Q62165 (DAG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	893 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Secreted › extracellular space By similarity Ref.13. Beta-dystroglycan: Cell membrane; Single-pass type I membrane protein By similarity. Cytoplasm › cytoskeleton. Nucleus › nucleoplasm. Cell membrane › sarcolemma. Cell junction › synapse › postsynaptic 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 abonormalities, 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 process	Host-virus interaction
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus Postsynaptic cell membrane Secreted Synapse
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NLS-bearing substrate import into nucleus Inferred from electronic annotation. Source: Compara branching involved in salivary gland morphogenesis Inferred from mutant phenotype PubMed 11798066. Source: MGI cytoskeletal anchoring at plasma membrane Inferred from electronic annotation. Source: Compara epithelial tube branching involved in lung morphogenesis Inferred from mutant phenotype PubMed 11798066. Source: MGI membrane protein ectodomain proteolysis Inferred from electronic annotation. Source: Compara microtubule anchoring Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of cell migration Inferred from electronic annotation. Source: Compara negative regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara nerve maturation Inferred from mutant phenotype Ref.12. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from direct assay PubMed 11798066PubMed 9524190. Source: MGI cell junction Inferred from electronic annotation. Source: UniProtKB-KW cell outer membrane Inferred from direct assay Ref.12. Source: UniProtKB contractile ring Inferred from electronic annotation. Source: Compara cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW 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: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lamellipodium Inferred from electronic annotation. Source: Compara 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 postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell sarcolemma Inferred from direct assay PubMed 11115849PubMed 11259414PubMed 9659216. Source: MGI
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro structural constituent of muscle Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Potential

Chain

28 – 651

624

Alpha-dystroglycan

PRO_0000021067

Chain

652 – 893

242

Beta-dystroglycan

PRO_0000021068

Regions

Topological domain

652 – 751

100

Extracellular Potential

Transmembrane

752 – 772

21

Helical; Potential

Topological domain

773 – 893

121

Cytoplasmic Potential

Domain

498 – 731

234

Peptidase S72

Region

28 – 406

379

Required for laminin recognition By similarity

Region

47 – 69

23

O-glycosylated at one site By similarity

Region

314 – 483

170

Mucin-like domain By similarity

Region

461 – 483

23

O-glycosylated at seven sites with GalNAc By similarity

Region

817 – 893

77

Required for interaction with CAV3 By similarity

Region

878 – 893

16

Required for binding DMD and UTRN By similarity

Motif

774 – 780

7

Nuclear localization signal By similarity

Motif

887 – 890

4

PPXY motif By similarity

Compositional bias

316 – 475

160

Pro-rich

Compositional bias

807 – 893

87

Pro-rich

Sites

Site

651 – 652

2

Cleavage; by autolysis By similarity

Site

713 – 714

2

Cleavage; by MMP9 By similarity

Amino acid modifications

Modified residue

890

1

Phosphotyrosine; by SRC By similarity

Glycosylation

139

1

N-linked (GlcNAc...) Potential

Glycosylation

377

1

O-linked (Man6P...) By similarity

Glycosylation

639

1

N-linked (GlcNAc...) Potential

Glycosylation

647

1

N-linked (GlcNAc...) Potential

Glycosylation

659

1

N-linked (GlcNAc...) Potential

Disulfide bond

180 ↔ 262

Ref.7

Disulfide bond

667 ↔ 711

Potential

Experimental info

Mutagenesis

796 – 798

3

IIF → AAA: Complete loss of ANK3-binding.

Mutagenesis

800 – 801

2

DE → AA: Complete loss of ANK3-binding.

Mutagenesis

803 – 804

2

DD → AA: Major reduction in ANK3-binding.

Sequence conflict

448 – 450

3

TKK → SKE in CAA84293. Ref.5

Sequence conflict

599 – 600

2

GD → PH in CAA84293. Ref.5

Sequence conflict

643

1

I → V in CAA60031. Ref.3

Sequence conflict

643

1

I → V in AAC52853. Ref.5

Secondary structure

1

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893

Helix Strand Turn

Details...

Beta strand

68 – 71

4

Beta strand

76 – 79

4

Helix

82 – 85

4

Beta strand

90 – 96

7

Beta strand

99 – 101

3

Beta strand

106 – 109

4

Turn

110 – 113

4

Beta strand

114 – 117

4

Helix

121 – 123

3

Beta strand

125 – 136

12

Beta strand

142 – 157

16

Beta strand

186 – 194

9

Helix

197 – 199

3

Helix

202 – 216

15

Helix

220 – 222

3

Beta strand

224 – 227

4

Beta strand

239 – 243

5

Beta strand

254 – 263

10

Turn

266 – 268

3

Helix

273 – 281

9

Helix

283 – 288

6

Beta strand

292 – 300

9

Sequences

	Sequence		Length	Mass (Da)
	Q62165 [UniParc]. Last modified July 11, 2001. Version 4. Checksum: 59C081EA86AB0AC1	FASTA	893	96,905
	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

References

	« Hide 'large scale' referencesShow '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, 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.
+	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.

IPI

IPI00122273.

PIR

S59630.

RefSeq

NP_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.

UniGene

Mm.7524.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U2C	X-ray	2.30	A	58-303	[»]

DisProt

DP00491.

ProteinModelPortal

Q62165.

SMR

Q62165. Positions 58-303.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q62165. 1 interaction.

MINT

MINT-145749.

Protein family/group databases

MEROPS

S72.001.

PTM databases

PhosphoSite

Q62165.

Proteomic databases

PaxDb

Q62165.

PRIDE

Q62165.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952.
ENSMUST00000166905; ENSMUSP00000128531; ENSMUSG00000039952.
ENSMUST00000171412; ENSMUSP00000130626; ENSMUSG00000039952.

GeneID

13138.

KEGG

mmu:13138.

Organism-specific databases

CTD

1605.

MGI

MGI:101864. Dag1.

Phylogenomic databases

eggNOG

NOG266557.

GeneTree

ENSGT00390000008429.

HOGENOM

HOG000072580.

HOVERGEN

HBG000078.

InParanoid

Q62165.

KO

K06265.

OMA

AMICYRK.

OrthoDB

EOG49S65X.

Gene expression databases

ArrayExpress

Q62165.

Bgee

Q62165.

CleanEx

MM_DAG1.

Genevestigator

Q62165.

GermOnline

ENSMUSG00000039952. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR006644. Cadg.
IPR015919. Cadherin-like.
IPR008465. DAG1.
IPR013783. Ig-like_fold.
[Graphical view]

PANTHER

PTHR21559:SF9. PTHR21559:SF9. 1 hit.

Pfam

PF05454. DAG1. 1 hit.
[Graphical view]

SMART

SM00736. CADG. 2 hits.
[Graphical view]

SUPFAM

SSF49313. Cadherin. 2 hits.

ProtoNet

Search...

Other

ChiTaRS

DAG1. mouse.

EvolutionaryTrace

Q62165.

NextBio

283210.

PMAP-CutDB

Q62165.

SOURCE

Search...

Entry information

Entry name

DAG1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program