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

 LRG2B_XENLA             Reviewed;         723 AA.
Q32NJ7;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
10-MAY-2017, entry version 54.
RecName: Full=LARGE xylosyl- and glucuronyltransferase 2-B {ECO:0000250|UniProtKB:Q8N3Y3};
EC=2.4.-.-;
AltName: Full=Glycosyltransferase-like 1B-B;
Includes:
RecName: Full=Xylosyltransferase LARGE2-B {ECO:0000305};
EC=2.4.2.-;
Includes:
RecName: Full=Beta-1,3-glucuronyltransferase LARGE2-B {ECO:0000305};
EC=2.4.1.-;
Name=large2-b {ECO:0000250|UniProtKB:Q8N3Y3}; Synonyms=gyltl1b-b;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
-!- 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; BC108590; AAI08591.1; -; mRNA.
RefSeq; NP_001089877.1; NM_001096408.1.
UniGene; Xl.50952; -.
ProteinModelPortal; Q32NJ7; -.
GeneID; 734944; -.
KEGG; xla:734944; -.
CTD; 734944; -.
Xenbase; XB-GENE-6256639; large1.
HOVERGEN; HBG052308; -.
KO; K09668; -.
UniPathway; UPA00378; -.
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: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;
Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese;
Membrane; Metal-binding; Multifunctional enzyme; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 723 LARGE xylosyl- and glucuronyltransferase
2-B.
/FTId=PRO_0000226817.
TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 723 Lumenal. {ECO:0000255}.
REGION 107 382 Xylosyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
REGION 383 723 Glucuronyltransferase activity.
{ECO:0000250|UniProtKB:O95461}.
METAL 211 211 Manganese 1.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 213 213 Manganese 1.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 530 530 Manganese 2.
{ECO:0000250|UniProtKB:Q8N3Y3}.
METAL 532 532 Manganese 2.
{ECO:0000250|UniProtKB:Q8N3Y3}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 723 AA; 83091 MW; 80E4A0B7DE935169 CRC64;
MLCSCRSKSK FLALTLLLLS AATWLYLSVG ETEYGPSLGP VAPHFSATSL FQVELESRLR
EAEEENRRLR QQLGEIRNEE QSPGGGTEGD NSSHCEHRSL TEKCELIHVA IVCAGHNSSR
DVVTLVKSIL FHRRNPLHLH LITDDVALRV LRNLFNTWMV PSLTISFYNA SELKPDVAWI
PNKHYSGIFG LLKLTLTKAL PSYLSKVIVL DTDITFATDI AELWAIFKKF TGEQVLGLVE
NQSDWYLGNL WKNHKPWPAL GRGFNTGVIL LLLDKLRLIG WEEMWRLTAE RELMNMLSTS
LADQDIFNAV IKSSPTLVYQ LPCYWNVQLS DHTRSEQCYS ELADLKVIHW NSPHKLRVKN
KHVELFRTLY LTFLEYDGSL LRRELIGCPS EGEQQGGSQA ALSQLDEEDP CYDFRRESLA
SHRVHLSFLP HLTPTPDPSD VTLVAQLSMD RLQMLELICR HWEGPMSLAL YLSDAEAQQF
LRYAQASEVL QSRTNIGYHV IYKEGQLYPV NLLRNVALKN SHTPYVFLSD IDFLPMYGLY
ENLRKSIAQQ DPTGSPKALI VPAFETLRYR LSFPKSKADL LSMLDTGALY TFRYHVWEKG
HAPTNYAKWR TATTPYRVEW APDFEPYVVV RQDCPEYDQR FLGFGWNKVS HIMELDAQEY
ELLVLPNAFI IHMPHAPSFD ISKFRSSEHY RRCVQVLKEE FHQDLSRRYG SAALKYLAAE
RNQ


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