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LARGE xylosyl- and glucuronyltransferase 1 (EC 2.4.-.-) (Acetylglucosaminyltransferase-like 1A) (Glycosyltransferase-like protein) [Includes: Xylosyltransferase LARGE (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE (EC 2.4.1.-)]

 LARG1_MOUSE             Reviewed;         756 AA.
Q9Z1M7; Q497S9; Q6P7U2; Q80TW0;
26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
30-AUG-2017, entry version 132.
RecName: Full=LARGE xylosyl- and glucuronyltransferase 1 {ECO:0000250|UniProtKB:O95461};
EC=2.4.-.-;
AltName: Full=Acetylglucosaminyltransferase-like 1A;
AltName: Full=Glycosyltransferase-like protein;
Includes:
RecName: Full=Xylosyltransferase LARGE {ECO:0000305};
EC=2.4.2.- {ECO:0000250|UniProtKB:O95461};
Includes:
RecName: Full=Beta-1,3-glucuronyltransferase LARGE {ECO:0000305};
EC=2.4.1.- {ECO:0000250|UniProtKB:O95461};
Name=Large1 {ECO:0000250|UniProtKB:O95461}; Synonyms=Kiaa0609, Large;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Embryo;
PubMed=9892679; DOI=10.1073/pnas.96.2.598;
Peyrard M., Seroussi E., Sandberg-Nordqvist A.-C., Xie Y.-G.,
Han F.-Y., Fransson I., Collins J.E., Dunham I., Kost-Alimova M.,
Imreh S., Dumanski J.P.;
"The human LARGE gene from 22q12.3-q13.1 is a new, distinct member of
the glycosyltransferase gene family.";
Proc. Natl. Acad. Sci. U.S.A. 96:598-603(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Embryonic stem cell, and Mammary tumor;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
DISEASE.
PubMed=11381262; DOI=10.1038/88865;
Grewal P.K., Holzfeind P.J., Bittner R.E., Hewitt J.E.;
"Mutant glycosyltransferase and altered glycosylation of alpha-
dystroglycan in the myodystrophy mouse.";
Nat. Genet. 28:151-154(2001).
[5]
INTERACTION WITH DAG1.
PubMed=15210115; DOI=10.1016/j.cell.2004.06.003;
Kanagawa M., Saito F., Kunz S., Yoshida-Moriguchi T., Barresi R.,
Kobayashi Y.M., Muschler J., Dumanski J.P., Michele D.E.,
Oldstone M.B., Campbell K.P.;
"Molecular recognition by LARGE is essential for expression of
functional dystroglycan.";
Cell 117:953-964(2004).
[6]
TISSUE SPECIFICITY.
PubMed=15958417; DOI=10.1093/glycob/cwi094;
Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.;
"Characterization of the LARGE family of putative glycosyltransferases
associated with dystroglycanopathies.";
Glycobiology 15:912-923(2005).
[7]
FUNCTION, AND PATHWAY.
PubMed=15184894; DOI=10.1038/nm1059;
Barresi R., Michele D.E., Kanagawa M., Harper H.A., Dovico S.A.,
Satz J.S., Moore S.A., Zhang W., Schachter H., Dumanski J.P.,
Cohn R.D., Nishino I., Campbell K.P.;
Nat. Med. 10:696-703(2004).
[8]
FUNCTION.
PubMed=23125099; DOI=10.1093/glycob/cws152;
Inamori K., Hara Y., Willer T., Anderson M.E., Zhu Z.,
Yoshida-Moriguchi T., Campbell K.P.;
"Xylosyl- and glucuronyltransferase functions of LARGE in alpha-
dystroglycan modification are conserved in LARGE2.";
Glycobiology 23:295-302(2013).
[9]
FUNCTION.
PubMed=23135544; DOI=10.1093/glycob/cws153;
Ashikov A., Buettner F.F., Tiemann B., Gerardy-Schahn R., Bakker H.;
"LARGE2 generates the same xylose- and glucuronic acid-containing
glycan structures as LARGE.";
Glycobiology 23:303-309(2013).
[10]
FUNCTION, AND PATHWAY.
PubMed=24132234; DOI=10.1038/nature12605;
Goddeeris M.M., Wu B., Venzke D., Yoshida-Moriguchi T., Saito F.,
Matsumura K., Moore S.A., Campbell K.P.;
"LARGE glycans on dystroglycan function as a tunable matrix scaffold
to prevent dystrophy.";
Nature 503:136-140(2013).
[11]
FUNCTION.
PubMed=25138275; DOI=10.1074/jbc.M114.597831;
Inamori K., Willer T., Hara Y., Venzke D., Anderson M.E., Clarke N.F.,
Guicheney P., Bonnemann C.G., Moore S.A., Campbell K.P.;
"Endogenous glucuronyltransferase activity of LARGE or LARGE2 required
for functional modification of alpha-dystroglycan in cells and
tissues.";
J. Biol. Chem. 289:28138-28148(2014).
-!- FUNCTION: Bifunctional glycosyltransferase with both
xylosyltransferase and beta-1,3-glucuronyltransferase activities
involved in the biosynthesis of the phosphorylated O-mannosyl
trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-
beta-4-(phosphate-6-)mannose), a carbohydrate structure present in
alpha-dystroglycan (DAG1) (PubMed:23125099, PubMed:23135544).
Phosphorylated O-mannosyl trisaccharid is required for binding
laminin G-like domain-containing extracellular proteins with high
affinity and plays a key role in skeletal muscle function and
regeneration (PubMed:15184894, PubMed:24132234). LARGE elongates
the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure
initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-
alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By
similarity). {ECO:0000250|UniProtKB:O95461,
ECO:0000269|PubMed:15184894, ECO:0000269|PubMed:23125099,
ECO:0000269|PubMed:23135544, ECO:0000269|PubMed:24132234,
ECO:0000269|PubMed:25138275}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:O95461};
Note=Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part
binds one Mn(2+) and the beta-1,3-glucuronyltransferase part binds
one Mn(2+). {ECO:0000250|UniProtKB:O95461};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:15184894, ECO:0000269|PubMed:24132234}.
-!- SUBUNIT: Interacts with DAG1 (via the N-terminal domain of alpha-
DAG1); the interaction increases binding of DAG1 to laminin.
Interacts with B3GNT1/B4GAT1. {ECO:0000250|UniProtKB:O95461,
ECO:0000269|PubMed:15210115}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:O95461}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:O95461}.
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in heart,
diaphragm and brain, where it is especially found in cerebral
cortex, hippocampus, and trigeminal ganglion.
{ECO:0000269|PubMed:15958417}.
-!- DEVELOPMENTAL STAGE: Ubiquitously found at 14.5 dpc with strong
expression in heart, central nervous system structures such as
cerebral cortex, hippocampus, olfactory lobe, trigeminal ganglion
and spinal cord. Also expressed in diaphragm and duodenum.
-!- DISEASE: Note=Defects in Large are the cause of myodystrophy
(myd), an autosomal recessive neuromuscular phenotype, probably
due to abnormal post-translational modification of alpha-
dystroglycan. {ECO:0000269|PubMed:11381262}.
-!- SIMILARITY: In the C-terminal section; belongs to the
glycosyltransferase 49 family. {ECO:0000305}.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 8 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH61506.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC65610.1; Type=Frameshift; Positions=48; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Large like-glycosyltransferase;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_589";
-----------------------------------------------------------------------
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EMBL; AJ006278; CAA06945.1; -; mRNA.
EMBL; AK122328; BAC65610.1; ALT_FRAME; mRNA.
EMBL; BC061506; AAH61506.1; ALT_INIT; mRNA.
EMBL; BC100399; AAI00400.1; -; mRNA.
CCDS; CCDS22420.1; -.
RefSeq; NP_001304320.1; NM_001317391.1.
RefSeq; NP_034817.1; NM_010687.2.
UniGene; Mm.324371; -.
ProteinModelPortal; Q9Z1M7; -.
STRING; 10090.ENSMUSP00000004497; -.
CAZy; GT49; Glycosyltransferase Family 49.
CAZy; GT8; Glycosyltransferase Family 8.
PhosphoSitePlus; Q9Z1M7; -.
MaxQB; Q9Z1M7; -.
PaxDb; Q9Z1M7; -.
PRIDE; Q9Z1M7; -.
Ensembl; ENSMUST00000004497; ENSMUSP00000004497; ENSMUSG00000004383.
Ensembl; ENSMUST00000119826; ENSMUSP00000112617; ENSMUSG00000004383.
Ensembl; ENSMUST00000212459; ENSMUSP00000148336; ENSMUSG00000004383.
GeneID; 16795; -.
KEGG; mmu:16795; -.
UCSC; uc009mgs.1; mouse.
CTD; 9215; -.
MGI; MGI:1342270; Large1.
eggNOG; KOG3765; Eukaryota.
eggNOG; ENOG410XRNY; LUCA.
GeneTree; ENSGT00530000063165; -.
HOGENOM; HOG000231467; -.
HOVERGEN; HBG052308; -.
InParanoid; Q9Z1M7; -.
KO; K09668; -.
OMA; NKQYRVC; -.
OrthoDB; EOG091G034V; -.
PhylomeDB; Q9Z1M7; -.
TreeFam; TF319168; -.
Reactome; R-MMU-5173105; O-linked glycosylation.
UniPathway; UPA00378; -.
PRO; PR:Q9Z1M7; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000004383; -.
CleanEx; MM_LARGE; -.
ExpressionAtlas; Q9Z1M7; baseline and differential.
Genevisible; Q9Z1M7; MM.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IMP:MGI.
GO; GO:0042285; F:xylosyltransferase activity; IDA:UniProtKB.
GO; GO:0009101; P:glycoprotein biosynthetic process; NAS:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
GO; GO:0035269; P:protein O-linked mannosylation; IDA:UniProtKB.
GO; GO:0060538; P:skeletal muscle organ development; IDA:UniProtKB.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:UniProtKB.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR002495; Glyco_trans_8.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF01501; Glyco_transf_8; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Metal-binding;
Multifunctional enzyme; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 756 LARGE xylosyl- and glucuronyltransferase
1.
/FTId=PRO_0000206061.
TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 756 Lumenal. {ECO:0000255}.
REGION 138 413 Xylosyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
REGION 414 756 Glucuronyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
COILED 53 95 {ECO:0000255}.
METAL 242 242 Manganese 1.
{ECO:0000250|UniProtKB:O95461}.
METAL 244 244 Manganese 1.
{ECO:0000250|UniProtKB:O95461}.
METAL 563 563 Manganese 2.
{ECO:0000250|UniProtKB:O95461}.
METAL 565 565 Manganese 2.
{ECO:0000250|UniProtKB:O95461}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 269 269 L -> S (in Ref. 3; AAI00400).
{ECO:0000305}.
CONFLICT 324 324 L -> H (in Ref. 3; AAI00400).
{ECO:0000305}.
CONFLICT 441 441 D -> N (in Ref. 3; AAI00400).
{ECO:0000305}.
CONFLICT 748 748 K -> E (in Ref. 3; AAI00400).
{ECO:0000305}.
SEQUENCE 756 AA; 87964 MW; 37B32E039AB8895F CRC64;
MLGICRGRRK FLAASLTLLC IPAITWIYLF AGSFEDGKPV SLSPLESQAH SPRYTASSQR
ERESLEVRVR EVEEENRALR RQLSLAQGQS PAHHRGNHSK TYSMEEGTGD SENLRAGIVA
GNSSECGQQP AVEKCETIHV AIVCAGYNAS RDVVTLVKSV LFHRRNPLHF HLIADSIAEQ
ILATLFQTWM VPAVRVDFYN ADELKSEVSW IPNKHYSGIY GLMKLVLTKT LPANLERVIV
LDTDITFATD IAELWAVFHK FKGQQVLGLV ENQSDWYLGN LWKNHRPWPA LGRGYNTGVI
LLLLDKLRKM KWEQMWRLTA ERELMGMLST SLADQDIFNA VIKQNPFLVY QLPCFWNVQL
SDHTRSEQCY RDVSDLKVIH WNSPKKLRVK NKHVEFFRNL YLTFLEYDGN LLRRELFGCP
SETDVNNENL QKQLSELDED DLCYEFRRER FTVHRTHLYF LHYEFEPSAD NTDVTLVAQL
SMDRLQMLEA ICKHWEGPIS LALYLSDAEA QQFLRYAQGS EVLMSRQNVG YHIVYKEGQF
YPVNLLRNVA MKHISTPYMF LSDIDFLPMY GLYEYLRKSV IQLDLANTKK AMIVPAFETL
RYRLSFPKSK AELLSMLDMG TLFTFRYHVW TKGHAPTNFA KWRTATTPYQ VEWEADFEPY
VVVRRDCPEY DRRFVGFGWN KVAHIMELDA QEYEFTVLPN AYMIHMPHAP SFDITKFRSN
KQYRICLKTL KEEFQQDMSR RYGFAALKYL TAENNS


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