ID A0A195C6Y8_9HYME Unreviewed; 1291 AA.
AC A0A195C6Y8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, 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};
GN ORFNames=ALC62_12906 {ECO:0000313|EMBL:KYM96400.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM96400.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYM96400.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYM96400.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM96400.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) 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}. 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 EMBL; KQ978219; KYM96400.1; -; Genomic_DNA.
DR RefSeq; XP_018402404.1; XM_018546902.1.
DR RefSeq; XP_018402405.1; XM_018546903.1.
DR RefSeq; XP_018402406.1; XM_018546904.1.
DR STRING; 456900.A0A195C6Y8; -.
DR GeneID; 108779464; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
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 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; 3.
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:SF21; DYSTROGLYCAN 1; 1.
DR PANTHER; PTHR21559; DYSTROGLYCAN-RELATED; 1.
DR Pfam; PF18424; a_DG1_N2; 1.
DR Pfam; PF05454; DAG1; 2.
DR SMART; SM00736; CADG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 3.
DR SUPFAM; SSF111006; Dystroglycan, domain 2; 1.
DR PROSITE; PS51699; SEA_DG; 2.
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:UP000078542};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1291
FT /note="Dystroglycan 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008269858"
FT TRANSMEM 1152..1177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 766..881
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT DOMAIN 1009..1121
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 49..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1291 AA; 143721 MW; C51658EC5D3ED4EB CRC64;
MKKHPYILAC VLLLLPLSLG LSLQEDDLVF DDVGEDNDND NVPVGSVLIN HHSSHGRSDR
YEHGSRDGRR HGSRVERAWG VPDSVVPVGH IFRMKIPRQA FSGSVDFYEV HETADRDRLP
QWMHWDDAVF TLLGVPSKKD MGNYHLSVTA VGKHHDTAKD QFVVQVIPEK LEELKHKDGK
THCDDGEDQT ILTILLDARM DQLSPTIRVN AIENLAGFLG MHTSAFSMHS QSIKDVTALD
SSVIFTGPGN VRHHKNKESH LTTIQWQVGC DGHLWKHQTE LVKQLREQAK DGTLAEVLQL
PVLSWRVRTD LNSFLRNRRE TGSGDYGDSD DYGGYDDDYD GDYDEENEED DNDDNLGVSP
TYVPDSKHPH RHHHGEETIG WKGEDIDGQE IIPRMSQSEL ENKTTTTTRT TELTTSSPST
TTTTSTTTTT TTTQATPTTV TSTSSTTTTI TSADITATAS ISTAVAPSIE SPRSETTDEE
SSTEKTKPVE PAEPVTVLPT IPSDITTTPP PATTLPPFST SATQTSVFDK IETEIVGITN
VTTEESEQTT TSMKEPTTVP TFIVTDVKTT TTTPSPAVIT NVSASTIIPV IVTNETTTMP
STSDLRTTIS STTPSTTSTT ISTTSTTTTT TTTAAPTTTT TTTTARITTE SIEYGQANFP
PRRDRRLKKI PVTAGKPLSY VIPADTFTDL EDGNTRSLKL SLYWQGVPLK TTHWLQFNHH
TQEVYGLPLE NDISTWNYEL VAMDREGANV TDSLDIHVQQ HKLSRSVNHE FSIYLKIDKR
IEFPTDVDWE LEVIRSLAEL YGDRDTQHIT VRSIDINTDR EQAIFIWTND SLPRSSECPR
EHINRLLRVL IDSDGDPSAS LKAVLAPEIR VKRVVFQGIG QCEDMNRPEI PKVSTEEPKV
NFPPVPRNQV DHVNATVGQL LVFKVPEDTF FDAEDGSSRN MKMSLLTIDR RPIPSYEWLQ
FDSKNQEFYG VPMITDIGRK EYQLVVVDKE GASATDGLVV VVHSAPPMAH TVEFSMTLDI
SYDSFAHSAL QKRNFIEKLR DLYGDRDTNA ILLHNISNGS TVITWHNRTL PTSYCAHDEV
NRLRSVLVKS DNDRRSVTDE VLDVMGLKFP VKQITVIPMG ICLGELTGVH SPDSHVPPVD
DSTSVGAFHD DYLLTFVLPA IIIAAMLILA GIIACVLHKR RRSGKMSVSE QDDERQSFRN
KGIPVIFQDE LEEKPDPGNK SPVILKEEKP PLPPPEYQKT EDGADVPMLP KENSEEPYQP
PPPFATNRDT NRQNRPKPTP TYRKPPPYVP P
//