LRG2A_XENLA
ID LRG2A_XENLA Reviewed; 723 AA.
AC Q6PA90;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Xylosyl- and glucuronyltransferase LARGE2s {ECO:0000250|UniProtKB:Q8N3Y3};
DE EC=2.4.-.- {ECO:0000250|UniProtKB:Q5XPT3};
DE AltName: Full=Glycosyltransferase-like 1B-A;
DE AltName: Full=LARGE xylosyl- and glucuronyltransferase 2-A {ECO:0000250|UniProtKB:Q8N3Y3};
DE Includes:
DE RecName: Full=Alpha-1,3-xylosyltransferase LARGE2-A {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q5XPT3};
DE Includes:
DE RecName: Full=Beta-1,3-glucuronyltransferase LARGE2-A {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q5XPT3};
GN Name=large2-a {ECO:0000250|UniProtKB:Q8N3Y3}; Synonyms=gyltl1b-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3-
CC xylosyltransferase and beta-1,3-glucuronyltransferase activities
CC involved in the maturation of alpha-dystroglycan (DAG1) by
CC glycosylation leading to DAG1 binding to laminin G-like domain-
CC containing extracellular proteins with high affinity and in a
CC phosphorylated-O-mannosyl trisaccharide dependent manner. Elongates the
CC glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding
CC repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a
CC heteropolysaccharide (By similarity). Supports the maturation of DAG1
CC more effectively than LARGE1 (By similarity). In addition, can modify
CC both heparan sulfate (HS)- and chondroitin/dermatan sulfate (CS/DS)-
CC proteoglycans (PGs), namely GPC4, with a glycosaminoglycan (GAG)-like
CC polysaccharide composed of xylose and glucuronic acid to confer laminin
CC binding (By similarity). {ECO:0000250|UniProtKB:Q5XPT3,
CC ECO:0000250|UniProtKB:Q8N3Y3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-
CC beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-
CC [protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-
CC beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:57336, Rhea:RHEA-COMP:17482, Rhea:RHEA-COMP:17483,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177336, ChEBI:CHEBI:177352;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57337;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-
CC D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-
CC (1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-alpha-D-glucuronate =
CC 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-
CC beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-
CC GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:67924, Rhea:RHEA-COMP:17484, Rhea:RHEA-COMP:17486,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67925;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-
CC alpha-D-xylose = 3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-
CC (1->](n+1)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-
CC (1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+)
CC + UDP; Xref=Rhea:RHEA:68368, Rhea:RHEA-COMP:17485, Rhea:RHEA-
CC COMP:17486, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:177354, ChEBI:CHEBI:177355;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68369;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q5XPT3};
CC Note=Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds
CC one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one
CC Mn(2+). {ECO:0000250|UniProtKB:Q5XPT3};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q5XPT3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q5XPT3}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q5XPT3}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC glycosyltransferase 49 family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; BC060410; AAH60410.1; -; mRNA.
DR RefSeq; NP_001083457.1; NM_001089988.1.
DR AlphaFoldDB; Q6PA90; -.
DR SMR; Q6PA90; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR DNASU; 398936; -.
DR GeneID; 398936; -.
DR KEGG; xla:398936; -.
DR CTD; 398936; -.
DR Xenbase; XB-GENE-5872007; large2.S.
DR OrthoDB; 729091at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 398936; Expressed in internal ear and 19 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042285; F:xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Multifunctional enzyme; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..723
FT /note="Xylosyl- and glucuronyltransferase LARGE2s"
FT /id="PRO_0000226816"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..723
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 73..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..382
FT /note="Xylosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT REGION 383..723
FT /note="Glucuronyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 530
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 532
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 723 AA; 83148 MW; 7AC84BE1AB5C91BA CRC64;
MLFSCRSKAK LLALTLLLLS AATWLYLSVG ETEYGQSLGP VAPRFSATPS FQMELEIRLR
EAKEENRRLR QQLGEVRNEE QSTGGGTEGD NSSHCEHRSL TEKCELIHVA IVCAGHNSSR
DVVTLVKSIL FHRRNPLHLH LITDDVALRV LGNLFNTWMV PSLQISFYNA SELKPDVAWI
PNKHYSGIYG LLKLTLTKAL PSDLSKVIVL DTDITFATDI AELWAIFKKF TGEQVLGLVE
NQSDWYLGNL WKNHKPWPAL GRGFNTGVIL LLLDKLRLIG WEEMWRLTAE RELMNMLSTS
LADQDIFNAV IKSSPTLVYQ LPCYWNVQLS DHTRSEQCYS ELADLKVIHW NSPHKLRVKN
KHVELFRTLY LTFLEYDGSL LRRELIGCPS EGEQQGGSQA TLSQLDEEDP CYDFRRESVA
SHRVHLSFLP HLTPPPDPYD VTLVAQLSMD RLQMLELICR HWEGPMSLAL YLSDAEAQQF
LRYAQASEVL QSRTNIGYHV VYKEGQLYPV NLLRNVALKN SHTPYVFLSD IDFLPMYGLY
EYLRKSIAQQ DPAGSPRALI VPAFETLRYR LSFPKSKADL LSMLDTGALY TFRYHVWEKG
HAPTDYAKWR TATTPYRVEW APDFEPYVVV RRDCPEYDQR FLGFGWNKVS HIMELDAQEY
ELVVLPNAFI VHMPHAPSFD ISKFRSSENY RLCVQALKEE FHQDLSRRYG SAALKYLTAE
RNR
