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Q62165 (DAG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dystroglycan
Alternative name(s):
Dystrophin-associated glycoprotein 1

Cleaved into the following 2 chains:

  1. Alpha-dystroglycan
    Short name=Alpha-DG
  2. Beta-dystroglycan
    Short name=Beta-DG
Gene names
Name:Dag1
Synonyms:Dag-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. Ref.1 Ref.11 Ref.12

Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses. Ref.1 Ref.11 Ref.12

Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity By similarity. Ref.1 Ref.11 Ref.12

Subunit structure

Monomer By similarity. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex. Interacts (via the N-terminal of alphaDAG1) with LARGE; the interaction enhances laminin binding By similarity. Interacts with AGR2 and AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylaion on the PPXY motif. Interacts (betaDAG1, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (betaDAG1, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts (betaDAG1) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD By similarity. Interacts with SGCD. BetaDAG1 directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres. Ref.8 Ref.9 Ref.13

Subcellular location

Alpha-dystroglycan: Secretedextracellular space By similarity Ref.13.

Beta-dystroglycan: Cell membrane; Single-pass type I membrane protein By similarity. Cytoplasmcytoskeleton. Nucleusnucleoplasm. Cell membranesarcolemma. Cell junctionsynapsepostsynaptic cell membrane. Note: The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli. Ref.13

Tissue specificity

Expressed in a variety of tissues. In brain, expressed in the hippocampal formation, the olfactory bulb, the cerebellum and the thalamus. In the peripheral nerve system, expressed in Schwann cells. Ref.1 Ref.5 Ref.11

Developmental stage

Broadly expressed in late embryonic and early postnatal cerebellar neurons, including premigratory granule neurons of the external granule cell layer, but expression is largely down-regulated. Weak expression in Purkinje cells throughout development. Alpha- and beta-DG proteins are also present on the Bergmann glial scaffolds used by granule cells during early postnatal radial migration. In the peripheral nerve system, expression briefly precedes and parallels myelination. First expressed at E18.5 in spinal roots, dorsal root ganglions and nerve trunks. At P1, at the onset of myelination, expressed in motor roots. At P5 and P15, expression progressively increases in sensory roots and peripheral nerves. Between postnatal 2 weeks and 18 months, localizes at the nodes of Ranvier as well as at the Schwann cell outer membrane. Ref.10 Ref.11 Ref.12

Post-translational modification

O- and N-glycosylated By similarity. Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated By similarity. In muscle, glycosylation on Thr-379 by a phosphorylated O-mannosyl glycan (N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE) protein amd is required for laminin binding. O-mannosylation is also required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses. Ref.9

Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa By similarity.

SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry By similarity.

Disruption phenotype

Homozygous null mice embryos exhibit gross developmental abnormalities, beginning around 6.5 days of gestation, in the Reichert's membrane, an extraembryonic basement membrane. In peripheral nerves, ablation of DAG1 from 4 week-old mice causes abnormalities in nerve structure and function including mildly impaired sorting of axons, dysmyelination, axonal loss and aberrant nerve conduction. Laminin-binding is lost and there is disruption of the Schwann cell dystroglycan complex. Ref.1 Ref.12

Sequence similarities

Contains 1 peptidase S72 domain.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
Postsynaptic cell membrane
Secreted
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNLS-bearing protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

Schwann cell development

Inferred from mutant phenotype Ref.12. Source: UniProtKB

basement membrane organization

Inferred from mutant phenotype PubMed 23217742. Source: MGI

branching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 11798066. Source: MGI

calcium-dependent cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

commissural neuron axon guidance

Inferred from mutant phenotype PubMed 23217742. Source: MGI

cytoskeletal anchoring at plasma membrane

Inferred from electronic annotation. Source: InterPro

epithelial tube branching involved in lung morphogenesis

Inferred from mutant phenotype PubMed 11798066. Source: MGI

membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

microtubule anchoring

Inferred from electronic annotation. Source: Ensembl

modulation by virus of host morphology or physiology

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial sheet

Inferred from mutant phenotype PubMed 11798066. Source: MGI

myelination in peripheral nervous system

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

nerve maturation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 11798066PubMed 23217742PubMed 9524190. Source: MGI

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell outer membrane

Inferred from direct assay Ref.12. Source: UniProtKB

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

contractile ring

Inferred from electronic annotation. Source: Ensembl

costamere

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

dystroglycan complex

Inferred from direct assay PubMed 11798066. Source: MGI

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 23217742. Source: MGI

membrane raft

Inferred from direct assay PubMed 11259414. Source: MGI

node of Ranvier

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 10988290PubMed 11430802PubMed 14627610. Source: MGI

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay PubMed 11115849PubMed 11259414PubMed 9659216. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

structural constituent of muscle

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EgflamQ4VBE42EBI-2025154,EBI-2025048

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 651624Alpha-dystroglycan
PRO_0000021067
Chain652 – 893242Beta-dystroglycan
PRO_0000021068

Regions

Topological domain652 – 751100Extracellular Potential
Transmembrane752 – 77221Helical; Potential
Topological domain773 – 893121Cytoplasmic Potential
Domain601 – 710110Peptidase S72
Region28 – 406379Required for laminin recognition By similarity
Region47 – 6923O-glycosylated at one site By similarity
Region314 – 483170Mucin-like domain By similarity
Region461 – 48323O-glycosylated at seven sites with GalNAc By similarity
Region817 – 89377Required for interaction with CAV3 By similarity
Region878 – 89316Required for binding DMD and UTRN By similarity
Motif774 – 7807Nuclear localization signal By similarity
Motif887 – 8904PPXY motif By similarity
Compositional bias316 – 475160Pro-rich
Compositional bias807 – 89387Pro-rich

Sites

Site651 – 6522Cleavage; by autolysis By similarity
Site713 – 7142Cleavage; by MMP9 By similarity

Amino acid modifications

Modified residue8901Phosphotyrosine; by SRC By similarity
Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation3771O-linked (Man6P...) By similarity
Glycosylation6391N-linked (GlcNAc...) Potential
Glycosylation6471N-linked (GlcNAc...) Potential
Glycosylation6591N-linked (GlcNAc...) Potential
Disulfide bond180 ↔ 262 Ref.7 Ref.15
Disulfide bond667 ↔ 711 By similarity

Experimental info

Mutagenesis796 – 7983IIF → AAA: Complete loss of ANK3-binding.
Mutagenesis800 – 8012DE → AA: Complete loss of ANK3-binding.
Mutagenesis803 – 8042DD → AA: Major reduction in ANK3-binding.
Sequence conflict448 – 4503TKK → SKE in CAA84293. Ref.5
Sequence conflict599 – 6002GD → PH in CAA84293. Ref.5
Sequence conflict6431I → V in CAA60031. Ref.3
Sequence conflict6431I → V in AAC52853. Ref.5

Secondary structure

........................................... 893
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q62165 [UniParc].

Last modified July 11, 2001. Version 4.
Checksum: 59C081EA86AB0AC1

FASTA89396,905
        10         20         30         40         50         60 
MSVDNWLLHP LWGQTFLLLL SVAVAQAHWP SEPSEAVRDW KNQLEASMHS VLSDFQEAVP 

        70         80         90        100        110        120 
TVVGIPDGTA VVGRSFRVSI PTDLIASSGE IIKVSAAGKE ALPSWLHWDP HSHILEGLPL 

       130        140        150        160        170        180 
DTDKGVHYIS VSAARLGANG SHVPQTSSVF SIEVYPEDHN EPQSVRAASS DPGEVVPSAC 

       190        200        210        220        230        240 
AADEPVTVLT VILDADLTKM TPKQRIDLLN RMQSFSEVEL HNMKLVPVVN NRLFDMSAFM 

       250        260        270        280        290        300 
AGPGNAKKVV ENGALLSWKL GCSLNQNSVP DIRGVETPAR EGAMSAQLGY PVVGWHIANK 

       310        320        330        340        350        360 
KPTLPKRLRR QIHATPTPVT AIGPPTTAIQ EPPSRIVPTP TSPAIAPPTE TMAPPVRDPV 

       370        380        390        400        410        420 
PGKPTVTIRT RGAIIQTPTL GPIQPTRVSE AGTTVPGQIR PTLTIPGYVE PTAVITPPTT 

       430        440        450        460        470        480 
TTKKPRVSTP KPATPSTDSS TTTTRRPTKK PRTPRPVPRV TTKAPITRLE TASPPTRIRT 

       490        500        510        520        530        540 
TTSGVPRGGE PNQRPELKNH IDRVDAWVGT YFEVKIPSDT FYDNEDTTTD KLKLTLKLRE 

       550        560        570        580        590        600 
QQLVGEKSWV QFNSNSQLMY GLPDSSHVGK HEYFMHATDK GGLSAVDAFE IHVHKRPQGD 

       610        620        630        640        650        660 
KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR GSIVVEWTNN 

       670        680        690        700        710        720 
TLPLEPCPKE QIIGLSRRIA DENGKPRPAF SNALEPDFKA LSIAVTGSGS CRHLQFIPVA 

       730        740        750        760        770        780 
PPSPGSSAAP ATEVPDRDPE KSSEDDVYLH TVIPAVVVAA ILLIAGIIAM ICYRKKRKGK 

       790        800        810        820        830        840 
LTLEDQATFI KKGVPIIFAD ELDDSKPPPS SSMPLILQEE KAPLPPPEYP NQSMPETTPL 

       850        860        870        880        890 
NQDTVGEYTP LRDEDPNAPP YQPPPPFTAP MEGKGSRPKN MTPYRSPPPY VPP 

« Hide

References

« Hide 'large scale' references
[1]"Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice."
Williamson R.A., Henry M.D., Daniels K.J., Hrstka R.F., Lee J.C., Sunada Y., Ibraghimov-Beskrovnaya O., Campbell K.P.
Hum. Mol. Genet. 6:831-841(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
Strain: 129/SvJ.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]"Cloning and sequencing of mouse skeletal muscle alpha-dystroglycan."
Brancaccio A., Ruegg M.A., Engel J.
Matrix Biol. 14:681-685(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-650.
Tissue: Skeletal muscle.
[4]Brancaccio A.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 142-143.
[5]"Dystroglycan: brain localisation and chromosome mapping in the mouse."
Gorecki D.C., Derry J.M.J., Barnard E.A.
Hum. Mol. Genet. 3:1589-1597(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-650, TISSUE SPECIFICITY.
Strain: C57BL/10.
Tissue: Skeletal muscle.
[6]"Cloning and expression analyses of mouse dystroglycan gene: specific expression in maternal decidua at the peri-implantation stage."
Yotsumoto S., Fujiwara H., Horton J.H., Mosby T.A., Wang X., Cui Y., Ko M.S.H.
Hum. Mol. Genet. 5:1259-1267(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 620-893.
Strain: C57BL/6J.
Tissue: Decidua.
[7]"A single disulfide bridge (Cys182-Cys264) is crucial for alpha-dystroglycan N-terminal domain stability."
Brancaccio A., Jeno P., Engel J.
Ann. N. Y. Acad. Sci. 857:228-231(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[8]"Molecular organization of sarcoglycan complex in mouse myotubes in culture."
Chan Y.-M., Boennemann C.G., Lidov H.G.W., Kunkel L.M.
J. Cell Biol. 143:2033-2044(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGCD.
[9]"The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation."
Ilsley J.L., Sudol M., Winder S.J.
Cell. Signal. 13:625-632(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH DMD.
[10]"Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar development."
Henion T.R., Qu Q., Smith F.I.
Brain Res. Mol. Brain Res. 112:177-181(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[11]"Expression of laminin receptors in schwann cell differentiation: evidence for distinct roles."
Previtali S.C., Nodari A., Taveggia C., Pardini C., Dina G., Villa A., Wrabetz L., Quattrini A., Feltri M.L.
J. Neurosci. 23:5520-5530(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION.
[12]"Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization."
Saito F., Moore S.A., Barresi R., Henry M.D., Messing A., Ross-Barta S.E., Cohn R.D., Williamson R.A., Sluka K.A., Sherman D.L., Brophy P.J., Schmelzer J.D., Low P.A., Wrabetz L., Feltri M.L., Campbell K.P.
Neuron 38:747-758(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, LIGAND-BINDING.
[13]"An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan."
Ayalon G., Davis J.Q., Scotland P.B., Bennett V.
Cell 135:1189-1200(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANK3, SUBCELLULAR LOCATION, MUTAGENESIS OF 796-ILE--PHE-798; 800-ASP-GLU-801 AND 803-ASP-ASP-804.
[14]"O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding."
Yoshida-Moriguchi T., Yu L., Stalnaker S.H., Davis S., Kunz S., Madson M., Oldstone M.B., Schachter H., Wells L., Campbell K.P.
Science 327:88-92(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES, LIGAND-BINDING, ADENOVIRUS BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture."
Bozic D., Sciandra F., Lamba D., Brancaccio A.
J. Biol. Chem. 279:44812-44816(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 58-303 IN COMPLEX WITH LIGAND, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48854 Genomic DNA. Translation: AAA99779.2.
BC007150 mRNA. Translation: AAH07150.1.
X86073 mRNA. Translation: CAA60031.1.
Z34532 mRNA. Translation: CAA84293.1.
U43512 mRNA. Translation: AAC52853.1.
PIRS59630.
RefSeqNP_001263410.1. NM_001276481.1.
NP_001263411.1. NM_001276482.1.
NP_001263414.1. NM_001276485.1.
NP_001263415.1. NM_001276486.1.
NP_001263421.1. NM_001276492.1.
NP_001263422.1. NM_001276493.1.
NP_001263423.1. NM_001276494.1.
NP_034147.1. NM_010017.4.
XP_006511699.1. XM_006511636.1.
UniGeneMm.491797.
Mm.7524.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2CX-ray2.30A58-303[»]
DisProtDP00491.
ProteinModelPortalQ62165.
SMRQ62165. Positions 58-303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199048. 7 interactions.
IntActQ62165. 4 interactions.
MINTMINT-145749.

Protein family/group databases

MEROPSS72.001.

PTM databases

PhosphoSiteQ62165.

Proteomic databases

PaxDbQ62165.
PRIDEQ62165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952.
ENSMUST00000166905; ENSMUSP00000128531; ENSMUSG00000039952.
ENSMUST00000171412; ENSMUSP00000130626; ENSMUSG00000039952.
GeneID13138.
KEGGmmu:13138.
UCSCuc009rox.1. mouse.

Organism-specific databases

CTD1605.
MGIMGI:101864. Dag1.

Phylogenomic databases

eggNOGNOG266557.
GeneTreeENSGT00390000008429.
HOGENOMHOG000072580.
HOVERGENHBG000078.
InParanoidQ62165.
KOK06265.
OMAAMICYRK.
OrthoDBEOG7KSX82.
PhylomeDBQ62165.
TreeFamTF328370.

Gene expression databases

ArrayExpressQ62165.
BgeeQ62165.
CleanExMM_DAG1.
GenevestigatorQ62165.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
3.30.70.1040. 1 hit.
InterProIPR027468. Alpha-dystroglycan_domain_2.
IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERPTHR21559:SF9. PTHR21559:SF9. 1 hit.
PfamPF05454. DAG1. 1 hit.
[Graphical view]
SMARTSM00736. CADG. 2 hits.
[Graphical view]
SUPFAMSSF111006. SSF111006. 1 hit.
SSF49313. SSF49313. 2 hits.
PROSITEPS51699. SEA_DG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDAG1. mouse.
EvolutionaryTraceQ62165.
NextBio283210.
PMAP-CutDBQ62165.
PROQ62165.
SOURCESearch...

Entry information

Entry nameDAG1_MOUSE
AccessionPrimary (citable) accession number: Q62165
Secondary accession number(s): Q61094, Q61141, Q61497
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: April 16, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot