Q9Y048 (DTN1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dystrobrevin-1

Gene names

Name:	dyb-1
ORF Names:	F47G6.1

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in cholinergic transmission and as a functional partner of dystrophin (dys-1), necessary for muscle maintenance. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7
Subunit structure	Component of the dystrophin glycoprotein complex (DGC). Interacts with dys-1 and syntrophin (stn-1) to form the DGC. Ref.3 Ref.5 Ref.7
Subcellular location	Cytoplasm By similarity UniProtKB Q9D2N4.
Tissue specificity	From late embryogenesis to adulthood, expressed in neurons and muscles; particularly strong in the ventral nerve cord and in muscles of the body wall, head pharyngeal, and vulva; weaker in the intestinal muscle (at protein level). Ref.4
Domain	The coiled-coil domain mediates the specific interaction with dys-1. Ref.5
Disruption phenotype	Mutants synergistically exhibit progressive myopathy. In dyb-1;hlh-1 double mutants there is an uncoordinated phenotype associated with some muscle degeneration. Overexpression of dyb-1 in dys-1;hlh-1 double mutants delays, but does not prevent the onset and progression of myopathy. Ref.1
Sequence similarities	Belongs to the dystrophin family. Dystrobrevin subfamily. Ref.1 Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	establishment of synaptic specificity at neuromuscular junction Traceable author statement Ref.4. Source: UniProtKB locomotion Inferred from mutant phenotype. Source: WormBase locomotory behavior Inferred from mutant phenotype Ref.4. Source: WormBase muscle cell homeostasis Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of locomotion Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of synaptic transmission, cholinergic Inferred from mutant phenotype Ref.4. Source: WormBase sarcomere organization Inferred from genetic interaction Ref.4. Source: WormBase synaptic transmission, cholinergic Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell dystrophin-associated glycoprotein complex Inferred from direct assay Ref.3. Source: UniProtKB
Molecular function	acetylcholine transmembrane transporter activity Inferred from mutant phenotype Ref.1. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.5Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
dys-1	Q9TW65	4	EBI-322698,EBI-446952

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 590	590	Dystrobrevin-1		PRO_0000080035
Regions
	Zinc finger	258 – 305	48	ZZ-type
	Region	484 – 490	7	Essential for interaction with dys-1
	Coiled coil	434 – 508	75	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9Y048 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: CA0ACD6D54AEBB2A	FASTA	590	65,427
	10 20 30 40 50 60 MLWSNGGGGP REPSSAPSPD HHRAMHSVPP IVASEMQQLI DEMRLQDFDS IRFATYRAAC 70 80 90 100 110 120 KLRFIQQKTK VHLVDIWNMI EAFRENGLNA LPLHTVIKTS RAELLLTTVF HNLNKRLVAS 130 140 150 160 170 180 QHVDTDVSIS LLLAFLLGAY DKQNTGRLTV FSIKVALATL CAGKLVDKLR YIFSQIADSN 190 200 210 220 230 240 GLMDHIKFTD FLQQILSLTT AVFEAPTFGF SENAVNQCFH KDEKVSLNVF LDTFLSDPCP 250 260 270 280 290 300 PCIMWLPLLH RMASVSNVYH PVVCDACQVR SFTGFRYKCQ RCANYQLCQS CFWRGRTSQN 310 320 330 340 350 360 HSNEHEMKEY SSYKSPTKQL VHSIHKSLQC IPATSTVGDA NIDIFNAKIG GPVSSKPARP 370 380 390 400 410 420 LNLNNIVPAT PTTIRRQHAA TSSADWPTSP VLLPGQASHG GVIDDEHKLI ARYAAKLSGR 430 440 450 460 470 480 ADYPLSNGRS MNSSMVGDER TLIAQLEEEN SMMVREMARL ESQTTSDDGL AGLRDRKMEL 490 500 510 520 530 540 EEKMFEMQQR RRELMMQLEH LMAQLNTGPQ PSGGVSSASL SQLPFTASDQ QLTGVNSTVA 550 560 570 580 590 NAFRAGSLPA TSLQGDLLHA ADQITTNMSD LVRQLDLAQS DENGVTINGF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dystrobrevin- and dystrophin-like mutants display similar phenotypes in the nematode Caenorhabditis elegans." Gieseler K., Bessou C., Segalat L. Neurogenetics 2:87-90(1999) [PubMed: 10369883] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE. Strain: Bristol N2.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[3]	"In vitro interactions of Caenorhabditis elegans dystrophin with dystrobrevin and syntrophin." Gieseler K., Abdel-Dayem M., Segalat L. FEBS Lett. 461:59-62(1999) [PubMed: 10561496] [Abstract] Cited for: INTERACTION WITH STN-1 AND DYS-1.
[4]	"Molecular, genetic and physiological characterisation of dystrobrevin-like (dyb-1) mutants of Caenorhabditis elegans." Gieseler K., Mariol M.-C., Bessou C., Migaud M., Franks C.J., Holden-Dye L., Segalat L. J. Mol. Biol. 307:107-117(2001) [PubMed: 11243807] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]	"Dystrobrevin requires a dystrophin-binding domain to function in Caenorhabditis elegans." Grisoni K., Gieseler K., Segalat L. Eur. J. Biochem. 269:1607-1612(2002) [PubMed: 11895430] [Abstract] Cited for: FUNCTION, INTERACTION WITH DYS-1.
[6]	"Overexpression of dystrobrevin delays locomotion defects and muscle degeneration in a dystrophin-deficient Caenorhabditis elegans." Gieseler K., Grisoni K., Mariol M.-C., Segalat L. Neuromuscul. Disord. 12:371-377(2002) [PubMed: 12062255] [Abstract] Cited for: FUNCTION.
[7]	"The stn-1 syntrophin gene of C.elegans is functionally related to dystrophin and dystrobrevin." Grisoni K., Gieseler K., Mariol M.-C., Martin E., Carre-Pierrat M., Moulder G., Barstead R., Segalat L. J. Mol. Biol. 332:1037-1046(2003) [PubMed: 14499607] [Abstract] Cited for: FUNCTION, INTERACTION WITH STN-1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ131742 mRNA. Translation: CAA10498.1. FO081322 Genomic DNA. Translation: CCD70779.1.
RefSeq	NP_490860.1. NM_058459.4.
UniGene	Cel.19602.
3D structure databases
ProteinModelPortal	Q9Y048.
SMR	Q9Y048. Positions 6-313.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-25663N.
IntAct	Q9Y048. 26 interactions.
MINT	MINT-1039894.
STRING	Q9Y048.
Proteomic databases
PRIDE	Q9Y048.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	F47G6.1; F47G6.1; F47G6.1.
GeneID	171715.
KEGG	cel:F47G6.1.
NMPDR	fig|6239.3.peg.240.
UCSC	F47G6.1. c. elegans.
Organism-specific databases
CTD	171715.
WormBase	F47G6.1; CE26812; WBGene00001115; dyb-1.
Phylogenomic databases
eggNOG	meNOG04762.
GeneTree	EMGT00050000000918.
HOGENOM	HBG378857.
InParanoid	Q9Y048.
OMA	DSIRFAT.
PhylomeDB	Q9Y048.
Gene expression databases
ArrayExpress	Q9Y048.
Family and domain databases
InterPro	IPR017432. Distrobrevin. IPR011992. EF-hand-like_dom. IPR015153. EF-hand_dom_typ1. IPR015154. EF-hand_dom_typ2. IPR000433. Znf_ZZ. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF09068. efhand_1. 1 hit. PF09069. efhand_2. 1 hit. PF00569. ZZ. 1 hit. [Graphical view]
PIRSF	PIRSF038204. Distrobrevin. 1 hit.
SMART	SM00291. ZnF_ZZ. 1 hit. [Graphical view]
PROSITE	PS01357. ZF_ZZ_1. 1 hit. PS50135. ZF_ZZ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	872407.

Entry information

Entry name

DTN1_CAEEL

Accession

Primary (citable) accession number: Q9Y048
Secondary accession number(s): Q9TZI6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	November 1, 1999
Last modified:	December 14, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project