InParanoid; Q07266; -.
DR OrthoDB; 885776at2759; -.
DR PhylomeDB; Q07266; -.
DR TreeFam; TF318935; -.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:Q07266; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000014170; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q07266; baseline and differential.
DR Genevisible; Q07266; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0032279; C:asymmetric synapse; IDA:RGD.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0044308; C:axonal spine; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:1902737; C:dendritic filopodium; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0005921; C:gap junction; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0044309; C:neuron spine; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0140661; F:cytoskeletal motor inhibitor activity; IDA:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:RGD.
DR GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0010643; P:cell communication by chemical coupling; ISO:RGD.
DR GO; GO:0010644; P:cell communication by electrical coupling; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:RGD.
DR GO; GO:0071481; P:cellular response to X-ray; IEP:RGD.
DR GO; GO:0051220; P:cytoplasmic sequestering of protein; ISS:UniProtKB.
DR GO; GO:0048699; P:generation of neurons; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048286; P:lung alveolus development; IEP:RGD.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:RGD.
DR GO; GO:0098828; P:modulation of inhibitory postsynaptic potential; IMP:RGD.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:RGD.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:RGD.
DR GO; GO:1904113; P:negative regulation of muscle filament sliding; IDA:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0061351; P:neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISS:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:RGD.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0060134; P:prepulse inhibition; IMP:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:RGD.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:RGD.
DR GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR028438; Drebrin.
DR PANTHER; PTHR10829:SF1; PTHR10829:SF1; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Developmental protein; Differentiation;
KW Neurogenesis; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT CHAIN 2..707
FT /note="Drebrin"
FT /id="PRO_0000080010"
FT DOMAIN 3..134
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT REGION 209..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS6"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS6"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16643"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXS6"
FT VAR_SEQ 320..365
FT /note="Missing (in isoform E1)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_004201"
FT CONFLICT 387
FT /note="S -> P (in Ref. 2; BAA28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="L -> R (in Ref. 2; BAA28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> V (in Ref. 2; BAA28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="Missing (in Ref. 3; AAI39848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 77472 MW; B5279BF6EB7B80AA CRC64;
MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN
QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS
VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF
WEQAKKEEEL RKEEERKKAL DARLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ
SLEAEEAKRR LKDQSIFGDQ RDEEEESQMK KSESEVEEAA AIIAQRPDNP REFFRQQERV
ASASGGSCDA PSPFNHRPGR PYCPFIKASD SGPSSSSSSS SSPPRTPFPY ITCHRTPNLS
SSLPCSHLDS HRRMAPTPIP TRSPSDSSTA STPITEQIER ALDEVTSSQP PPPPPPPPPA
QEAQESAPRL DGEEVCKEAK VAAAPQVWAG CAEEPPRAQE PPLLQSSPTE DLMCTESPEQ
AVLAASPEPD ASVTSVADAH AADTIETTTA TTATTIADNV TPAAASLIDL WPGNGEEAST
PQAEPRVPTP PSGAEASLAE VPLLNEAAQE PLPPVGEGCA NLLNFDELPE PPATFCDPEE
EAEGEPLAAS QVLTMPSALE EVDQVLEQEL EPEPHLLTNG ETTQKEGTQQ ASEGYFSQSQ
EEEFAQSEEP CAKAPPPVFY NKPPEIDITC WDADPVPEEE EGFEGGD
