ID Q9GT67_DROME Unreviewed; 649 AA. AC Q9GT67; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 2. DT 24-JAN-2024, entry version 110. 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}; DE Flags: Fragment; GN Name=Dg {ECO:0000313|FlyBase:FBgn0034072}; GN ORFNames=CG18250 {ECO:0000313|FlyBase:FBgn0034072}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAG17399.2}; RN [1] {ECO:0000313|EMBL:AAG17399.2} RP NUCLEOTIDE SEQUENCE. RX PubMed=11018515; DOI=10.1016/S0014-5793(00)02018-4; RA Greener M.J., Roberts R.G.; RT "Conservation of components of the dystrophin complex in Drosophila."; RL FEBS Lett. 482:13-18(2000). RN [2] {ECO:0000313|EMBL:AAG17399.2} RP NUCLEOTIDE SEQUENCE. RA Greener M.J., Roberts R.G.; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. 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}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF277390; AAG17399.2; -; mRNA. DR AlphaFoldDB; Q9GT67; -. DR MEROPS; S72.A01; -. DR EnsemblMetazoa; FBtr0306238; FBpp0297348; FBgn0034072. DR AGR; FB:FBgn0034072; -. DR FlyBase; FBgn0034072; Dg. DR VEuPathDB; VectorBase:FBgn0034072; -. DR GeneTree; ENSGT00390000008429; -. DR HOGENOM; CLU_007629_0_0_1; -. DR Bgee; FBgn0034072; Expressed in musculature of body and 76 other cell types or tissues. DR ExpressionAtlas; Q9GT67; baseline and differential. DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase. DR GO; GO:0016011; C:dystroglycan complex; IDA:FlyBase. DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IPI:FlyBase. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042383; C:sarcolemma; IDA:FlyBase. DR GO; GO:0030315; C:T-tubule; IDA:FlyBase. DR GO; GO:0030018; C:Z disc; IDA:FlyBase. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0043236; F:laminin binding; IBA:GO_Central. DR GO; GO:0008307; F:structural constituent of muscle; ISS:FlyBase. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase. DR GO; GO:0007411; P:axon guidance; IGI:FlyBase. DR GO; GO:0030010; P:establishment of cell polarity; IMP:FlyBase. DR GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:FlyBase. DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IMP:FlyBase. DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase. DR GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:FlyBase. DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase. DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central. DR GO; GO:0016203; P:muscle attachment; IMP:FlyBase. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase. DR GO; GO:0021675; P:nerve development; IBA:GO_Central. DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase. DR GO; GO:0007309; P:oocyte axis specification; IMP:FlyBase. DR GO; GO:0006110; P:regulation of glycolytic process; IGI:FlyBase. DR GO; GO:0060025; P:regulation of synaptic activity; IMP:FlyBase. DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase. DR CDD; cd11303; Dystroglycan_repeat; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. 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:SF21; ALPHA-DYSTROGLYCAN; 1. DR PANTHER; PTHR21559; DYSTROGLYCAN-RELATED; 1. DR Pfam; PF05454; DAG1; 1. DR Pfam; PF05345; He_PIG; 1. DR SMART; SM00736; CADG; 2. DR SUPFAM; SSF49313; Cadherin-like; 2. DR PROSITE; PS51699; SEA_DG; 2. PE 2: Evidence at transcript level; KW Membrane {ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257}; KW Synapse {ECO:0000256|ARBA:ARBA00023018}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 522..546 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 144..251 FT /note="Peptidase S72" FT /evidence="ECO:0000259|PROSITE:PS51699" FT DOMAIN 369..486 FT /note="Peptidase S72" FT /evidence="ECO:0000259|PROSITE:PS51699" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 584..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..33 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAG17399.2" SQ SEQUENCE 649 AA; 72837 MW; 8D9948731C6CCD5B CRC64; ATPTSSVATT TASTPESSSI SSNFVSTDYM EPQPEENSPP IIKTRLQKLA VTSGKAFTFH VLPETFYDAE DQGNLRLALT DKDGHELKAN SWLQFNADKR ELYGLPLDDT VSRWQYRLSA TDSGNASVTE TVEISVQQHR AVRTINHEIS VFVRINEKPG HNIDWQLKLI NAVARTLDDS TNSAVVVREI RQTPHDPHSA TFVYFNETLP TSECPEKELK DIIARLDANR LSDLVQPQLG IKSITGQLIG SCQKDLTQVK PTQHMTKNVP PMPRNQVDRV NASLGQLLVY KVPADTFYDA NDNQLTLTLK TRDHLELSPR HWLQFDSKNE EFYGIPKSGD IGSEEYLLVA EDSGGLSAHD ALVVVVSPAP KRDFGFFFKA YLSIKHERFN ADLQRKFVER VAKLNGDPTT GQIQIRSITT HHDSDGTIVN FYNTTLYRKH NSCREKEVAM TRSVYLNSDL SLREAAKRAL GPELNLTNFS VVPFSICHHT ENIDTNQLDY IPSRPEEPTH KSSFGEDYMI TFVWPIVIIV AMLVAASIIA CCLHWCRQRS GKMELGDEEE RKSFRAKGIP VIFQDEYEEK PEIGNKSPVI LKDEKPPLLP PSYNTSNMNG DNDVDDYVPP PSVVVGGREV RGKSPATPSY RKPPPYVSP //