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Protein

Dystroglycan

Gene

DAG1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.By similarity
Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells (By similarity).By similarity
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).By similarity

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • laminin binding Source: UniProtKB

GO - Biological processi

Protein family/group databases

MEROPSiS72.001

Names & Taxonomyi

Protein namesi
Recommended name:
Dystroglycan
Alternative name(s):
Dystrophin-associated glycoprotein 1
Cleaved into the following 2 chains:
Alpha-dystroglycan
Short name:
Alpha-DG
Beta-dystroglycan
Short name:
Beta-DG
Gene namesi
Name:DAG1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini654 – 749ExtracellularSequence analysisAdd BLAST96
Transmembranei750 – 775HelicalSequence analysisAdd BLAST26
Topological domaini776 – 895CytoplasmicSequence analysisAdd BLAST120

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000002106130 – 653Alpha-dystroglycanAdd BLAST624
ChainiPRO_0000021062654 – 895Beta-dystroglycanAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi141N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi182 ↔ 264By similarity
Glycosylationi317O-linked (Man6P...) threonineBy similarity1
Glycosylationi319O-linked (Man6P...) threonineBy similarity1
Glycosylationi379O-linked (Man6P...) threonineBy similarity1
Glycosylationi641N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi649N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi661N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi669 ↔ 713By similarity
Modified residuei790PhosphothreonineBy similarity1
Modified residuei892Phosphotyrosine; by SRCBy similarity1

Post-translational modificationi

O- and N-glycosylated (By similarity). POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. 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. In muscle, glycosylation on Thr-317, Thr-319 and Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein amd is required for laminin binding. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated (By similarity).By similarity
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).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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei653 – 654Cleavage; by autolysisBy similarity2
Sitei715 – 716Cleavage; by MMP9By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO18738
PeptideAtlasiO18738
PRIDEiO18738

PTM databases

GlyConnecti39

Expressioni

Tissue specificityi

Expressed in the myelin sheath of peripheral nerves.1 Publication

Interactioni

Subunit structurei

Monomer. 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 LARGE1; the interaction enhances laminin binding (By similarity). Interacts with SGCD. Interacts with AGR2 and AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylation 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. BetaDAG1 directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres (By similarity). Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By similarity). Interacts with POMGNT1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Lama1P191372EBI-8522926,EBI-7176628From Mus musculus.

GO - Molecular functioni

  • laminin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi158770, 4 interactors
IntActiO18738, 4 interactors
MINTiO18738
STRINGi9913.ENSBTAP00000015385

Structurei

3D structure databases

ProteinModelPortaliO18738
SMRiO18738
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini603 – 712Peptidase S72Add BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni30 – 408Required for laminin recognitionBy similarityAdd BLAST379
Regioni49 – 71O-glycosylated at one siteBy similarityAdd BLAST23
Regioni316 – 485Mucin-like domainBy similarityAdd BLAST170
Regioni463 – 485O-glycosylated at seven sites with GalNAcBy similarityAdd BLAST23
Regioni819 – 895Required for interaction with CAV3By similarityAdd BLAST77
Regioni880 – 895Required for binding DMD and UTRNBy similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi776 – 782Nuclear localization signalBy similarity7
Motifi889 – 892PPXY motifBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi809 – 895Pro-richAdd BLAST87

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3781 Eukaryota
ENOG410XQTU LUCA
HOGENOMiHOG000072580
HOVERGENiHBG000078
InParanoidiO18738
KOiK06265

Family and domain databases

Gene3Di2.60.40.10, 2 hits
3.30.70.1040, 1 hit
InterProiView protein in InterPro
IPR027468 Alpha-dystroglycan_domain_2
IPR006644 Cadg
IPR015919 Cadherin-like
IPR008465 DAG1
IPR013783 Ig-like_fold
IPR030398 SEA_DG_dom
PfamiView protein in Pfam
PF05454 DAG1, 1 hit
SMARTiView protein in SMART
SM00736 CADG, 2 hits
SUPFAMiSSF111006 SSF111006, 1 hit
SSF49313 SSF49313, 2 hits
PROSITEiView protein in PROSITE
PS51699 SEA_DG, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O18738-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRMSVGSAVP LPLWGRTFLL LLSVAVTQSH WPSEPSEAVR DWENQLEASM
60 70 80 90 100
HSALSDLHET VPTVVGIPDG TAVVGRSFRV TIPTDLIASN GEVIKVSAAG
110 120 130 140 150
KEALPSWLHW DPQSHTLEGL PLDTDKGVHY ISVSAARLGA NGSHVPQTSS
160 170 180 190 200
VFSIEVYPED HSEPQSLRAA SPDPGEVVSL VCAADEPVTV LTVILDADLT
210 220 230 240 250
KMTPKQRIDL LRRMRGFSEV EPHNMKLVPV VNNRLFDMSA FMAGPGNAKK
260 270 280 290 300
VVENGALLSW KLGCCLNQNS VPDIRGVEVP AREGAMSAQL GYPVVGWHIA
310 320 330 340 350
NKKPSLPKRI RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP
360 370 380 390 400
TETMAPPVRD PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPSQ
410 420 430 440 450
IRPTMTIPGY MEPSTVTTPP TTTTKKPRVS TPRPATPSTD SSTTTTRRPT
460 470 480 490 500
KKPRTSRPVP RVTTKAPITR LETASPATRM RTTTSGVPHG GEPNQRPELK
510 520 530 540 550
NHIDRVDAWV GTYFEVKIPS DTFYDNEDTT TDKLKLTLKL REQQLVGEKS
560 570 580 590 600
WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ
610 620 630 640 650
GDKAPARFKA KLTGDPAAVT NDIHKKIALV KKLAFAFGDR NCSTITLQNI
660 670 680 690 700
TRGSIVVEWT NNTLPLEPCP KEQITALSRR IAEDDGKPRG AFVNALEPDF
710 720 730 740 750
QAMSITVTGS GSCRHLQFVP VAPPMRVPSE APATEVPDRD PEKSSEDDVY
760 770 780 790 800
LHTVIPAVVV AAILLIAGII AMICYRKKRK GKLTLEDQAT FIKKGVPIIF
810 820 830 840 850
ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSMPETT PLNQDTVGEY
860 870 880 890
APLRDEDPSA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP
Length:895
Mass (Da):97,321
Last modified:January 1, 1998 - v1
Checksum:i400213A299630D11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009079 mRNA Translation: BAA23650.1
RefSeqiNP_776587.1, NM_174162.1
UniGeneiBt.88492

Genome annotation databases

GeneIDi281439
KEGGibta:281439

Similar proteinsi

Entry informationi

Entry nameiDAG1_BOVIN
AccessioniPrimary (citable) accession number: O18738
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: May 23, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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