LARG2_CHICK
ID LARG2_CHICK Reviewed; 739 AA.
AC Q66PG4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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;
DE AltName: Full=LARGE xylosyl- and glucuronyltransferase 2 {ECO:0000250|UniProtKB:Q8N3Y3};
DE Includes:
DE RecName: Full=Alpha-1,3-xylosyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q5XPT3};
DE Includes:
DE RecName: Full=Beta-1,3-glucuronyltransferase LARGE2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q5XPT3};
GN Name=LARGE2 {ECO:0000250|UniProtKB:Q8N3Y3}; Synonyms=GYLTL1B;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15958417; DOI=10.1093/glycob/cwi094;
RA Grewal P.K., McLaughlan J.M., Moore C.J., Browning C.A., Hewitt J.E.;
RT "Characterization of the LARGE family of putative glycosyltransferases
RT associated with dystroglycanopathies.";
RL Glycobiology 15:912-923(2005).
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; AY662336; AAU12249.1; -; mRNA.
DR RefSeq; NP_001004404.1; NM_001004404.2.
DR AlphaFoldDB; Q66PG4; -.
DR SMR; Q66PG4; -.
DR STRING; 9031.ENSGALP00000037568; -.
DR CAZy; GT49; Glycosyltransferase Family 49.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR PaxDb; Q66PG4; -.
DR GeneID; 423200; -.
DR KEGG; gga:423200; -.
DR CTD; 120071; -.
DR VEuPathDB; HostDB:geneid_423200; -.
DR eggNOG; KOG3765; Eukaryota.
DR InParanoid; Q66PG4; -.
DR OrthoDB; 729091at2759; -.
DR PhylomeDB; Q66PG4; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q66PG4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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..739
FT /note="Xylosyl- and glucuronyltransferase LARGE2s"
FT /id="PRO_0000226814"
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..739
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 80..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..396
FT /note="Xylosyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT REGION 397..739
FT /note="Glucuronyltransferase activity"
FT /evidence="ECO:0000250|UniProtKB:O95461"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 546
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT BINDING 548
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Y3"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 739 AA; 85568 MW; CF65F7C0E65414AE CRC64;
MLCSWRVKLK LLLATITLAV LLSWLYLFVG SLEYGRFLLL PPCLGEQPSR DVEREALASQ
VRRVEEENQQ LRMQLGQVQA EGSDGNPQWA ASAEDGPPLG GERNNRTACP EQRMVRKCEL
LHVAIVCAGH NASRDVVTLV KSILFHRKNP LHFHFITDSV AHQILQTLFQ SWMVPSIHVS
FYNADDLKPE VSWIPNKHYS GIYGLMKLTL TKALPSNLSK VIVLDTDITF ATDIAELWAV
FGKFSEKQVI GLVENQSDWY LGNLWKNHKP WPALGRGFNT GVILLLLDRL RRLGWEQMWR
LTAERELMSM LSTSLADQDI FNAVIKQNPA LVYRLPCFWN VQLSDHTRSE LCYTEVSDLK
VIHWNSPKKL RVKNKHVEFF RNLYLTFLEY DGNLLRRELF GCASLPSPPS DQLQQALEEL
DEDDPCYDFR RQHLTQHRVH LFFLQYEFLA LPNPTDVTLV AQLSMDRLQM LEAICKHWAG
PISLALYMSD AEAQQFLRYA QASEVLSARR NVAYHIVYKE GQFYPINLLR NVALANTQTP
YVFLTDIDFL PMYGLYDYLR NSIQQLELPH RKAALIVPAF ETLHYRLTFP KSKAELLSML
DMGSLYTFRY HVWPKGHAPT DYAKWRTATV PYRVAWQPDF EPYVVVRRDC PKYDQRFVGF
GWNKVSHIME LDAQEYELLV LPNAFMIHMP HAPSFDISKF RLSAGYRGCL QTLREEFHQD
LSRKYGAAAL KYLTAERNL
