ID U4UGA5_DENPD Unreviewed; 1236 AA.
AC U4UGA5;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=D910_06303 {ECO:0000313|EMBL:ERL88925.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL88925.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL88925.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(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}. 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; KB632114; ERL88925.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UGA5; -.
DR STRING; 77166.U4UGA5; -.
DR MEROPS; S72.A01; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000030742; 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 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 Pfam; PF05345; He_PIG; 1.
DR SMART; SM00736; CADG; 3.
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:UP000030742};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1236
FT /note="Dystroglycan 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004656536"
FT TRANSMEM 1106..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 718..830
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT DOMAIN 961..1076
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 275..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 138019 MW; 2C4E540285B8E6A6 CRC64;
MTSRFQSSLL FSILLVFSVQ AQEDGFTFDT PEEMHEALMA PIRPQYYPNN VQTAVVGKVF
HYAVQHGKST RGFVAKAQNS KSVPSWLVFN KHTGWFWGVP LPGDEGTLHL KVTTLGEETA
SEILKLRVLE ESPEATPSCK PEEDNTVLTL LLDRHLHAIK PKQRVVAINN IAKFLSLPQS
AFTFKLQSGN DDITDSAVVL AGPGNIQTRI GRKSGSSLEV PVGCDGRLWE STALLIHNLK
QQARDGTIAE VLRLPLIGWR VKTETKPILR NRREATDNFG SGDYDNDYYQ DYDDDYNEEY
DEDDLGDVEA NPPTSSKPVT FPSTTVARTS TTSTTTAAST TTHPHRHHHG EPKVTEGQSE
PVLPIEEALP EQSRTITQPS LPTEPPKSSG PTRIDILKPS DDFDVTYDYD QNYDDDEDDD
DTEDEAIESE TIVPEVSRQM FNKPVFTPVE MVPTTQEVDI EEDAEVATSV LHASTAVYSS
TPEAPTTSEI IVDAEPPIYS VPDTAPPEEG AASTTTTSTT TTSTTTTTST TTTSRPESPP
PSSTSYAVPS TSEATTEAIS IREEPPNTEN PTTEQEESRA TTPRHAPSTT QEVFVQETTE
ATVRFVPEPK NTKPYIENRL QHSQVIAGKI FRLEIPKNTF RDAEDGYNLT FQVLDSNGQP
IPKSSWLQFN PARRELYGLP LPDDASHWDY IVRATDKDGA YEQDQLTVQV QQHRLDRVVN
HEFAVHLRIE KLQEYPHYVD WSLKVLRALG RLYNTNMSEI TVRYINHTSD PVVFAWSNDS
LPTNYCPRQE ILSLYEMLAD NDRGDPSLEL SYTLAPSLRA TKVLSYDLTT CKQQPAPVTP
AAPATPAAPV SLPTNFPPIL RNPIDTVNAT LGELLVYKVQ DDTFYDPEDV DPQTLNITLL
TADRTPIPAT SWLQFDNKNR EFYGIPQKAG ITEYYLICID SGGMEGKDSL IVDVRPAAKR
PYNVEFSMTI GLPFDTFSSN AGLQRKFVEK LMEIFKEPTP GNFHFRPFVA KRDSHLDSTV
VYWFNKSLPV DVCPHKEIKQ LEYLLHSDSR SISSTVHRIM GPEFTISTIK VHHIGNCKSK
PPPVLPTPEV QAPSEKTPQP QADNDIMLTL VLPIIIISIM LFVAFVAACL LYRKRRMGKM
NVEEDGRQSY GNKGIPVIFQ EELEEKPEPG TKAPVILKDE KPPLAPPEYS KSGSVKLEDS
EPYQPPPPFT RTQDNGRQSR PKPTPTYRKP PPYVPP
//
