DTN1_CAEEL
ID DTN1_CAEEL Reviewed; 590 AA.
AC Q9Y048; Q9TZI6;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Dystrobrevin-1;
GN Name=dyb-1 {ECO:0000312|WormBase:F47G6.1}; ORFNames=F47G6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA10498.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10369883};
RX PubMed=10369883; DOI=10.1007/s100480050057;
RA Gieseler K., Bessou C., Segalat L.;
RT "Dystrobrevin- and dystrophin-like mutants display similar phenotypes in
RT the nematode Caenorhabditis elegans.";
RL Neurogenetics 2:87-90(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP INTERACTION WITH STN-1 AND DYS-1.
RX PubMed=10561496; DOI=10.1016/s0014-5793(99)01421-0;
RA Gieseler K., Abdel-Dayem M., Segalat L.;
RT "In vitro interactions of Caenorhabditis elegans dystrophin with
RT dystrobrevin and syntrophin.";
RL FEBS Lett. 461:59-62(1999).
RN [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11243807; DOI=10.1006/jmbi.2000.4480;
RA Gieseler K., Mariol M.-C., Bessou C., Migaud M., Franks C.J.,
RA Holden-Dye L., Segalat L.;
RT "Molecular, genetic and physiological characterisation of dystrobrevin-like
RT (dyb-1) mutants of Caenorhabditis elegans.";
RL J. Mol. Biol. 307:107-117(2001).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH DYS-1.
RX PubMed=11895430; DOI=10.1046/j.1432-1327.2002.02780.x;
RA Grisoni K., Gieseler K., Segalat L.;
RT "Dystrobrevin requires a dystrophin-binding domain to function in
RT Caenorhabditis elegans.";
RL Eur. J. Biochem. 269:1607-1612(2002).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=12062255; DOI=10.1016/s0960-8966(01)00330-3;
RA Gieseler K., Grisoni K., Mariol M.-C., Segalat L.;
RT "Overexpression of dystrobrevin delays locomotion defects and muscle
RT degeneration in a dystrophin-deficient Caenorhabditis elegans.";
RL Neuromuscul. Disord. 12:371-377(2002).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH STN-1.
RX PubMed=14499607; DOI=10.1016/j.jmb.2003.08.021;
RA Grisoni K., Gieseler K., Mariol M.-C., Martin E., Carre-Pierrat M.,
RA Moulder G., Barstead R., Segalat L.;
RT "The stn-1 syntrophin gene of C.elegans is functionally related to
RT dystrophin and dystrobrevin.";
RL J. Mol. Biol. 332:1037-1046(2003).
CC -!- FUNCTION: Plays a role in cholinergic transmission and as a functional
CC partner of dystrophin (dys-1), necessary for muscle maintenance.
CC {ECO:0000269|PubMed:10369883, ECO:0000269|PubMed:11243807,
CC ECO:0000269|PubMed:11895430, ECO:0000269|PubMed:12062255,
CC ECO:0000269|PubMed:14499607}.
CC -!- SUBUNIT: Component of the dystrophin glycoprotein complex (DGC).
CC Interacts with dys-1 and syntrophin (stn-1) to form the DGC.
CC {ECO:0000269|PubMed:10561496, ECO:0000269|PubMed:11895430,
CC ECO:0000269|PubMed:14499607}.
CC -!- INTERACTION:
CC Q9Y048; Q9TW65: dys-1; NbExp=4; IntAct=EBI-322698, EBI-446952;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: From late embryogenesis to adulthood, expressed in
CC neurons and muscles; particularly strong in the ventral nerve cord and
CC in muscles of the body wall, head pharyngeal, and vulva; weaker in the
CC intestinal muscle (at protein level). {ECO:0000269|PubMed:11243807}.
CC -!- DOMAIN: The coiled-coil domain mediates the specific interaction with
CC dys-1. {ECO:0000269|PubMed:11895430}.
CC -!- DISRUPTION PHENOTYPE: Mutants synergistically exhibit progressive
CC myopathy. In dyb-1 and hlh-1 double mutants, there is an uncoordinated
CC phenotype associated with some muscle degeneration. Overexpression of
CC dyb-1 in dys-1 and hlh-1 double mutants delays, but does not prevent
CC the onset and progression of myopathy. {ECO:0000269|PubMed:10369883}.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000269|PubMed:10369883}.
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DR EMBL; AJ131742; CAA10498.1; -; mRNA.
DR EMBL; FO081322; CCD70779.1; -; Genomic_DNA.
DR RefSeq; NP_490860.1; NM_058459.5.
DR AlphaFoldDB; Q9Y048; -.
DR SMR; Q9Y048; -.
DR BioGRID; 37210; 37.
DR DIP; DIP-25663N; -.
DR IntAct; Q9Y048; 26.
DR STRING; 6239.F47G6.1; -.
DR iPTMnet; Q9Y048; -.
DR EPD; Q9Y048; -.
DR PaxDb; Q9Y048; -.
DR PeptideAtlas; Q9Y048; -.
DR EnsemblMetazoa; F47G6.1a.1; F47G6.1a.1; WBGene00001115.
DR GeneID; 171715; -.
DR KEGG; cel:CELE_F47G6.1; -.
DR UCSC; F47G6.1; c. elegans.
DR CTD; 171715; -.
DR WormBase; F47G6.1; CE26812; WBGene00001115; dyb-1.
DR eggNOG; KOG4301; Eukaryota.
DR HOGENOM; CLU_011676_1_0_1; -.
DR InParanoid; Q9Y048; -.
DR OMA; HSAGCSM; -.
DR OrthoDB; 699158at2759; -.
DR PhylomeDB; Q9Y048; -.
DR PRO; PR:Q9Y048; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001115; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9Y048; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016014; C:dystrobrevin complex; IPI:WormBase.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015870; P:acetylcholine transport; IMP:UniProtKB.
DR GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; TAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:WormBase.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:UniProtKB.
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 Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..590
FT /note="Dystrobrevin-1"
FT /id="PRO_0000080035"
FT ZN_FING 259..315
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..490
FT /note="Essential for interaction with dys-1"
FT COILED 434..508
FT /evidence="ECO:0000255"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 590 AA; 65427 MW; CA0ACD6D54AEBB2A CRC64;
MLWSNGGGGP REPSSAPSPD HHRAMHSVPP IVASEMQQLI DEMRLQDFDS IRFATYRAAC
KLRFIQQKTK VHLVDIWNMI EAFRENGLNA LPLHTVIKTS RAELLLTTVF HNLNKRLVAS
QHVDTDVSIS LLLAFLLGAY DKQNTGRLTV FSIKVALATL CAGKLVDKLR YIFSQIADSN
GLMDHIKFTD FLQQILSLTT AVFEAPTFGF SENAVNQCFH KDEKVSLNVF LDTFLSDPCP
PCIMWLPLLH RMASVSNVYH PVVCDACQVR SFTGFRYKCQ RCANYQLCQS CFWRGRTSQN
HSNEHEMKEY SSYKSPTKQL VHSIHKSLQC IPATSTVGDA NIDIFNAKIG GPVSSKPARP
LNLNNIVPAT PTTIRRQHAA TSSADWPTSP VLLPGQASHG GVIDDEHKLI ARYAAKLSGR
ADYPLSNGRS MNSSMVGDER TLIAQLEEEN SMMVREMARL ESQTTSDDGL AGLRDRKMEL
EEKMFEMQQR RRELMMQLEH LMAQLNTGPQ PSGGVSSASL SQLPFTASDQ QLTGVNSTVA
NAFRAGSLPA TSLQGDLLHA ADQITTNMSD LVRQLDLAQS DENGVTINGF
