Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Dystroglycan (Dystrophin-associated glycoprotein 1) [Cleaved into: Alpha-dystroglycan (Alpha-DG); Beta-dystroglycan (Beta-DG)]

 DAG1_HUMAN              Reviewed;         895 AA.
Q14118; A8K6M7; Q969J9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 172.
RecName: Full=Dystroglycan;
AltName: Full=Dystrophin-associated glycoprotein 1;
Contains:
RecName: Full=Alpha-dystroglycan;
Short=Alpha-DG;
Contains:
RecName: Full=Beta-dystroglycan;
Short=Beta-DG;
Flags: Precursor;
Name=DAG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT TRP-14.
TISSUE=Skeletal muscle;
PubMed=8268918; DOI=10.1093/hmg/2.10.1651;
Ibraghimov-Beskrovnaya O., Milatovich A., Ozcelik T., Yang B.,
Koepnick K., Francke U., Campbell K.P.;
"Human dystroglycan: skeletal muscle cDNA, genomic structure, origin
of tissue specific isoforms and chromosomal localization.";
Hum. Mol. Genet. 2:1651-1657(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-14.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-14.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-14.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH DMD.
PubMed=7592992; DOI=10.1074/jbc.270.45.27305;
Jung D., Yang B., Meyer J., Chamberlain J.S., Campbell K.P.;
"Identification and characterization of the dystrophin anchoring site
on beta-dystroglycan.";
J. Biol. Chem. 270:27305-27310(1995).
[7]
FUNCTION (MICROBIAL INFECTION) AS RECEPTOR FOR MYCOBACTERIUM LEPRAE,
SUBCELLULAR LOCATION, AND INTERACTION WITH LAMA2.
PubMed=9851927; DOI=10.1126/science.282.5396.2076;
Rambukkana A., Yamada H., Zanazzi G., Mathus T., Salzer J.L.,
Yurchenco P.D., Campbell K.P., Fischetti V.A.;
"Role of alpha-dystroglycan as a Schwann cell receptor for
Mycobacterium leprae.";
Science 282:2076-2079(1998).
[8]
INTERACTION WITH UTRN.
PubMed=10767429; DOI=10.1016/S0014-5793(00)01400-9;
Tommasi di Vignano A., Di Zenzo G., Sudol M., Cesareni G., Dente L.;
"Contribution of the different modules in the utrophin carboxy-
terminal region to the formation and regulation of the DAP complex.";
FEBS Lett. 471:229-234(2000).
[9]
INTERACTION WITH CAV3.
PubMed=10988290; DOI=10.1074/jbc.M005321200;
Sotgia F., Lee J.K., Das K., Bedford M., Petrucci T.C., Macioce P.,
Sargiacomo M., Bricarelli F.D., Minetti C., Sudol M., Lisanti M.P.;
"Caveolin-3 directly interacts with the C-terminal tail of beta
-dystroglycan. Identification of a central WW-like domain within
caveolin family members.";
J. Biol. Chem. 275:38048-38058(2000).
[10]
PHOSPHORYLATION, AND INTERACTION WITH UTRN.
PubMed=10769203;
James M., Nuttall A., Ilsley J.L., Ottersbach K., Tinsley J.M.,
Sudol M., Winder S.J.;
"Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan
regulates its interaction with utrophin.";
J. Cell Sci. 113:1717-1726(2000).
[11]
PHOSPHORYLATION, INTERACTION WITH FYN; CSK; NCK AND SHC, AND POSSIBLE
FUNCTION.
PubMed=11724572; DOI=10.1021/bi011247r;
Sotgia F., Lee H., Bedford M.T., Petrucci T., Sudol M., Lisanti M.P.;
"Tyrosine phosphorylation of beta-dystroglycan at its WW domain
binding motif, PPxY, recruits SH2 domain containing proteins.";
Biochemistry 40:14585-14592(2001).
[12]
PHOSPHORYLATION AT TYR-892, AND INTERACTION WITH DMD.
PubMed=11495720; DOI=10.1016/S0898-6568(01)00188-7;
Ilsley J.L., Sudol M., Winder S.J.;
"The interaction of dystrophin with beta-dystroglycan is regulated by
tyrosine phosphorylation.";
Cell. Signal. 13:625-632(2001).
[13]
GLYCOSYLATION, LIGAND-BINDING, AND ASSOCIATION WITH CONGENITAL
MUSCULAR DYSTROPHIES.
PubMed=12140558; DOI=10.1038/nature00837;
Michele D.E., Barresi R., Kanagawa M., Saito F., Cohn R.D., Satz J.S.,
Dollar J., Nishino I., Kelley R.I., Somer H., Straub V., Mathews K.D.,
Moore S.A., Campbell K.P.;
"Post-translational disruption of dystroglycan-ligand interactions in
congenital muscular dystrophies.";
Nature 418:417-422(2002).
[14]
PHOSPHORYLATION AT TYR-892, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
TYR-892.
PubMed=12795607; DOI=10.1021/bi0271289;
Sotgia F., Bonuccelli G., Bedford M., Brancaccio A., Mayer U.,
Wilson M.T., Campos-Gonzalez R., Brooks J.W., Sudol M., Lisanti M.P.;
"Localization of phospho-beta-dystroglycan (pY892) to an intracellular
vesicular compartment in cultured cells and skeletal muscle fibers in
vivo.";
Biochemistry 42:7110-7123(2003).
[15]
INTERACTION WITH AGR2 AND AGR3.
PubMed=12592373; DOI=10.1038/sj.bjc.6600740;
Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M.,
Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L.,
Terrett J.A.;
"hAG-2 and hAG-3, human homologues of genes involved in
differentiation, are associated with oestrogen receptor-positive
breast tumours and interact with metastasis gene C4.4a and
dystroglycan.";
Br. J. Cancer 88:579-585(2003).
[16]
PROTEOLYTIC PROCESSING OF THE BETA SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=15175026; DOI=10.1111/j.0022-202X.2004.22605.x;
Herzog C., Has C., Franzke C.W., Echtermeyer F.G.,
Schlotzer-Schrehardt U., Kroger S., Gustafsson E., Fassler R.,
Bruckner-Tuderman L.;
"Dystroglycan in skin and cutaneous cells: beta-subunit is shed from
the cell surface.";
J. Invest. Dermatol. 122:1372-1380(2004).
[17]
GLYCOSYLATION, FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH
LYMPHOCYCTIC CHORIOMENINGITIS VIRUS GLYCOPROTEIN.
PubMed=16254364; DOI=10.1128/JVI.79.22.14297-14308.2005;
Imperiali M., Thoma C., Pavoni E., Brancaccio A., Callewaert N.,
Oxenius A.;
"O Mannosylation of alpha-dystroglycan is essential for lymphocytic
choriomeningitis virus receptor function.";
J. Virol. 79:14297-14308(2005).
[18]
DISULFIDE BOND.
PubMed=17212656; DOI=10.1111/j.1365-2443.2006.01033.x;
Watanabe N., Sasaoka T., Noguchi S., Nishino I., Tanaka T.;
"Cys669-Cys713 disulfide bridge formation is a key to dystroglycan
cleavage and subunit association.";
Genes Cells 12:75-88(2007).
[19]
GLYCOSYLATION, AND FUNCTION (MICROBIAL INFECTION) AS RECEPTOR FOR OLD
WORLD AND CLADE C NEW WORLD ARENAVIRUSES.
PubMed=17360738; DOI=10.1128/JVI.02574-06;
Rojek J.M., Spiropoulou C.F., Campbell K.P., Kunz S.;
"Old World and clade C New World arenaviruses mimic the molecular
mechanism of receptor recognition used by alpha-dystroglycan's host-
derived ligands.";
J. Virol. 81:5685-5695(2007).
[20]
PROTEOLYTIC PROCESSING, CLEAVAGE AT GLY-653, GLYCOSYLATION,
LIGAND-BINDING, AND MUTAGENESIS OF SER-654.
PubMed=17905726; DOI=10.1096/fj.07-8354com;
Akhavan A., Crivelli S.N., Singh M., Lingappa V.R., Muschler J.L.;
"SEA domain proteolysis determines the functional composition of
dystroglycan.";
FASEB J. 22:612-621(2008).
[21]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
SER-654; THR-663; 777-LYS--LYS-780; 793-LYS-LYS-794; LYS-823;
828-PRO-PRO-829 AND TYR-831.
PubMed=18764929; DOI=10.1111/j.1600-0854.2008.00822.x;
Oppizzi M.L., Akhavan A., Singh M., Fata J.E., Muschler J.L.;
"Nuclear translocation of beta-dystroglycan reveals a distinctive
trafficking pattern of autoproteolyzed mucins.";
Traffic 9:2063-2072(2008).
[22]
PROTEOLYTIC PROCESSING OF BETA SUBUNIT, CLEAVAGE AT HIS-715, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19946898; DOI=10.1002/iub.273;
Bozzi M., Inzitari R., Sbardell D., Monaco S., Pavoni E., Gioia M.,
Marini S., Morlacchi S., Sciandra F., Castagnola M., Giardina B.,
Brancaccio A., Coletta M.;
"Enzymatic processing of beta-dystroglycan recombinant ectodomain by
MMP-9: identification of the main cleavage site.";
IUBMB Life 61:1143-1152(2009).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS], AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[24]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH LASSA VIRUS
GLYCOPROTEIN.
PubMed=19324387; DOI=10.1016/j.virol.2009.02.042;
Kunz S.;
"Receptor binding and cell entry of Old World arenaviruses reveal
novel aspects of virus-host interaction.";
Virology 387:245-249(2009).
[25]
STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY, AND
GLYCOSYLATION AT THR-367; THR-369; THR-372 AND THR-455.
PubMed=20507882; DOI=10.1093/glycob/cwq082;
Nilsson J., Nilsson J., Larson G., Grahn A.;
"Characterization of site-specific O-glycan structures within the
mucin-like domain of {alpha}-dystroglycan from human skeletal
muscle.";
Glycobiology 20:1160-1169(2010).
[26]
PHOSPHORYLATION AT TYR-892, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 777-LYS--LYS-782 AND TYR-892.
PubMed=20512930; DOI=10.1002/jcb.22581;
Lara-Chacon B., de Leon M.B., Leocadio D., Gomez P., Fuentes-Mera L.,
Martinez-Vieyra I., Ortega A., Jans D.A., Cisneros B.;
"Characterization of an Importin alpha/beta-recognized nuclear
localization signal in beta-dystroglycan.";
J. Cell. Biochem. 110:706-717(2010).
[27]
GLYCOSYLATION AT THR-379; THR-381 AND THR-388, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=20044576; DOI=10.1126/science.1180512;
Yoshida-Moriguchi T., Yu L., Stalnaker S.H., Davis S., Kunz S.,
Madson M., Oldstone M.B., Schachter H., Wells L., Campbell K.P.;
"O-mannosyl phosphorylation of alpha-dystroglycan is required for
laminin binding.";
Science 327:88-92(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
INVOLVEMENT IN MDDGC9, VARIANT MDDGC9 MET-192, AND CHARACTERIZATION OF
VARIANT MDDGC9 MET-192.
PubMed=21388311; DOI=10.1056/NEJMoa1006939;
Hara Y., Balci-Hayta B., Yoshida-Moriguchi T., Kanagawa M.,
Beltran-Valero de Bernabe D., Gundesli H., Willer T., Satz J.S.,
Crawford R.W., Burden S.J., Kunz S., Oldstone M.B., Accardi A.,
Talim B., Muntoni F., Topaloglu H., Dincer P., Campbell K.P.;
"A dystroglycan mutation associated with limb-girdle muscular
dystrophy.";
N. Engl. J. Med. 364:939-946(2011).
[30]
GLYCOSYLATION AT THR-317 AND THR-319, AND MUTAGENESIS OF
317-THR--THR-319 AND 328-THR-THR-329.
PubMed=21987822; DOI=10.1073/pnas.1114836108;
Hara Y., Kanagawa M., Kunz S., Yoshida-Moriguchi T., Satz J.S.,
Kobayashi Y.M., Zhu Z., Burden S.J., Oldstone M.B., Campbell K.P.;
"Like-acetylglucosaminyltransferase (LARGE)-dependent modification of
dystroglycan at Thr-317/319 is required for laminin binding and
arenavirus infection.";
Proc. Natl. Acad. Sci. U.S.A. 108:17426-17431(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-790, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
GLYCOSYLATION AT THR-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[33]
INVOLVEMENT IN MDDGA9, AND VARIANT MDDGA9 PHE-669.
PubMed=24052401; DOI=10.1007/s10048-013-0374-9;
Geis T., Marquard K., Roedl T., Reihle C., Schirmer S., von Kalle T.,
Bornemann A., Hehr U., Blankenburg M.;
"Homozygous dystroglycan mutation associated with a novel muscle-eye-
brain disease-like phenotype with multicystic leucodystrophy.";
Neurogenetics 14:205-213(2013).
[34]
GLYCOSYLATION AT THR-317 AND THR-319, AND MUTAGENESIS OF
317-THR--THR-319.
PubMed=24256719; DOI=10.1038/srep03288;
Yagi H., Nakagawa N., Saito T., Kiyonari H., Abe T., Toda T., Wu S.W.,
Khoo K.H., Oka S., Kato K.;
"AGO61-dependent GlcNAc modification primes the formation of
functional glycans on alpha-dystroglycan.";
Sci. Rep. 3:3288-3288(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-790, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
INVOLVEMENT IN MDDGC9, VARIANTS MDDGC9 ILE-74 AND ASN-111, AND
CHARACTERIZATION OF VARIANTS MDDGC9 ILE-74 AND ASN-111.
PubMed=25503980; DOI=10.1212/WNL.0000000000001162;
Dong M., Noguchi S., Endo Y., Hayashi Y.K., Yoshida S., Nonaka I.,
Nishino I.;
"DAG1 mutations associated with asymptomatic hyperCKemia and
hypoglycosylation of alpha-dystroglycan.";
Neurology 84:273-279(2015).
[37]
INVOLVEMENT IN MDDGA9.
PubMed=25934851; DOI=10.1212/WNL.0000000000001615;
Riemersma M., Mandel H., van Beusekom E., Gazzoli I., Roscioli T.,
Eran A., Gershoni-Baruch R., Gershoni M., Pietrokovski S.,
Vissers L.E., Lefeber D.J., Willemsen M.A., Wevers R.A.,
van Bokhoven H.;
"Absence of alpha- and beta-dystroglycan is associated with Walker-
Warburg syndrome.";
Neurology 84:2177-2182(2015).
[38]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 881-895.
PubMed=10932245; DOI=10.1038/77923;
Huang X., Poy F., Zhang R., Joachimiak A., Sudol M., Eck M.J.;
"Structure of a WW domain containing fragment of dystrophin in complex
with beta-dystroglycan.";
Nat. Struct. Biol. 7:634-638(2000).
-!- FUNCTION: The dystroglycan complex is involved in a number of
processes including laminin and basement membrane assembly,
sarcolemmal stability, cell survival, peripheral nerve
myelination, nodal structure, cell migration, and epithelial
polarization.
-!- FUNCTION: Alpha-dystroglycan is an extracellular peripheral
glycoprotein that acts as a receptor for both extracellular matrix
proteins containing laminin-G domains. Receptor for laminin-2
(LAMA2) and agrin in peripheral nerve Schwann cells.
-!- FUNCTION: Beta-dystroglycan is a transmembrane protein that plays
important roles in connecting the extracellular matrix to the
cytoskeleton. Acts as a cell adhesion receptor in both muscle and
non-muscle tissues. Receptor for both DMD and UTRN and, through
these interactions, scaffolds axin to the cytoskeleton. Also
functions in cell adhesion-mediated signaling and implicated in
cell polarity.
-!- FUNCTION: (Microbial infection) Alpha-dystroglycan acts as a
receptor for lassa virus and lymphocytic choriomeningitis virus
glycoprotein and class C new-world arenaviruses (PubMed:16254364,
PubMed:19324387, PubMed:17360738). Alpha-dystroglycan acts as a
Schwann cell receptor for Mycobacterium leprae, the causative
organism of leprosy, but only in the presence of the G-domain of
LAMA2 (PubMed:9851927). {ECO:0000269|PubMed:16254364,
ECO:0000269|PubMed:17360738, ECO:0000269|PubMed:19324387,
ECO:0000269|PubMed:9851927}.
-!- SUBUNIT: Monomer. Heterodimer of alpha- and beta-dystroglycan
subunits which are the central components of the dystrophin-
glycoprotein complex. This complex then can form a dystrophin-
associated glycoprotein complex (DGC) which is composed of three
subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN),
DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and
SNTG2, the transmembrane dystroglycan complex, and the
sarcoglycan-sarcospan complex. Interacts (via the N-terminal of
alphaDAG1) with LARGE1; the interaction enhances laminin binding
(By similarity). Interacts with SGCD. Interacts with AGR2 and
AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited
by phosphorylation on the PPXY motif. Interacts (betaDAG1, via its
PPXY motif) with UTRN (via its WWW and ZZ domains); the
interaction is inhibited by phosphorylation on the PPXY motif.
Interacts (betaDAG1, via its phosphorylated PPXY motif) with the
SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts
(betaDAG1) with CAV3 (via a central WW-like domain); the
interaction disrupts the binding of DMD. BetaDAG1 directly
interacts with ANK3, but not with ANK2; this interaction does not
interfere with DMD-binding and is required for retention at
costameres (By similarity). Identified in a dystroglycan complex
that contains at least PRX, DRP2, UTRN, DMD and DAG1 (By
similarity). {ECO:0000250|UniProtKB:Q28685,
ECO:0000250|UniProtKB:Q62165}.
-!- SUBUNIT: (Microbial infection) Interacts with lassa virus and
lymphocytic choriomeningitis virus glycoprotein (PubMed:16254364,
PubMed:19324387). {ECO:0000269|PubMed:16254364,
ECO:0000269|PubMed:19324387}.
-!- SUBUNIT: (Microbial infection) Interacts with surface molecules of
mycobacterium leprae. {ECO:0000269|PubMed:9851927}.
-!- INTERACTION:
Q3T1J5:Ank3 (xeno); NbExp=2; IntAct=EBI-1755945, EBI-2133962;
P16333:NCK1; NbExp=2; IntAct=EBI-1755945, EBI-389883;
-!- SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular
space.
-!- SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane; Single-
pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus,
nucleoplasm. Cell membrane, sarcolemma {ECO:0000250}. Cell
junction, synapse, postsynaptic cell membrane {ECO:0000250}.
Note=The monomeric form translocates to the nucleus via the action
of importins and depends on RAN. Nuclear transport is inhibited by
Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated
form locates to a vesicular internal membrane compartment. In
muscle cells, sarcolemma localization requires the presence of
ANK2, while localization to costameres requires the presence of
ANK3. Localizes to neuromuscular junctions (NMJs) in the presence
of ANK2 (By similarity). In peripheral nerves, localizes to the
Schwann cell membrane. Colocalizes with ERM proteins in Schwann-
cell microvilli. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in a variety of fetal and adult
tissues. In epidermal tissue, located to the basement membrane.
Also expressed in keratinocytes and fibroblasts.
{ECO:0000269|PubMed:15175026, ECO:0000269|PubMed:8268918}.
-!- PTM: O- and N-glycosylated. Alpha-dystroglycan is heavily O-
glycosylated comprising of up to two thirds of its mass and the
carbohydrate composition differs depending on tissue type. Mucin-
type O-glycosylation is important for ligand binding activity. O-
mannosylation of alpha-DAG1 is found in high abundance in both
brain and muscle where the most abundant glycan is Sia-alpha-2-3-
Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on
Thr-317, Thr-319 and Thr-379 by a phosphorylated O-mannosyl glycan
with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-
(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is
mediated by like-acetylglucosaminyltransferase (LARGE1) protein
and is required for laminin binding (PubMed:20044576,
PubMed:21987822, PubMed:24256719). O-mannosylation is also
required for binding lymphocytic choriomeningitis virus, Old World
Lassa fever virus, and clade C New World arenaviruses. The O-
glycosyl hexose on Thr-367, Thr-369, Thr-372, Thr-381 and Thr-388
is probably mannose. O-glycosylated in the N-terminal region with
a core 1 or possibly core 8 glycan. The beta subunit is N-
glycosylated. {ECO:0000269|PubMed:12140558,
ECO:0000269|PubMed:16254364, ECO:0000269|PubMed:17360738,
ECO:0000269|PubMed:17905726, ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:20044576, ECO:0000269|PubMed:20507882,
ECO:0000269|PubMed:21987822, ECO:0000269|PubMed:23234360,
ECO:0000269|PubMed:24256719}.
-!- PTM: Autolytic cleavage produces the alpha and beta subunits. In
cutaneous cells, as well as in certain pathological conditions,
shedding of beta-dystroglcan can occur releasing a peptide of
about 30 kDa. {ECO:0000269|PubMed:15175026,
ECO:0000269|PubMed:17905726, ECO:0000269|PubMed:18764929,
ECO:0000269|PubMed:19946898}.
-!- PTM: SRC-mediated phosphorylation of the PPXY motif of the beta
subunit recruits SH2 domain-containing proteins, but inhibits
binding to WWW domain-containing proteins, DMD and UTRN. This
phosphorylation also inhibits nuclear entry.
-!- DISEASE: Muscular dystrophy-dystroglycanopathy limb-girdle C9
(MDDGC9) [MIM:613818]: An autosomal recessive muscular dystrophy
showing onset in early childhood, and associated with mental
retardation without structural brain anomalies.
{ECO:0000269|PubMed:21388311, ECO:0000269|PubMed:25503980}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. MDDGC7 is caused by DAG1 mutations that
interfere with normal post-translational processing, resulting in
defective DAG1 glycosylation and impaired interactions with
extracellular-matrix components. Other muscular dystrophy-
dystroglycanopathies are caused by defects in enzymes involved in
protein O-glycosylation.
-!- DISEASE: Muscular dystrophy-dystroglycanopathy congenital with
brain and eye anomalies A9 (MDDGA9) [MIM:616538]: An autosomal
recessive disorder characterized by congenital muscular dystrophy
associated with cobblestone lissencephaly and other brain
anomalies, eye malformations, profound mental retardation, and
death usually in the first years of life. Included diseases are
the more severe Walker-Warburg syndrome and the slightly less
severe muscle-eye-brain disease. {ECO:0000269|PubMed:24052401,
ECO:0000269|PubMed:25934851}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Wikipedia; Note=Dystroglycan entry;
URL="https://en.wikipedia.org/wiki/Dystroglycan";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L19711; AAA81779.1; -; mRNA.
EMBL; AK291692; BAF84381.1; -; mRNA.
EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64989.1; -; Genomic_DNA.
EMBL; BC012740; AAH12740.1; -; mRNA.
EMBL; BC014616; AAH14616.1; -; mRNA.
CCDS; CCDS2799.1; -.
PIR; I54343; I54343.
RefSeq; NP_001159400.2; NM_001165928.3.
RefSeq; NP_001171105.1; NM_001177634.2.
RefSeq; NP_001171106.1; NM_001177635.2.
RefSeq; NP_001171107.1; NM_001177636.2.
RefSeq; NP_001171108.1; NM_001177637.2.
RefSeq; NP_001171109.1; NM_001177638.2.
RefSeq; NP_001171110.1; NM_001177639.2.
RefSeq; NP_001171111.1; NM_001177640.2.
RefSeq; NP_001171112.1; NM_001177641.2.
RefSeq; NP_001171113.1; NM_001177642.2.
RefSeq; NP_001171114.1; NM_001177643.2.
RefSeq; NP_001171115.1; NM_001177644.2.
RefSeq; NP_004384.4; NM_004393.5.
UniGene; Hs.76111; -.
PDB; 1EG4; X-ray; 2.00 A; P=881-895.
PDB; 2MK7; NMR; -; A=419-427.
PDB; 5GGP; X-ray; 1.60 A; C/D=316-325.
PDB; 5LLK; X-ray; 1.80 A; A=52-315.
PDBsum; 1EG4; -.
PDBsum; 2MK7; -.
PDBsum; 5GGP; -.
PDBsum; 5LLK; -.
ProteinModelPortal; Q14118; -.
SMR; Q14118; -.
BioGrid; 107975; 57.
CORUM; Q14118; -.
DIP; DIP-40928N; -.
IntAct; Q14118; 11.
MINT; MINT-5004541; -.
STRING; 9606.ENSP00000312435; -.
ChEMBL; CHEMBL3714399; -.
MEROPS; S72.001; -.
iPTMnet; Q14118; -.
PhosphoSitePlus; Q14118; -.
SwissPalm; Q14118; -.
UniCarbKB; Q14118; -.
BioMuta; DAG1; -.
DMDM; 229462879; -.
EPD; Q14118; -.
MaxQB; Q14118; -.
PaxDb; Q14118; -.
PeptideAtlas; Q14118; -.
PRIDE; Q14118; -.
TopDownProteomics; Q14118; -.
DNASU; 1605; -.
Ensembl; ENST00000308775; ENSP00000312435; ENSG00000173402.
Ensembl; ENST00000515359; ENSP00000440705; ENSG00000173402.
Ensembl; ENST00000538711; ENSP00000438421; ENSG00000173402.
Ensembl; ENST00000539901; ENSP00000439334; ENSG00000173402.
Ensembl; ENST00000541308; ENSP00000440590; ENSG00000173402.
Ensembl; ENST00000545947; ENSP00000442600; ENSG00000173402.
GeneID; 1605; -.
KEGG; hsa:1605; -.
UCSC; uc003cxc.5; human.
CTD; 1605; -.
DisGeNET; 1605; -.
EuPathDB; HostDB:ENSG00000173402.11; -.
GeneCards; DAG1; -.
HGNC; HGNC:2666; DAG1.
HPA; CAB001960; -.
HPA; CAB016353; -.
MalaCards; DAG1; -.
MIM; 128239; gene.
MIM; 613818; phenotype.
MIM; 616538; phenotype.
neXtProt; NX_Q14118; -.
OpenTargets; ENSG00000173402; -.
Orphanet; 280333; Autosomal recessive limb-girdle muscular dystrophy type 2P.
Orphanet; 370997; Muscle-eye-brain disease with bilateral multicystic leucodystrophy.
PharmGKB; PA27138; -.
eggNOG; KOG3781; Eukaryota.
eggNOG; ENOG410XQTU; LUCA.
GeneTree; ENSGT00390000008429; -.
HOGENOM; HOG000072580; -.
HOVERGEN; HBG000078; -.
InParanoid; Q14118; -.
KO; K06265; -.
OMA; AMICYRK; -.
OrthoDB; EOG091G05R9; -.
PhylomeDB; Q14118; -.
TreeFam; TF328370; -.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-5083628; Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3.
Reactome; R-HSA-5083629; Defective POMT2 causes MDDGA2, MDDGB2 and MDDGC2.
Reactome; R-HSA-5083633; Defective POMT1 causes MDDGA1, MDDGB1 and MDDGC1.
Reactome; R-HSA-5173105; O-linked glycosylation.
SIGNOR; Q14118; -.
ChiTaRS; DAG1; human.
EvolutionaryTrace; Q14118; -.
GeneWiki; Dystroglycan; -.
GenomeRNAi; 1605; -.
PRO; PR:Q14118; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000173402; -.
CleanEx; HS_DAG1; -.
ExpressionAtlas; Q14118; baseline and differential.
Genevisible; Q14118; HS.
GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
GO; GO:0043034; C:costamere; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016011; C:dystroglycan complex; IEA:Ensembl.
GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0033268; C:node of Ranvier; IEA:Ensembl.
GO; GO:0034399; C:nuclear periphery; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0051393; F:alpha-actinin binding; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
GO; GO:0043237; F:laminin-1 binding; ISS:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0016340; P:calcium-dependent cell-matrix adhesion; IEA:Ensembl.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IMP:UniProtKB.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
GO; GO:0019048; P:modulation by virus of host morphology or physiology; IDA:UniProtKB.
GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0021682; P:nerve maturation; IEA:Ensembl.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IDA:UniProtKB.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl.
GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0006493; P:protein O-linked glycosylation; TAS:Reactome.
GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.30.70.1040; -; 1.
InterPro; IPR027468; Alpha-dystroglycan_domain_2.
InterPro; IPR006644; Cadg.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR008465; DAG1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR030398; SEA_DG_dom.
Pfam; PF05454; DAG1; 1.
SMART; SM00736; CADG; 2.
SUPFAM; SSF111006; SSF111006; 1.
SUPFAM; SSF49313; SSF49313; 2.
PROSITE; PS51699; SEA_DG; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Cell junction; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation;
Disulfide bond; Dystroglycanopathy; Glycoprotein;
Host cell receptor for virus entry; Host-virus interaction;
Limb-girdle muscular dystrophy; Lissencephaly; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Secreted; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 653 Alpha-dystroglycan.
/FTId=PRO_0000021065.
CHAIN 654 895 Beta-dystroglycan.
/FTId=PRO_0000021066.
TOPO_DOM 654 749 Extracellular. {ECO:0000255}.
TRANSMEM 750 775 Helical. {ECO:0000255}.
TOPO_DOM 776 895 Cytoplasmic. {ECO:0000255}.
DOMAIN 603 712 Peptidase S72.
REGION 30 408 Required for laminin recognition.
REGION 169 200 O-glycosylated at one site.
REGION 316 485 Mucin-like domain.
REGION 463 485 O-glycosylated at seven sites with
GalNAc.
REGION 819 895 Required for interaction with CAV3.
{ECO:0000269|PubMed:10988290}.
REGION 880 895 Required for binding DMD and UTRN.
MOTIF 776 782 Nuclear localization signal.
{ECO:0000269|PubMed:20512930}.
MOTIF 889 892 PPXY motif.
COMPBIAS 317 484 Thr-rich.
COMPBIAS 809 895 Pro-rich.
SITE 653 654 Cleavage; by autolysis.
SITE 715 716 Cleavage; by MMP9.
MOD_RES 790 790 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 892 892 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:11495720,
ECO:0000269|PubMed:12795607,
ECO:0000269|PubMed:20512930}.
CARBOHYD 63 63 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 O-linked (Man6P...) threonine.
{ECO:0000269|PubMed:21987822,
ECO:0000269|PubMed:24256719}.
CARBOHYD 319 319 O-linked (Man6P...) threonine.
{ECO:0000269|PubMed:21987822,
ECO:0000269|PubMed:24256719}.
CARBOHYD 367 367 O-linked (Hex...) threonine.
{ECO:0000269|PubMed:20507882}.
CARBOHYD 369 369 O-linked (Hex...) threonine.
{ECO:0000269|PubMed:20507882}.
CARBOHYD 372 372 O-linked (Hex...) threonine.
{ECO:0000269|PubMed:20507882}.
CARBOHYD 379 379 O-linked (Man6P...) threonine.
{ECO:0000269|PubMed:20044576}.
CARBOHYD 381 381 O-linked (Hex...) threonine.
{ECO:0000269|PubMed:20044576}.
CARBOHYD 388 388 O-linked (Hex...) threonine.
{ECO:0000269|PubMed:20044576}.
CARBOHYD 455 455 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:20507882}.
CARBOHYD 641 641 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 649 649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 661 661 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 182 264 {ECO:0000250}.
DISULFID 669 713 {ECO:0000269|PubMed:17212656}.
VARIANT 14 14 S -> W (in dbSNP:rs2131107).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8268918,
ECO:0000269|Ref.4}.
/FTId=VAR_024335.
VARIANT 74 74 V -> I (in MDDGC9; no effect on
dystroglycan expression; impairs alpha-
dystroglycan glycosylation;
dbSNP:rs189360006).
{ECO:0000269|PubMed:25503980}.
/FTId=VAR_075809.
VARIANT 111 111 D -> N (in MDDGC9; does not affect
dystroglycan expression; impairs alpha-
dystroglycan glycosylation;
dbSNP:rs117209107).
{ECO:0000269|PubMed:25503980}.
/FTId=VAR_075810.
VARIANT 192 192 T -> M (in MDDGC9; results in impaired
interaction with LARGE1 and incomplete
DAG1 glycosylation; dbSNP:rs193922955).
{ECO:0000269|PubMed:21388311}.
/FTId=VAR_065266.
VARIANT 669 669 C -> F (in MDDGA9; dbSNP:rs797045023).
{ECO:0000269|PubMed:24052401}.
/FTId=VAR_075811.
MUTAGEN 317 319 TPT->APA: Impaired laminin-binding.
{ECO:0000269|PubMed:21987822,
ECO:0000269|PubMed:24256719}.
MUTAGEN 328 329 TT->AA: Does not affect laminin-binding.
{ECO:0000269|PubMed:21987822}.
MUTAGEN 654 654 S->A: Abolishes autoproteolysis and
enhances laminin-binding.
{ECO:0000269|PubMed:17905726,
ECO:0000269|PubMed:18764929}.
MUTAGEN 663 663 T->A: Reduced N-linked glycosylation. No
change in nuclear translocation.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 776 782 RKKRKGK->AKKRKGA: Moderate reduction in
nuclear accumulation.
MUTAGEN 777 782 KKRKGK->AARKGA: About 50% reduction in
nuclear accumulation.
{ECO:0000269|PubMed:20512930}.
MUTAGEN 777 782 KKRKGK->RKKAAGA: Drastic reduction in
nuclear accumulation.
{ECO:0000269|PubMed:20512930}.
MUTAGEN 777 780 KKRK->NPGE: Abolishes nuclear
translocation.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 779 779 R->A: Significant reduction in nuclear
accumulation.
MUTAGEN 780 780 K->A: Significant reduction in nuclear
accumulation.
MUTAGEN 793 794 KK->TA: Abolishes nuclear translocation.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 823 823 K->A: No change in nuclear location.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 828 829 PP->AA: No change in nuclear location.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 831 831 Y->A: No change in nuclear location.
{ECO:0000269|PubMed:18764929}.
MUTAGEN 892 892 Y->A: Abolishes phosphorylation. No
change in plasma membrane location.
{ECO:0000269|PubMed:12795607,
ECO:0000269|PubMed:20512930}.
MUTAGEN 892 892 Y->E: Redistributes to a vesicular
internal membrane compartment.
{ECO:0000269|PubMed:12795607,
ECO:0000269|PubMed:20512930}.
MUTAGEN 892 892 Y->F: Abolishes phosphorylation. Increase
in nuclear location.
{ECO:0000269|PubMed:12795607,
ECO:0000269|PubMed:20512930}.
CONFLICT 163 163 E -> D (in Ref. 1; AAA81779).
{ECO:0000305}.
CONFLICT 248 248 A -> P (in Ref. 1; AAA81779).
{ECO:0000305}.
CONFLICT 319 319 T -> A (in Ref. 2; BAF84381).
{ECO:0000305}.
CONFLICT 871 871 A -> V (in Ref. 1; AAA81779).
{ECO:0000305}.
SEQUENCE 895 AA; 97441 MW; 3AF6CBB0DCF91962 CRC64;
MRMSVGLSLL LPLSGRTFLL LLSVVMAQSH WPSEPSEAVR DWENQLEASM HSVLSDLHEA
VPTVVGIPDG TAVVGRSFRV TIPTDLIASS GDIIKVSAAG KEALPSWLHW DSQSHTLEGL
PLDTDKGVHY ISVSATRLGA NGSHIPQTSS VFSIEVYPED HSELQSVRTA SPDPGEVVSS
ACAADEPVTV LTVILDADLT KMTPKQRIDL LHRMRSFSEV ELHNMKLVPV VNNRLFDMSA
FMAGPGNAKK VVENGALLSW KLGCSLNQNS VPDIHGVEAP AREGAMSAQL GYPVVGWHIA
NKKPPLPKRV RRQIHATPTP VTAIGPPTTA IQEPPSRIVP TPTSPAIAPP TETMAPPVRD
PVPGKPTVTI RTRGAIIQTP TLGPIQPTRV SEAGTTVPGQ IRPTMTIPGY VEPTAVATPP
TTTTKKPRVS TPKPATPSTD STTTTTRRPT KKPRTPRPVP RVTTKVSITR LETASPPTRI
RTTTSGVPRG GEPNQRPELK NHIDRVDAWV GTYFEVKIPS DTFYDHEDTT TDKLKLTLKL
REQQLVGEKS WVQFNSNSQL MYGLPDSSHV GKHEYFMHAT DKGGLSAVDA FEIHVHRRPQ
GDRAPARFKA KFVGDPALVL NDIHKKIALV KKLAFAFGDR NCSTITLQNI TRGSIVVEWT
NNTLPLEPCP KEQIAGLSRR IAEDDGKPRP AFSNALEPDF KATSITVTGS GSCRHLQFIP
VVPPRRVPSE APPTEVPDRD PEKSSEDDVY LHTVIPAVVV AAILLIAGII AMICYRKKRK
GKLTLEDQAT FIKKGVPIIF ADELDDSKPP PSSSMPLILQ EEKAPLPPPE YPNQSVPETT
PLNQDTMGEY TPLRDEDPNA PPYQPPPPFT APMEGKGSRP KNMTPYRSPP PYVPP


Related products :

Catalog number Product name Quantity
EIAAB38105 50 kDa dystrophin-associated glycoprotein,50DAG,Adhalin,ADL,Alpha-sarcoglycan,Alpha-SG,DAG2,Dystroglycan-2,Oryctolagus cuniculus,Rabbit,SGCA
EIAAB38106 50 kDa dystrophin-associated glycoprotein,50DAG,Adhalin,ADL,Alpha-sarcoglycan,Alpha-SG,DAG2,Dystroglycan-2,Homo sapiens,Human,SGCA
DAGLB DAG1 Gene dystroglycan 1 (dystrophin-associated glycoprotein 1)
EIAAB10394 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Pig,Sus scrofa
EIAAB10395 Dag1,Dag-1,Dystroglycan,Dystrophin-associated glycoprotein 1,Mouse,Mus musculus
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit 96T
EIAAB10391 Bos taurus,Bovine,DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1
EIAAB10392 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Oryctolagus cuniculus,Rabbit
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit SpeciesHuman 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit SpeciesMouse 96T
EIAAB10393 DAG1,Dystroglycan,Dystrophin-associated glycoprotein 1,Homo sapiens,Human
GS-0538a dystroglycan 1 (dystrophin-associated glycoprotein 1) primary antibody, Host: Rabbit 200ul
CSB-EL006488PI Pig dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL006488DO Dog dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL006488BO Bovine dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL006488HU Human dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006488RB Rabbit dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL006488MO Mouse dystroglycan 1 (dystrophin-associated glycoprotein 1) (DAG1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
NB100-79904 Dystroglycan Beta 0.1 ml
GWB-671E0F Beta-Dystroglycan, Antibody
AJ1095a Beta-Dystroglycan Antibody
NB100-79904 Dystroglycan Beta 0.1 ml
NBL1-09713 Alpha Dystroglycan Lysate 0.1 mg
Y090790 Anti-dystroglycan, beta- Monoclonal Antibody 100ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur