DTNB_RAT
ID DTNB_RAT Reviewed; 654 AA.
AC P84060; Q66HF4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dystrobrevin beta {ECO:0000305};
DE Short=DTN-B {ECO:0000250|UniProtKB:O60941};
DE AltName: Full=Beta-dystrobrevin {ECO:0000250|UniProtKB:O60941};
GN Name=Dtnb {ECO:0000312|RGD:1309579};
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 350-451.
RC STRAIN=Sprague-Dawley {ECO:0000269|PubMed:8889548};
RC TISSUE=Embryo {ECO:0000269|PubMed:8889548};
RX PubMed=8889548; DOI=10.1101/gr.6.9.791;
RA Bonaldo M.F., Lennon G., Soares M.B.;
RT "Normalization and subtraction: two approaches to facilitate gene
RT discovery.";
RL Genome Res. 6:791-806(1996).
RN [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH DMD AND
RP UTRN.
RX PubMed=10545507; DOI=10.1083/jcb.147.3.645;
RA Blake D.J., Hawkes R., Benson M.A., Beesley P.W.;
RT "Different dystrophin-like complexes are expressed in neurons and glia.";
RL J. Cell Biol. 147:645-658(1999).
RN [4]
RP INTERACTION WITH KIF5A.
RX PubMed=14600269; DOI=10.1242/jcs.00805;
RA Macioce P., Gambara G., Bernassola M., Gaddini L., Torreri P., Macchia G.,
RA Ramoni C., Ceccarini M., Petrucci T.C.;
RT "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain.";
RL J. Cell Sci. 116:4847-4856(2003).
RN [5]
RP INTERACTION WITH OLFM1.
RX PubMed=17265465; DOI=10.1002/jnr.21186;
RA Veroni C., Grasso M., Macchia G., Ramoni C., Ceccarini M., Petrucci T.C.,
RA Macioce P.;
RT "beta-dystrobrevin, a kinesin-binding receptor, interacts with the
RT extracellular matrix components pancortins.";
RL J. Neurosci. Res. 85:2631-2639(2007).
RN [6]
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: Scaffolding protein that assembles DMD and SNTA1 molecules to
CC the basal membrane of kidney cells and liver sinusoids. May function as
CC a repressor of the SYN1 promoter through the binding of repressor
CC element-1 (RE-1), in turn regulates SYN1 expression and may be involved
CC in cell proliferation regulation during the early phase of neural
CC differentiation. May be required for proper maturation and function of
CC a subset of inhibitory synapses. {ECO:0000250|UniProtKB:O70585}.
CC -!- SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins
CC SNTG1 and SNTG2 (By similarity). Binds DTNBP1 (By similarity). Forms a
CC specific complex composed of DMD, SNTB2 and SNTA1 in neuron; the
CC interaction with SNTB2 and SNTA1 is DMD independent (PubMed:10545507).
CC Interacts with UTRN and dystrophin short form DP71 in the kidney and
CC liver (PubMed:10545507). Interacts with SNTB1, SNTB2 and SNTA1 in
CC kidney and liver. Interacts with KIF5A (PubMed:14600269). Interacts
CC with HMG20A and HMG20B (By similarity). Interacts with OLFM1
CC (PubMed:17265465). Interacts with PRKAR2B and PRKAR1A (By similarity).
CC {ECO:0000250|UniProtKB:O60941, ECO:0000250|UniProtKB:O70585,
CC ECO:0000269|PubMed:10545507, ECO:0000269|PubMed:14600269,
CC ECO:0000269|PubMed:17265465}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O70585}.
CC Postsynaptic density {ECO:0000269|PubMed:10545507}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:O70585}. Basal cell membrane
CC {ECO:0000250|UniProtKB:O70585}. Postsynapse
CC {ECO:0000250|UniProtKB:O70585}. Nucleus {ECO:0000250|UniProtKB:O70585}.
CC Note=Localized at inhibitory synapses on the dendrites of cerebellar
CC Purkinje cells. {ECO:0000250|UniProtKB:O70585}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons. In the isocortex, expressed
CC most prominently in the somata (including the nuclei) and the dendrites
CC of the pyramidal cells. Expressed in the hippocampus CA1, CA2, and CA3
CC neurons, namely in the initial segments of dendrites. Expressed in the
CC Purkinje cells, molecular layer interneurons, and granule cells of
CC cerebellum. Expressed in axon fascicles associated with the spinal
CC trigeminal tract and in the internal capsule in the brainstem.
CC {ECO:0000269|PubMed:10545507}.
CC -!- DOMAIN: The coiled coil domain may mediate the interaction with
CC dystrophin. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKA. Phosphorylation at Thr-11 alters the
CC interaction with KIF5A. {ECO:0000250|UniProtKB:O70585}.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000250|UniProtKB:O70585}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC081889; AAH81889.1; -; mRNA.
DR EMBL; AA899479; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001012191.1; NM_001012191.1.
DR AlphaFoldDB; P84060; -.
DR SMR; P84060; -.
DR BioGRID; 263662; 5.
DR CORUM; P84060; -.
DR IntAct; P84060; 1.
DR STRING; 10116.ENSRNOP00000057536; -.
DR iPTMnet; P84060; -.
DR PhosphoSitePlus; P84060; -.
DR PaxDb; P84060; -.
DR PRIDE; P84060; -.
DR GeneID; 362715; -.
DR KEGG; rno:362715; -.
DR CTD; 1838; -.
DR RGD; 1309579; Dtnb.
DR VEuPathDB; HostDB:ENSRNOG00000011914; -.
DR eggNOG; KOG4301; Eukaryota.
DR InParanoid; P84060; -.
DR OMA; HSAGCSM; -.
DR OrthoDB; 699158at2759; -.
DR PhylomeDB; P84060; -.
DR PRO; PR:P84060; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000011914; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; P84060; baseline and differential.
DR Genevisible; P84060; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0060077; C:inhibitory synapse; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017432; Distrobrevin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038204; Distrobrevin; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Membrane; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Synapse; Zinc; Zinc-finger.
FT CHAIN 1..654
FT /note="Dystrobrevin beta"
FT /id="PRO_0000086880"
FT ZN_FING 238..294
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 399..448
FT /note="Syntrophin-binding region"
FT /evidence="ECO:0000250"
FT REGION 520..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..519
FT /evidence="ECO:0000255"
FT COMPBIAS 541..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60941"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60941"
FT MOD_RES 424
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70585"
SQ SEQUENCE 654 AA; 73878 MW; AC0A98AE9E0A7234 CRC64;
MIEEGGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE
AFRDNGLNTL DHATEISVSR LETVISSIYY QLNKRLPSTH QINVEQSISL LLNFMIAAYD
SEGRGKLTVF SVKAMLATMC GGKMLDKLRY IFSQMSDSNG LMMFGKLDQF LKEALKLPTA
VFEGPSFGYT EHAVRTCFPQ QKKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP
VECSYCHCES MMGFRYRCQQ CHNYQLCQNC FWRGHAGGPH SNQHQMKELS SWKSPAKKLS
HAISKSLGCV PSREPPHPVF PEQPEKPLDL AHIVPPRPLT NMNDTMVSHM SSGVPTPTKR
LQYGQDMPNL LADEHALIAS YVARLQHCTR VLDSPSRLDE EHRLIARYAA RLAAEAGNMT
RPPTDASFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPTLLA
ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EGLMKLLKAQ ATGSPHTSPT HGGGRSMPMP
VRSTSAGSTP THGPQDSLSG VGGDVQEAFA QGTRRNLRND LLVAADSITN TMSSLVKELH
SGETQRFPLV SSSPSCPLPC PTIPTHSPSF HATFPSRNTR DLHPVPPSHM VSLY
