ID Q9GT67_DROME Unreviewed; 649 AA. AC Q9GT67; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2002, sequence version 2. DT 11-DEC-2019, entry version 92. DE SubName: Full=Dystroglycan-like protein DG {ECO:0000313|EMBL:AAG17399.2}; 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; Holometabola; 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 --------------------------------------------------------------------------- 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 MEROPS; S72.A01; -. DR PRIDE; Q9GT67; -. DR FlyBase; FBgn0034072; Dg. DR eggNOG; KOG3781; Eukaryota. DR eggNOG; ENOG410XQTU; LUCA. DR OrthoDB; 299349at2759; -. DR Bgee; FBgn0034072; Expressed in 58 organ(s), highest expression level in embryo. DR GO; GO:0009925; C:basal plasma membrane; IDA:FlyBase. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0016011; C:dystroglycan complex; IDA:FlyBase. DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IPI:FlyBase. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. 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:0008307; F:structural constituent of muscle; ISS:FlyBase. DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:FlyBase. DR GO; GO:0007411; P:axon guidance; IGI:FlyBase. DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; ISS: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:0016203; P:muscle attachment; IMP:FlyBase. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase. 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:1903798; P:regulation of production of miRNAs involved in gene silencing by miRNA; IDA:FlyBase. DR GO; GO:0060025; P:regulation of synaptic activity; IMP:FlyBase. DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase. DR Gene3D; 2.60.40.10; -; 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 Pfam; PF05454; DAG1; 1. DR SMART; SM00736; CADG; 2. DR SUPFAM; SSF49313; SSF49313; 2. DR PROSITE; PS51699; SEA_DG; 2. PE 2: Evidence at transcript level; KW Membrane {ECO:0000256|SAM:Phobius}; 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" 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 //