ID A0A482XHQ6_LAOST Unreviewed; 1112 AA.
AC A0A482XHQ6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=LSTR_LSTR000803 {ECO:0000313|EMBL:RZF44851.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF44851.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF44851.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF44851.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF44851.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
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}.
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:RZF44851.1}.
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DR EMBL; QKKF02010319; RZF44851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482XHQ6; -.
DR STRING; 195883.A0A482XHQ6; -.
DR InParanoid; A0A482XHQ6; -.
DR Proteomes; UP000291343; 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; cd11303; Dystroglycan_repeat; 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 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:UP000291343};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1112
FT /note="Dystroglycan 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019716312"
FT TRANSMEM 977..1003
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 602..713
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT DOMAIN 838..947
FT /note="Peptidase S72"
FT /evidence="ECO:0000259|PROSITE:PS51699"
FT REGION 286..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 124208 MW; 93EA85B698DBFB55 CRC64;
MKMAAKLFQT VVLFVTLCLI SISSSHHEED FAFDQEIIPQ SEIARISSRT PLRRQFGIPD
AMAYLGRLFF FKIPPDAFSG TLSHYKVSGM PSWMIFKEGE GLFEGVPGDK DVGETYITVI
AIGPTAEDSV KDIFVVEVSP DPREYGSDIK ERCKSGQDAT TITVLLDKDF YSIKPADKIL
AVKNLAGFLS LNHDKFSLLP QNSEDDILSE NVINAGPGNV KKKSSLTSTS LQWQVGCGGS
VWSMHGITHV KQIAKDGTLA EVIQLPVIGW HLATSPFPFR ARRELVGSGE GEEREAKEDE
TENADDDEEE EEPEKRVTVP MRSPTPVLPE HMKTTDAHHP LRHAHNSNHH HHGENGEEAE
EEGDDGLSGK LVHNTTSGDP VVSLNILPTP TLVPERPIQK ATEYPSYSSQ ITPDQVTRFY
TTETSAVPEA FSPPPEYTDG DTEPLGEDQL QTSTIYMMDN SSSTVTPFLT NTPTDVTKAI
DYTKETDVEE PKNFPPRISE RLPQLAVTAG KLLQYTIPDN TFSDLEDGNT RELSIDFLTN
EKNPLERSSW IQFNPQSLTI YALPLEEHVS KWYFTIKATD SEGESVSDEV VVAVQNHRQQ
RTITHEITIH FQPWLDEKVD KMLPLDLHIL ILNRLVKLYN NTDSSHITVL SMNSTSFSWT
NDSLSRISPC PRQEIQNLIK VLTESDDQPR SAVKSLFLPE LDVLHVTWTG RGQCQRTDKE
MPEPPPQTVN FSPTRRNSID LLNATVGELL VYTVPGDSYY DHEDGSVRNL KLTLLTANRS
AIPYSHWLQF DVKNQEFYGI PNPNDTGRTQ YQLVCEDSGG LSFNDGLIVE VHPARKILYN
VEFSMTLGIH YDNFVMSPAS QRHFFEKLAE LFGDKDTSAI VRSGMSPGST VVTWHNRTLP
TNICPNDQIK VLRQVLLGDD ERVSMRAKTI MGPELNVLTA SLTPTRLCEG ASTPVHIPEP
PAAPPDEVRP VSRSDEYLVT VVVPAVVIAT MLICAALVAC ILYRRRRTGK MSVGDEDERQ
SFRSKGIPVI FQDELEERPE PTNKSPVIMK EEKPPLPPPE YQRSSHPTVA TALLSDTEDS
PYQPPPPFTS SRDSARPKPP PTYRMPPPYV PP
//
