GGTA1_CALJA
ID GGTA1_CALJA Reviewed; 376 AA.
AC Q8SQ20;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11773054; DOI=10.1074/jbc.m110527200;
RA Koike C., Fung J.J., Geller D.A., Kannagi R., Libert T., Luppi P.,
RA Nakashima I., Profozich J., Rudert W., Sharma S.B., Starzl T.E., Trucco M.;
RT "Molecular basis of evolutionary loss of the alpha 1,3-
RT galactosyltransferase gene in higher primates.";
RL J. Biol. Chem. 277:10114-10120(2002).
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) (By similarity).
CC {ECO:0000250}.
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
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF384428; AAL93214.1; -; mRNA.
DR RefSeq; NP_001254661.1; NM_001267732.1.
DR AlphaFoldDB; Q8SQ20; -.
DR SMR; Q8SQ20; -.
DR STRING; 9483.ENSCJAP00000037549; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR GeneID; 100390928; -.
DR KEGG; cjc:100390928; -.
DR CTD; 2681; -.
DR eggNOG; ENOG502QW2H; Eukaryota.
DR InParanoid; Q8SQ20; -.
DR BRENDA; 2.4.1.87; 1068.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008225; Unplaced.
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: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: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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="N-acetyllactosaminide alpha-1,3-
FT galactosyltransferase"
FT /id="PRO_0000333698"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 142..147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 233..235
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 233
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 255..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 367..373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 376 AA; 44439 MW; D1A8645E8E647D75 CRC64;
MNVKGKVILS MLVVSTVIVV FWEYINSPEG SFLWIYHSKN PEVDDSSAQK GWWFPGWFNN
GIHNYQQEEE DTDKEKGREE EQRKEDDTTE LRLWDWFNPK KRPEVVTVTK WKAPVVWEGT
YNKAILENYY AKQKITVGLT VFAIGRYIEH YLEEFVTSAN RYFMVGHKVI FYVMVDDVSK
VPFIELGPLR SFKVFEVKPE KRWQDISMMR MKTIGEHILA HIQHEVDFLF CMDVDQVFQD
HFGVETLGQS VAQLQAWWYK ADPDDFTYER RKESAAYIPF GQGDFYYHAA IFGGTPIQVL
NITQECFKGI LLDKKNDIEA EWHDESHLNE YFLLNKPSKI LSPEYCWDYH IGLPSDIKTV
KLSWQTKEYN LVRNKV
