ID L8Y3L3_TUPCH Unreviewed; 916 AA.
AC L8Y3L3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=TREES_T100002396 {ECO:0000313|EMBL:ELV09644.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV09644.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. 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; KB369979; ELV09644.1; -; Genomic_DNA.
DR AlphaFoldDB; L8Y3L3; -.
DR STRING; 246437.L8Y3L3; -.
DR MEROPS; S72.001; -.
DR eggNOG; KOG3781; Eukaryota.
DR InParanoid; L8Y3L3; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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; 2.
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 InterPro; IPR016560; TCTA.
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 Pfam; PF15128; T_cell_tran_alt; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
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 Reference proteome {ECO:0000313|Proteomes:UP000011518};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 770..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 624..733
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 400..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 99365 MW; 966A3800EF7CC9FB CRC64;
MAEPWSAQSL QALPATVLGA LGALGSEFLR EWEAQDMRVT LFKVLLLWLV LSLLGIQLAW
GFYGNTVTGL YHRPGLGGQN GSTPDGSTNP SCTAVVGRSF RVTIPTDLIA ASGEVIKVSA
AGKEALPSWL HWDPQSHTLE GLPLDTDKGV HYISVSAARL GANGSHVPQT SSVFSIEVYP
EDHSEPHSVR AASPDPSEAV ASACAADEPV TVLTVILDAD LTKMSPKQRL DLLQRMQSFS
GVELHHMKLV PVVNNRLFDM SAFMAGPGNA KKVVENGALL SWKLGCSLSQ NNVPDIRGVE
APAREGAMSA QLGYPVVGWH IANKKPPLPK RIRRQIHATP TPVTAIGPPT TAIQEPPSRI
VPTPTSPAIA PPTETMVPPV RDPVPGKPTV TIRTRGTIFQ TPTLGPIQPT RVSEPGTTVP
GQIRPTMTIP GYVEPTAVAT PPTTTTKKPR VSTPKPATPS TDSATTTRRP TKKPRTPRPV
PRVTTKAPIT RLETASPPTR VRTTTSGVPR GGEPNQRPEL KNHIDRVDAW VGTYFEVKIP
PDTFYDNEDT TTDKLKLTLK LREQQLVGEK SWVQFNSNSQ LMYGLPDSSH VGKHEYFMHA
TDKGGLSAVD AFEIHVHKRP QGDRAPARFK AKFVGDPAPV VNDIHKKIAL VKKLAFAFGD
RNCSTITLQN ITRGSIVVEW TNNTLPLEPC PKEQITGLSR RIAEDNGKPR PAFSNALEPD
FKAMSVSVMG AGSCRHLQFI PVAPPRRIPS EAPPTEVPDR DPEKSSEDDV YLHTVIPAVV
VAAILLIAGI IAMICYRKKR KGKLTLEDQA TFIKKGVPII FADELDDSKP PPSSSMPLIL
QEEKAPLPPP EYPNQSVPET TPLNQDTVGE YTPLRDEDPN APPYQPPPPF TAPMEGKGSR
PKNMTPYRSP PPYVPP
//
