ID A0A3B3CXS2_ORYME Unreviewed; 872 AA.
AC A0A3B3CXS2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000021964.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000021964.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B3CXS2; -.
DR STRING; 30732.ENSOMEP00000021964; -.
DR PaxDb; 30732-ENSOMEP00000021964; -.
DR Ensembl; ENSOMET00000015984.1; ENSOMEP00000021964.1; ENSOMEG00000001249.1.
DR GeneTree; ENSGT00390000008429; -.
DR OMA; WRLGCSL; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000261560; 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 Pfam; PF05345; He_PIG; 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 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 726..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 583..692
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 361..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..812
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 95482 MW; AB159489B06713DD CRC64;
MCNKLNEERR RASRGLHLTP SRTRVLALGL VLAAAGWLPP LALAQVEIDV LGGNGLEASM
SSSLLSGFKE VTESLQSLKE PTAFPDSSAM VGRIFQIKLP NKVENSFTGE IVQITEMGKN
SLPAWLHWDS ESRILQGLPL EKDKGIHYIS VSISNQTKAT STEVFSIEVH PEDHLDADSA
QMVSNQASAE DDLQPFMCEA EEPVTVLTVI LDADLTKMSS EQRVELMDKM RSFSGVGLHH
MRMLPVVNNR LFDMSAFMAG PGNAKKVVEN GALLSWKLGC SLDQSTVPNL DSVQGPAKEG
TMSTKLGYPV VGWHIANKKP GVPKRVRRQL NNTPTPILAV VPPATAVEPP VRVVPTLSSP
SIAAPTESFA PPIRGPVPLP GKPTPRVHEP TLHTPTMDPP LPTKVMETTS TIQPTGTRPI
YVEATATPTP STKKPPRKQK KPKSTPVPKV PSKSSTTKPP RRTTPPPSIS SDPSNEPPVL
RNAIDRVYAL VGTYFEVKIP SDTFFDIEDG TTDKLRLTLK QNHDKVVEDG SWIQFNTTSQ
LLYGLPDLEQ VGEHVYYLHA TDKGGRFTVD AFEVYVSNWP QNKIPVIFKA RFVGEPRSLK
NDIHKKILLV KKLAYALGDR NSSTVSLTKI EKGSILVEWT NTSLQQKPCP KEQLAIMSRA
LADASGNPSQ AFRYTMEPEF RTINVTVKGT GSCAKYSFIP PEEYDPMPSI TRAPDLGSSR
GSTDDVYLHT VIPAVVVAAI LLIAGVIAMI CYRKKRKGKL TIEDQATFIK KGVPIIFADE
LDDSKPPPSS SMPLILQEEK PPLPPPEYPN MATPETTPLN QELLGEYTAL KDEDPNAPPY
QPPPPFATPM EGKGSRPKNM TPYRSPPPYV PP
//
