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Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)]

 DAG1_CANLF              Reviewed;         892 AA.
Q9TSZ6;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 112.
RecName: Full=Dystroglycan;
AltName: Full=Dystrophin-associated glycoprotein 1;
Contains:
RecName: Full=Alpha-dystroglycan;
Short=Alpha-DG;
Contains:
RecName: Full=Beta-dystroglycan;
Short=Beta-DG;
Flags: Precursor;
Name=DAG1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10720570; DOI=10.1101/gr.10.3.295;
Leeb T., Neumann S., Deppe A., Breen M., Brenig B.;
"Genomic organization of the dog dystroglycan gene DAG1 locus on
chromosome 20q15.1-q15.2.";
Genome Res. 10:295-301(2000).
-!- 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. {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q14118, ECO:0000250|UniProtKB:Q28685,
ECO:0000250|UniProtKB:Q62165}.
-!- SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular
space {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane,
sarcolemma {ECO:0000250}. Cell junction, synapse, postsynaptic
cell membrane {ECO:0000250}. 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 the presence of ANK2 (By
similarity). In peripheral nerves, localizes to the Schwann cell
membrane. Colocalizes with ERM proteins in Schwann-cell microvilli
(By similarity). {ECO:0000250}.
-!- PTM: 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-314, Thr-316 and Thr-376 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). {ECO:0000250|UniProtKB:Q14118}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
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EMBL; AJ012166; CAB62568.1; -; Genomic_DNA.
RefSeq; NP_001029164.1; NM_001033992.1.
RefSeq; XP_005632375.1; XM_005632318.2.
RefSeq; XP_005632376.1; XM_005632319.2.
UniGene; Cfa.33142; -.
ProteinModelPortal; Q9TSZ6; -.
SMR; Q9TSZ6; -.
STRING; 9615.ENSCAFP00000016488; -.
MEROPS; S72.001; -.
PaxDb; Q9TSZ6; -.
PRIDE; Q9TSZ6; -.
Ensembl; ENSCAFT00000017810; ENSCAFP00000016488; ENSCAFG00000011207.
GeneID; 476623; -.
KEGG; cfa:476623; -.
CTD; 1605; -.
VGNC; VGNC:39763; DAG1.
eggNOG; KOG3781; Eukaryota.
eggNOG; ENOG410XQTU; LUCA.
GeneTree; ENSGT00390000008429; -.
HOGENOM; HOG000072580; -.
HOVERGEN; HBG000078; -.
InParanoid; Q9TSZ6; -.
KO; K06265; -.
OMA; AMICYRK; -.
OrthoDB; EOG091G05R9; -.
TreeFam; TF328370; -.
Reactome; R-CFA-3000178; ECM proteoglycans.
Reactome; R-CFA-5173105; O-linked glycosylation.
Reactome; R-CFA-9010553; Regulation of expression of SLITs and ROBOs.
Proteomes; UP000002254; Chromosome 20.
Bgee; ENSCAFG00000011207; -.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0070938; C:contractile ring; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0016011; C:dystroglycan complex; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0051393; F:alpha-actinin binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
GO; GO:0017166; F:vinculin binding; IEA:Ensembl.
GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:Ensembl.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
GO; GO:0034453; P:microtubule anchoring; IEA:Ensembl.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:Ensembl.
GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0021682; P:nerve maturation; IEA:Ensembl.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IEA:Ensembl.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0010470; P:regulation of gastrulation; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.30.70.1040; -; 1.
InterPro; IPR027468; Alpha-dystroglycan_domain_2.
InterPro; IPR006644; Cadg.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR008465; DAG1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR030398; SEA_DG_dom.
Pfam; PF05454; DAG1; 1.
SMART; SM00736; CADG; 2.
SUPFAM; SSF111006; SSF111006; 1.
SUPFAM; SSF49313; SSF49313; 2.
PROSITE; PS51699; SEA_DG; 1.
3: Inferred from homology;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Disulfide bond; Glycoprotein; Membrane; Nucleus;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Secreted; Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 650 Alpha-dystroglycan.
/FTId=PRO_0000021063.
CHAIN 651 892 Beta-dystroglycan.
/FTId=PRO_0000021064.
TOPO_DOM 28 750 Extracellular. {ECO:0000255}.
TRANSMEM 751 771 Helical. {ECO:0000255}.
TOPO_DOM 772 892 Cytoplasmic. {ECO:0000255}.
DOMAIN 600 709 Peptidase S72.
REGION 30 405 Required for laminin recognition.
{ECO:0000250}.
REGION 46 68 O-glycosylated at one site.
{ECO:0000250}.
REGION 313 482 Mucin-like domain. {ECO:0000250}.
REGION 460 482 O-glycosylated at seven sites with
GalNAc. {ECO:0000250}.
REGION 816 892 Required for interaction with CAV3.
{ECO:0000250}.
REGION 877 892 Required for binding DMD and UTRN.
{ECO:0000250}.
MOTIF 773 779 Nuclear localization signal.
{ECO:0000250}.
MOTIF 886 889 PPXY motif. {ECO:0000250}.
COMPBIAS 806 892 Pro-rich.
SITE 650 651 Cleavage; by autolysis. {ECO:0000250}.
SITE 712 713 Cleavage; by MMP9. {ECO:0000250}.
MOD_RES 787 787 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14118}.
MOD_RES 889 889 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 O-linked (Man6P...) threonine.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 316 316 O-linked (Man6P...) threonine.
{ECO:0000250|UniProtKB:Q14118}.
CARBOHYD 376 376 O-linked (Man6P...) threonine.
{ECO:0000250}.
CARBOHYD 638 638 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 658 658 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 179 261 {ECO:0000250|UniProtKB:Q14118}.
DISULFID 666 710 {ECO:0000250|UniProtKB:Q14118}.
SEQUENCE 892 AA; 97192 MW; 0228FAFD471CD5F3 CRC64;
MRMSAGLSLL LPLWGRTFLL LLSVAMAQSH WPSEAGRDWE NQLEASMHSV LSDLHEAVPT
VVGIPDGIAV VGRSFRVTIP MDLIASNGEL VKVSAVGKEV LPSWLHWDPQ SHTLEGLPLD
TDKGVHYISV SATRLGANGS HVPQTSSVFS IEVYPEDHSE PQSVRAASPD PAEVVSSACA
ADEPVTVLTV ILDADLTKMT PKQRIDLLHR MRSFSEVELH NMKLVPVVNN RLFDMSAFMA
GPGNAKKVVE NGALLSWKLG CSLNQNNVPD IHGVEAPARE GAMSAQLGYP VVGWHIANKK
PPIPKRIRRQ IHATPTPVTA IGPPTTAIQE PPSRIVPTPT SPAIAPPTET MAPPVRDPVP
GKPTVTIRTR GAIIQTPTLG PIQPTRVSEA GTTVPGQIRP TMTIPGYVEP TAVATPPTTT
TKKPRVSTPK PATPSTDSST TTTRRPTKKP RTPRPVPRVT TKAPITRLET ASPPTRIRTT
TSGVPRGGEP NQRPELKNHI DRVDAWVGTY FEVKIPSDTF YDHEDTTTDK LKLTLKLREQ
QLVGEKSWVQ FNSNSQLMYG LPDSSHVGKH EYFMHATDKG GLSAVDAFEI HVHKRPQGDR
APARFKAKFM GDPVPVVNDI HKKISLVKKL AFAFGDRNCS TITLQNITRG SILVEWTNNT
LPLEPCPKEQ IMALSQRIAE DNGKPRAAFS NALEPDFQAS SIAVTGSGSC RHLQFIPVAP
PRRVPSEVPS TDVPDRDPEK SSEDDVYLHT VIPAVVVAAI LLIAGIIAMI CYRKKRKGKL
TLEDQATFIK KGVPIIFADE LDDSKPPPSS SMPLILQEEK APLPPPEYPN QSVPETTPLN
QDTVGEYTPL REEDPNAPPY QPPPPFTAPM EGKGSRPKNM TPYRSPPPYV PP


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