B4GT7_MOUSE
ID B4GT7_MOUSE Reviewed; 327 AA.
AC Q8R087; Q7TNU3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Beta-1,4-galactosyltransferase 7;
DE Short=Beta-1,4-GalTase 7;
DE Short=Beta4Gal-T7;
DE Short=b4Gal-T7;
DE EC=2.4.1.-;
DE AltName: Full=Proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 7;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 7;
DE AltName: Full=UDP-galactose:beta-xylose beta-1,4-galactosyltransferase;
DE AltName: Full=XGPT;
DE AltName: Full=XGalT-1;
DE AltName: Full=Xylosylprotein 4-beta-galactosyltransferase;
DE EC=2.4.1.133;
DE AltName: Full=Xylosylprotein beta-1,4-galactosyltransferase;
GN Name=B4galt7; Synonyms=Xgalt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage
CC region of proteoglycans, especially for small proteoglycans in skin
CC fibroblasts. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose
CC = 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:15297, Rhea:RHEA-COMP:12567, Rhea:RHEA-
CC COMP:12570, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132085, ChEBI:CHEBI:132088; EC=2.4.1.133;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Cis cisternae of Golgi stack. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R087-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R087-2; Sequence=VSP_014231;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b4GalT7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_466";
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DR EMBL; BC027195; AAH27195.1; -; mRNA.
DR EMBL; BC055703; AAH55703.1; -; mRNA.
DR CCDS; CCDS26550.1; -. [Q8R087-1]
DR CCDS; CCDS79190.1; -. [Q8R087-2]
DR RefSeq; NP_001298066.1; NM_001311137.1. [Q8R087-2]
DR RefSeq; NP_666157.1; NM_146045.2. [Q8R087-1]
DR AlphaFoldDB; Q8R087; -.
DR SMR; Q8R087; -.
DR BioGRID; 230009; 1.
DR STRING; 10090.ENSMUSP00000068532; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q8R087; 1 site.
DR PhosphoSitePlus; Q8R087; -.
DR SwissPalm; Q8R087; -.
DR MaxQB; Q8R087; -.
DR PaxDb; Q8R087; -.
DR PRIDE; Q8R087; -.
DR ProteomicsDB; 273592; -. [Q8R087-1]
DR ProteomicsDB; 273593; -. [Q8R087-2]
DR Antibodypedia; 29347; 125 antibodies from 21 providers.
DR DNASU; 218271; -.
DR Ensembl; ENSMUST00000064701; ENSMUSP00000068532; ENSMUSG00000021504. [Q8R087-1]
DR Ensembl; ENSMUST00000100764; ENSMUSP00000098327; ENSMUSG00000021504. [Q8R087-2]
DR GeneID; 218271; -.
DR KEGG; mmu:218271; -.
DR UCSC; uc007qru.1; mouse. [Q8R087-1]
DR UCSC; uc011yzw.1; mouse. [Q8R087-2]
DR CTD; 11285; -.
DR MGI; MGI:2384987; B4galt7.
DR VEuPathDB; HostDB:ENSMUSG00000021504; -.
DR eggNOG; KOG3917; Eukaryota.
DR GeneTree; ENSGT00940000157712; -.
DR InParanoid; Q8R087; -.
DR OMA; QMNGMSN; -.
DR PhylomeDB; Q8R087; -.
DR TreeFam; TF312834; -.
DR Reactome; R-MMU-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 218271; 8 hits in 75 CRISPR screens.
DR ChiTaRS; B4galt7; mouse.
DR PRO; PR:Q8R087; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R087; protein.
DR Bgee; ENSMUSG00000021504; Expressed in saccule of membranous labyrinth and 246 other tissues.
DR ExpressionAtlas; Q8R087; baseline and differential.
DR Genevisible; Q8R087; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0008378; F:galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0046525; F:xylosylprotein 4-beta-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006029; P:proteoglycan metabolic process; ISS:UniProtKB.
DR GO; GO:0097435; P:supramolecular fiber organization; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Beta-1,4-galactosyltransferase 7"
FT /id="PRO_0000080551"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 61..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..104
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 139..141
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 164..165
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 194
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 224
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 226..229
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 257..259
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 266
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 241..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014231"
SQ SEQUENCE 327 AA; 37754 MW; F79B656325DCFDE0 CRC64;
MLPSRRKAAQ LPWEDGRARL LPGGLRRKCS IFHLFIAFLL LVFFSLLWLQ LSCSGDMAQV
TRGQGQETSG PPRACPPEPP PEHWEEDESW GPHRLAVLVP FRERFEELLV FVPHMHRFLS
RKRIQHHIYV LNQVDHFRFN RAALINVGFL ESSNSTDYIA MHDVDLLPLN EELDYGFPEA
GPFHVASPEL HPLYHYKTYV GGILLLSKQH YQLCNGMSNR FWGWGREDDE FYRRIKGAGL
QLFRPSGITT GYQTFRHLHD PAWRKRDQKR IAAQKQEQFK VDREGGLNTV KYRVDSRTAL
SIGGAPCTVL NVMLDCDKTA TPWCIFG
