GGTA1_MOUSE
ID GGTA1_MOUSE Reviewed; 394 AA.
AC P23336; Q91V22;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=N-acetyllactosaminide alpha-1,3-galactosyltransferase;
DE EC=2.4.1.87 {ECO:0000250|UniProtKB:P14769};
DE AltName: Full=UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase;
DE Short=Galactosyltransferase;
GN Name=Ggta1; Synonyms=Ggta-1;
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 [MRNA].
RX PubMed=2510162; DOI=10.1073/pnas.86.21.8227;
RA Larsen R.D., Rajan V.P., Ruff M.M., Kukowska-Latallo J., Cummings R.D.,
RA Lowe J.B.;
RT "Isolation of a cDNA encoding a murine UDPgalactose:beta-D-galactosyl-1,4-
RT N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase: expression
RT cloning by gene transfer.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8227-8231(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=1544928; DOI=10.1016/s0021-9258(18)42799-8;
RA Joziasse D.H., Shaper N.L., Kim D., van den Eijnden D.H., Shaper J.H.;
RT "Murine alpha 1,3-galactosyltransferase. A single gene locus specifies four
RT isoforms of the enzyme by alternative splicing.";
RL J. Biol. Chem. 267:5534-5541(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ;
RX PubMed=11267031; DOI=10.1016/s0041-1345(00)02216-8;
RA Koike C., Friday R., Fung J.J., Starzl T.E., Trucco M.;
RT "Comparison of the regulatory regions of the alpha1,3galactosyltransferase
RT gene between murine and porcine species.";
RL Transplant. Proc. 33:710-711(2001).
RN [4]
RP FUNCTION.
RX PubMed=12626403; DOI=10.1093/glycob/cwg030;
RA Taylor S.G., McKenzie I.F., Sandrin M.S.;
RT "Characterization of the rat alpha(1,3)galactosyltransferase: evidence for
RT two independent genes encoding glycosyltransferases that synthesize
RT Galalpha(1,3)Gal by two separate glycosylation pathways.";
RL Glycobiology 13:327-337(2003).
CC -!- FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by
CC catalyzing the transfer of a galactose residue, with an alpha-1,3
CC linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide
CC borne by a glycoprotein or a glycolipid. Preferentially glycosylates
CC proteins, can synthesize galactose-alpha(1,3)-galactose on
CC glycoproteins but cannot synthesize the glycolipid called
CC isoglobotrihexosylceramide or isogloboside 3 (iGb3).
CC {ECO:0000269|PubMed:12626403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative +
CC H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507,
CC ChEBI:CHEBI:138024; EC=2.4.1.87;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P14769}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P23336-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P23336-2; Sequence=VSP_001804;
CC Name=3;
CC IsoId=P23336-3; Sequence=VSP_001804, VSP_001805;
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
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DR EMBL; M26925; AAA37657.1; -; mRNA.
DR EMBL; M85153; AAA37711.1; -; mRNA.
DR EMBL; AF297614; AAK97205.1; -; Genomic_DNA.
DR EMBL; AF297609; AAK97205.1; JOINED; Genomic_DNA.
DR EMBL; AF297610; AAK97205.1; JOINED; Genomic_DNA.
DR EMBL; AF297611; AAK97205.1; JOINED; Genomic_DNA.
DR EMBL; AF297612; AAK97205.1; JOINED; Genomic_DNA.
DR EMBL; AF297613; AAK97205.1; JOINED; Genomic_DNA.
DR EMBL; AF297615; AAK97206.1; -; mRNA.
DR CCDS; CCDS50576.1; -. [P23336-1]
DR PIR; A34417; A34417.
DR PIR; I49698; I49698.
DR RefSeq; NP_001139293.1; NM_001145821.2. [P23336-1]
DR AlphaFoldDB; P23336; -.
DR SMR; P23336; -.
DR STRING; 10090.ENSMUSP00000099858; -.
DR BindingDB; P23336; -.
DR ChEMBL; CHEMBL2479; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GlyGen; P23336; 2 sites.
DR iPTMnet; P23336; -.
DR PhosphoSitePlus; P23336; -.
DR EPD; P23336; -.
DR MaxQB; P23336; -.
DR PaxDb; P23336; -.
DR PeptideAtlas; P23336; -.
DR PRIDE; P23336; -.
DR ProteomicsDB; 271215; -. [P23336-1]
DR ProteomicsDB; 271216; -. [P23336-2]
DR ProteomicsDB; 271217; -. [P23336-3]
DR DNASU; 14594; -.
DR Ensembl; ENSMUST00000113002; ENSMUSP00000108626; ENSMUSG00000035778. [P23336-1]
DR Ensembl; ENSMUST00000164889; ENSMUSP00000132408; ENSMUSG00000035778. [P23336-1]
DR GeneID; 14594; -.
DR KEGG; mmu:14594; -.
DR UCSC; uc008jkm.2; mouse. [P23336-1]
DR CTD; 2681; -.
DR MGI; MGI:95704; Ggta1.
DR VEuPathDB; HostDB:ENSMUSG00000035778; -.
DR eggNOG; ENOG502QW2H; Eukaryota.
DR GeneTree; ENSGT00950000182858; -.
DR InParanoid; P23336; -.
DR BRENDA; 2.4.1.87; 3474.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14594; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ggta1; mouse.
DR PRO; PR:P23336; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P23336; protein.
DR Bgee; ENSMUSG00000035778; Expressed in decidua and 221 other tissues.
DR ExpressionAtlas; P23336; baseline and differential.
DR Genevisible; P23336; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0031985; C:Golgi cisterna; ISS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047276; F:N-acetyllactosaminide 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
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..394
FT /note="N-acetyllactosaminide alpha-1,3-
FT galactosyltransferase"
FT /id="PRO_0000157299"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..60
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..394
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 160..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 251..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 273..276
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 385..391
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267031"
FT /id="VSP_001804"
FT VAR_SEQ 62
FT /note="R -> SPDGSFLWIYHTK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11267031"
FT /id="VSP_001805"
SQ SEQUENCE 394 AA; 46475 MW; 7766831640D1BBF7 CRC64;
MITMLQDLHV NKISMSRSKS ETSLPSSRSG SQEKIMNVKG KVILLMLIVS TVVVVFWEYV
NRIPEVGENR WQKDWWFPSW FKNGTHSYQE DNVEGRREKG RNGDRIEEPQ LWDWFNPKNR
PDVLTVTPWK APIVWEGTYD TALLEKYYAT QKLTVGLTVF AVGKYIEHYL EDFLESADMY
FMVGHRVIFY VMIDDTSRMP VVHLNPLHSL QVFEIRSEKR WQDISMMRMK TIGEHILAHI
QHEVDFLFCM DVDQVFQDNF GVETLGQLVA QLQAWWYKAS PEKFTYERRE LSAAYIPFGE
GDFYYHAAIF GGTPTHILNL TRECFKGILQ DKKHDIEAQW HDESHLNKYF LFNKPTKILS
PEYCWDYQIG LPSDIKSVKV AWQTKEYNLV RNNV
