ID A0A3Q2G020_CYPVA Unreviewed; 905 AA.
AC A0A3Q2G020;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Dystroglycan 1 {ECO:0000256|ARBA:ARBA00026224};
DE AltName: Full=Dystroglycan {ECO:0000256|ARBA:ARBA00031034};
DE AltName: Full=Dystrophin-associated glycoprotein 1 {ECO:0000256|ARBA:ARBA00030092};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000014580.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000014580.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: The dystroglycan complex is involved in a number of processes
CC including laminin and basement membrane assembly, sarcolemmal
CC stability, cell survival, peripheral nerve myelination, nodal
CC structure, cell migration, and epithelial polarization.
CC {ECO:0000256|ARBA:ARBA00023567}.
CC -!- FUNCTION: Transmembrane protein that plays important roles in
CC connecting the extracellular matrix to the cytoskeleton. Acts as a cell
CC adhesion receptor in both muscle and non-muscle tissues. Receptor for
CC both DMD and UTRN and, through these interactions, scaffolds axin to
CC the cytoskeleton. Also functions in cell adhesion-mediated signaling
CC and implicated in cell polarity. {ECO:0000256|ARBA:ARBA00024991}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004135}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space
CC {ECO:0000256|ARBA:ARBA00004239}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
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DR RefSeq; XP_015256960.1; XM_015401474.1.
DR AlphaFoldDB; A0A3Q2G020; -.
DR STRING; 28743.ENSCVAP00000014580; -.
DR Ensembl; ENSCVAT00000022476.1; ENSCVAP00000014580.1; ENSCVAG00000017262.1.
DR GeneID; 107102255; -.
DR KEGG; cvg:107102255; -.
DR GeneTree; ENSGT00390000008429; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR GO; GO:0016203; P:muscle attachment; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0007525; P:somatic muscle development; IEA:Ensembl.
DR GO; GO:0033292; P:T-tubule organization; IEA:Ensembl.
DR CDD; cd11305; alpha_DG_C; 1.
DR CDD; cd11303; Dystroglycan_repeat; 1.
DR Gene3D; 3.30.70.1040; Dystroglycan, domain 2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR027468; Alpha-dystroglycan_domain_2.
DR InterPro; IPR041631; Alpha_DG1_N2.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008465; DAG1_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR030398; SEA_DG_dom.
DR PANTHER; PTHR21559:SF22; DYSTROGLYCAN 1; 1.
DR PANTHER; PTHR21559; DYSTROGLYCAN-RELATED; 1.
DR Pfam; PF18424; a_DG1_N2; 1.
DR Pfam; PF05454; DAG1; 1.
DR SMART; SM00736; CADG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR SUPFAM; SSF111006; Dystroglycan, domain 2; 1.
DR PROSITE; PS51699; SEA_DG; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 759..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 616..725
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 99354 MW; 829547564C25EC3B CRC64;
MFSKRSVGWL RASRGLSGTS SRTRVWLLGL VFTAISWIPL PASAEVEIDM LGGMVLLDAG
GEGEELGGGG SELEASMHSS LLRDFQEVAE SLRVMDVGEM AAARQETATP TAFPDSSAVV
GRVFQIKVPN KMEDAYLGDI IKVTEMGKDS LPSWLHWDVD SRILRGLPLD EDKGVHYISL
TISNHTKPSS SSTSSSSEVF SIEVHPEDHF DSDSSQLLSN QAAVEDHIQP FTCGNEEPVT
ILTVILDADL TKMNSEQRVE LLENMRSFSG VELQHMKMLP VVNNRLFDMS AFMAGPGNAK
KVVENGALLS WKLGCSLDQT TVPNINSVQD PAKEGTMSAR LGYPVVGWHI ANKKPHVPKR
VRRQLNITPT PILAVLPPTT AVEPPVRIVP TLSSPSIASP TESSAPPVRG PVPLPGKPTN
KIRDPIAHTP TLGPPQPTRV VETTSTVSIQ PTMTRPNYVE ATPTLPTPPK KTTRKPPRRP
KTTPMTPKST TPATSTPSPD VIHDPFNEKP VLRNPIDQVN ALVGTYFEVK IPSDTFFDKE
DGTTDKLRLT LRENHKDVVG DESWIQFNTT SQLLYGLPDV QHIGKHEYYM QAEDKGGLKA
IDAFEVRVKR WPLNDKTPVI FTARFEGEPR MITNNIHKKI LLVKKLAYVL GDRNSSTVSL
RNISKGSIVV EWTNTSLPQH PCPKEILRDM SRTLGDASGK PSQKFKNYMG PEFSPIKVEV
RGKASCRTYS FIPPAEIDIP EPSAVTPGLG SSRDSTDDVY LHTVIPAVVV AAILLIAGII
AMICYRKKRR GKLTIEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKPPLPPPE
YPNMASPETT PLNQELLGEY TALRDEDPNA PPYQPPPPFT TPMEGKGSRP KNMTPYRSPP
PYVPP
//
