ID A0A182QLM1_9DIPT Unreviewed; 939 AA.
AC A0A182QLM1;
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 farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF012684-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., 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 farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF012684-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF012684-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 EMBL; AXCN02001001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QLM1; -.
DR STRING; 69004.A0A182QLM1; -.
DR EnsemblMetazoa; AFAF012684-RA; AFAF012684-PA; AFAF012684.
DR VEuPathDB; VectorBase:AFAF012684; -.
DR OrthoDB; 3598963at2759; -.
DR Proteomes; UP000075886; 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 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 808..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 436..543
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT DOMAIN 667..781
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 939 AA; 104953 MW; 31C975CCAD8D322C CRC64;
MLLDAKHHRQ SDDETPRGSS TVRNTFESAE KTTTTTTVLL AAFDSSSTSS VSASTTTASF
TSTTTTQTPS SSTPVVDSWS SEMDEEDESL EDETNKQFVD EVDSKSSPFA RTEYPASSTT
AAVSSLDSAT GLDSYTTIVS VPLTTGKQEE LSRYDRFPVD RALGEQDVSV EDELEQEDID
EDEEDDYFSQ GPTTTTERNG AVFTTPKQNA ADTWKEVEYE NYDEEYDDEE EEGGAQEMTT
ISTLPDPRAL PSSTERTSTE ASTVPSTTST EATTPSTTTS TTTTTTTTTT TEAPTTTTST
TTTTTTTTEA TTTTTFTVPP VTELDEPTNL PPIIRNRIPK QAIPAGKVFR YQVPLETFSD
NEDGNNLRLE LLDSRDQPLK PSSWMQFNED TKEIYGLPLE KDVSRWAYKL RATDSGNLTV
TEKVDIMVQQ HKSHRSLNHE ISLALRLNRK FTSNVDWHIE TARGISGVLG DVTLANIIVR
DIRYSIQDPS LATFVYTNET LPKDRCPEEK LDELVALLTE EALNVALNPD ITVKSVQGQQ
IAQCTKPTLP KAKPTQSISR NMAPQTRNQV DQVNATVGHL LVFKVPVDTF FDNEDGNELK
MKLLTTERHT LDPYHWLQFD SKNQEFYGVP RTNDIGRKEY LLMAEDREGL TATDALVVVV
NPHHKRDYSV LFELTLDITH EQFSTAQVQR RFIERLAQVF GDASTHYIKI HHIRPIHHTG
QVQVSFFNTT LNRQHQRCPQ EEIEALRNIL LHQDSTIRAK VREILGQEFS LQNVSLVPLD
NCHGFDTPHH ATSEPEKAAP KPISKDDYLL TFVLPTVIIL VMLLFASVIA CILYKRRLTG
KMELGTDEER KSFRSKGIPV IFQDELDEKP EIGNKSPVIL KDEKPPLLPP SYSSTNNDGE
NEDVDEYVPP QPVIVGGRES RGKSPVTPSY RRPPPYVSP
//
