ID A0A182XJD3_ANOQN Unreviewed; 981 AA.
AC A0A182XJD3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA009967-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA009967-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA009967-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A182XJD3; -.
DR STRING; 34691.A0A182XJD3; -.
DR EnsemblMetazoa; AQUA009967-RA; AQUA009967-PA; AQUA009967.
DR VEuPathDB; VectorBase:AQUA009967; -.
DR Proteomes; UP000076407; 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 Pfam; PF05345; He_PIG; 1.
DR SMART; SM00736; CADG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 2.
DR PROSITE; PS51699; SEA_DG; 2.
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 Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 850..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 478..585
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT DOMAIN 709..823
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 981 AA; 109564 MW; 5E182B751CDB56C7 CRC64;
MFAFSSTIVG LSDDEPAASS SSTIKTIVPE ATTEKSSKIS SYSSAVEYST PSSTTTATAT
TTIAALPAIT STPASSWHLG MDEDEEASYE SKEFFDEIDS KPSTFANAEM ASITSTTTTT
HGSEDQGTSD YTTTTISYVP LTTTPTTQEE LSRYATNLDR SPFGRKIKDE DISADQEEED
QEEGEDIDEE EEEEDYFSQG VRITVLPPNN LPPLIPRAEE VEVTVPTSTL TPDSVDSDRP
TSTQRSVSTF TTPKQDNEEE DKELEYENYD DEYDDEEEGA IELTTQPDPR VLSSTTTTER
PMPSSTEPST TPTTVTMPTT TPSTTTTTTT EAPTTTTTTT TSTTTTTTTT TTEASTTTST
MLTTELDEPT NLPPIIRNRI PKQAIPAGKV FRYQVPLETF HDNEDGNNLS LELLDARDQP
LKPSSWIQFN EDTKEIYGLP LEKDVSRWPY KLRATDSGNL TVTEKVDIQV QQHKSHRSLN
HEISLALRLN RKFASNVDWH IETARGISVV LGDVTLSNII VRDIRNSIQD PSLATFVYTN
ETLPKDRCPE EKLDELVALL TEEALNDALN PDITVKSVQG QQIAQCTKVT PPKVKPTQSI
QRNYAPQTRN QVDQVNATVG HLLVFKVPVD TFYDPEDGNE LKMKLLTTDR NTLDPNHWLQ
FDSKNQEFYG VPRTNDIGRK EYLLMAEDRE GLTATDALVV VVNPHHKRDY SVLFELTLDI
SHEQFNTAQV QRRFIERLAQ VFGDASTHYI KIHHIRPIHH TGQVQVSFFN TTLSRQHQRC
PQEEIETLRN ILLHQDSTIR AKVREILGQE FSLQNVSLVP LDNCHGFDTP HHATSEPEKA
APKPISKDDY LLTFVLPSVI IIVMLLIAAI IACILYKRRL TGKMELGTDE ERKSFRSKGI
PVIFQDELDE KPEIGNKSPV ILKDEKPPLL PPSYSSTNHD GDNEDVDEYV PPQPVIVGGR
ESRGKSPVTP SYRRPPPYVS P
//
