ID A0A0V0VBU7_9BILA Unreviewed; 785 AA.
AC A0A0V0VBU7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=T09_12504 {ECO:0000313|EMBL:KRX61004.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61004.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX61004.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX61004.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX61004.1}.
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; JYDN01000052; KRX61004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VBU7; -.
DR STRING; 181606.A0A0V0VBU7; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; cd11303; Dystroglycan_repeat; 1.
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; DYSTROGLYCAN 1; 1.
DR PANTHER; PTHR21559; DYSTROGLYCAN-RELATED; 1.
DR Pfam; PF05454; DAG1; 1.
DR SMART; SM00736; CADG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR PROSITE; PS51699; SEA_DG; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Signal {ECO:0000256|SAM:SignalP}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..785
FT /note="Dystroglycan 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006870729"
FT TRANSMEM 619..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 471..580
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 283..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 87461 MW; 4056D45469A80190 CRC64;
MALLLFLFLL VAVLATSSHA QYGLPDAVAN VGRLFNYDLP NLDPATKFHQ FSEIGGDGLP
PWLEWDKKES TLAGVPMVND NGPMYIAVKF ANGSRDVFAI DVRDPDEPCD STTTGTVERV
YAVLPMDVNL DQLLPTERVL LMKLANRRWS TVVRTGQLTL GNWRFFKTAQ RIWSNADPLK
PDLSIQDSEA VFYWTVACQM PLKANETKLI AQLAQQTQNT PTEKMQFLLP DFNKKITIKG
LLLVKWEISN FRTKRQFDDD YSRYLASRFG HARFTTELYP QTTTTRRPFT FPPRRPPVQS
IRPTSRIDYG STTATTTSPT TSRFTATLRP VTTDRESPKI EVHLTRTTPT VTTSPFKLDE
NSRPKVQKSL GTVVCYKGIV CEVRIPDDTF YDREDGSTVM LELSLSALDG GNKSHSDWIY
LDKLDRTLYG LNLNTGQWQY SLTATDSAGS AVSDAFAIQV VEPSHETDHA HYNHLFTVTL
SEQLDKLSVH PTTLVKLVSK LAEFFGDLSP SAIVVRSLKS GSTVLEWSNG TLFDSACPRS
DIGKLTSKMR RKGGGVKSDF YRFMKPEFTV TDVDVAFHGA CSDDASRMKS DDEKEDEEEE
IPMVLAQPEE GGNALMSTVL PAIIIIVLLV IAGVIACLYY RRSRSTAKKH EEVEKKFLSK
GTPIIFPDEV DGDEECTATS PMLLKEDKPP TPMTELSSFQ PTSLNGSSTP KSTKANNSTN
SYAEVRKQPA TTTATSSDDG SCPRITENPL YRPPPPFDSA RLADRSPKPR HTNAPFREPP
PYVPP
//
