GGTA1_LEMCA
ID GGTA1_LEMCA Reviewed; 375 AA.
AC Q8HYB2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 67.
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 Lemur catta (Ring-tailed lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Lemur.
OX NCBI_TaxID=9447;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17194757; DOI=10.1073/pnas.0610012104;
RA Koike C., Uddin M., Wildman D.E., Gray E.A., Trucco M., Starzl T.E.,
RA Goodman M.;
RT "Functionally important glycosyltransferase gain and loss during catarrhine
RT primate emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:559-564(2007).
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 isogloboside
CC 3 (iGb3) (By similarity). {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}.
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DR EMBL; AY126667; AAM95595.2; -; mRNA.
DR AlphaFoldDB; Q8HYB2; -.
DR SMR; Q8HYB2; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR BRENDA; 2.4.1.87; 9186.
DR UniPathway; UPA00378; -.
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; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..375
FT /note="N-acetyllactosaminide alpha-1,3-
FT galactosyltransferase"
FT /id="PRO_0000333702"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 57..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 141..146
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 232..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 366..372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 375 AA; 44402 MW; 211F95DCB9F2BABB CRC64;
MNVKGKVILS MLVVSTVMVV FWEYINSPEG SFLWIYHSKN PEVGDSSTQK GWWFPSWFHD
GTPSNQEEED IDKEKRREKE QRKEDDEEEL QLWDWFNPKK RPEVVTVTSW KAPVVWEGTY
NKAILENYYA KQKITVGLTV FAVGRYIEHY LEEFITSANR YFMVGHKVIF YIMLDDISKM
PLIELGPLRS FKVFEIKPEK RWQDISMMRM KTIGEHILAH IQHEVDFLFC MDVDQVFQDN
FGVETLGQSV AQLQAWWYKA DPDEFTYERR KESAAYIPFG EGDFYYHAAI FGGTPIQVLN
ITRECFKGIL QDKKNDIEAE WHDESHLNKY FLLNKPSKIL SPEYCWDFHI GLPSDIKIVK
ISWQTKHYNL VRNNV
