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LARGE xylosyl- and glucuronyltransferase 2 (EC 2.4.-.-) (Glycosyltransferase-like 1B) [Includes: Xylosyltransferase LARGE2 (EC 2.4.2.-); Beta-1,3-glucuronyltransferase LARGE2 (EC 2.4.1.-)]

 LARG2_DANRE             Reviewed;         750 AA.
Q66PG1; Q1LUJ7; Q1LV71;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
27-SEP-2017, entry version 87.
RecName: Full=LARGE xylosyl- and glucuronyltransferase 2 {ECO:0000250|UniProtKB:Q8N3Y3};
EC=2.4.-.-;
AltName: Full=Glycosyltransferase-like 1B;
Includes:
RecName: Full=Xylosyltransferase LARGE2 {ECO:0000305};
EC=2.4.2.-;
Includes:
RecName: Full=Beta-1,3-glucuronyltransferase LARGE2 {ECO:0000305};
EC=2.4.1.-;
Name=large2 {ECO:0000250|UniProtKB:Q8N3Y3}; Synonyms=gyltl1b;
ORFNames=si:ch211-206g24.1, si:ch211-282n12.1;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
-!- 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). Phosphorylated O-mannosyl trisaccharid
is required for binding laminin G-like domain-containing
extracellular proteins with high affinity. Elongates the
glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by
adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to
produce a heteropolysaccharide. Has a higher activity toward
alpha-dystroglycan than LARGE. {ECO:0000250|UniProtKB:Q5XPT3}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q8N3Y3};
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:Q8N3Y3};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000250|UniProtKB:Q5XPT3}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q5XPT3}; Single-pass type II membrane
protein {ECO:0000305}.
-!- 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}.
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EMBL; AY662339; AAU12252.1; -; mRNA.
EMBL; BX908385; CAK04901.1; -; Genomic_DNA.
EMBL; BX936304; CAK04442.1; -; Genomic_DNA.
RefSeq; NP_001004538.1; NM_001004538.1.
RefSeq; XP_017207405.1; XM_017351916.1.
UniGene; Dr.36508; -.
ProteinModelPortal; Q66PG1; -.
STRING; 7955.ENSDARP00000108343; -.
CAZy; GT49; Glycosyltransferase Family 49.
CAZy; GT8; Glycosyltransferase Family 8.
PaxDb; Q66PG1; -.
Ensembl; ENSDART00000015786; ENSDARP00000019858; ENSDARG00000017058.
Ensembl; ENSDART00000127953; ENSDARP00000108343; ENSDARG00000017058.
Ensembl; ENSDART00000172328; ENSDARP00000130814; ENSDARG00000017058.
GeneID; 446214; -.
KEGG; dre:446214; -.
CTD; 446214; -.
ZFIN; ZDB-GENE-050419-253; gyltl1b.
eggNOG; KOG3765; Eukaryota.
eggNOG; ENOG410XRNY; LUCA.
GeneTree; ENSGT00530000063165; -.
HOGENOM; HOG000231467; -.
HOVERGEN; HBG052308; -.
InParanoid; Q66PG1; -.
KO; K09668; -.
OMA; CPEYDQR; -.
OrthoDB; EOG091G034V; -.
PhylomeDB; Q66PG1; -.
TreeFam; TF319168; -.
Reactome; R-DRE-5173105; O-linked glycosylation.
UniPathway; UPA00378; -.
PRO; PR:Q66PG1; -.
Proteomes; UP000000437; Chromosome 18.
Bgee; ENSDARG00000017058; -.
ExpressionAtlas; Q66PG1; baseline.
GO; GO:0005794; C:Golgi apparatus; ISS:ZFIN.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042285; F:xylosyltransferase activity; ISS:UniProtKB.
GO; GO:0006486; P:protein glycosylation; ISS:ZFIN.
GO; GO:0035269; P:protein O-linked mannosylation; ISS: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.
2: Evidence at transcript level;
Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
Manganese; Membrane; Metal-binding; Multifunctional enzyme;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 750 LARGE xylosyl- and glucuronyltransferase
2.
/FTId=PRO_0000226815.
TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 750 Lumenal. {ECO:0000255}.
REGION 132 407 Xylosyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
REGION 408 750 Glucuronyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
METAL 236 236 Manganese 1.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 238 238 Manganese 1.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 557 557 Manganese 2.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 559 559 Manganese 2.
{ECO:0000250|UniProtKB:Q8N3Y3}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 87 87 A -> V (in Ref. 2; CAK04442).
{ECO:0000305}.
SEQUENCE 750 AA; 86987 MW; 79C9BAC9F707CBB2 CRC64;
MLCPCRGKLK LLVVSLSFVI LFTWLYLLVG NSENGRSLLL SACLVESTEA RLLERDVLAS
RVREVEEENR QIRLQLSQSQ GLAGQPAEGN YGNQQWVASA DTGPEDVENT AEERANHSEC
SRSPTAEKCE LLHVACVCAG HNASRDVVTL VKSILFHRRN PLHFHFITDT VANQILSTLF
QSWMVPSVQV SFYDADELKS EVSWIPNKHY SGIYGLMKLT LTKALPSNLS KVIVLDTDIT
FATDIAELWA IFRKFTEKQV IGLVENQSDW YLGNLWKNHK PWPALGRGFN TGVILLYLER
LRRMGWEQMW RLTAERELMS MLSTSLADQD IFNAFIKQNP VLVHQLPCFW NVQLSDHTRS
EQCYTEVSDL KVIHWNSPKK LRVKNKHVEF FRNLYLTFLE YDGNLLRREL FGCPSQASSE
STVLQQALEE LDEDDQCYDF RRERIMLHRV HLYFLQYEYS PTDDGTDITL VAQLSMDRLQ
MLEAICKHWE GPISLALYMS DAEAQQFLRY AQASEVLKNR KNVGYHIVYK EGQFYPVNLV
RNVALRNVNT PYVFLTDVDF LPMYGLYDYL RKSIVQLDMA NTKKALVVPA FETLRYRLSF
PKSKAELLSM LDMGTLYTFR YHVWTKGHAP TNYAKWRTAT TPYKVEWEAD FEPYVVVRRD
CPEYDQRFVG FGWNKVSHIM ELDAQEYDLI VLPNAFMIHM PHAPSFDISK FRSSPSYRYC
LTTLKDEFHQ DLSRKYGSAA LKYLTAQRNI


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