GBGT1_CANLF
ID GBGT1_CANLF Reviewed; 347 AA.
AC Q95158;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000250|UniProtKB:Q8VI38};
DE EC=2.4.1.88 {ECO:0000269|PubMed:8855242};
DE AltName: Full=Forssman glycolipid synthase {ECO:0000303|PubMed:8855242};
GN Name=GBGT1 {ECO:0000250|UniProtKB:Q8VI38};
GN Synonyms=FS {ECO:0000303|PubMed:8855242};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=8855242; DOI=10.1073/pnas.93.20.10697;
RA Haslam D.B., Baenziger J.U.;
RT "Expression cloning of Forssman glycolipid synthetase: a novel member of
RT the histo-blood group ABO gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10697-10702(1996).
RN [2]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Substantia nigra;
RX PubMed=10506200; DOI=10.1074/jbc.274.41.29390;
RA Xu H., Storch T., Yu M., Elliott S.P., Haslam D.B.;
RT "Characterization of the human Forssman synthetase gene: an evolving
RT association between glycolipid synthesis and host-microbial interactions.";
RL J. Biol. Chem. 274:29390-29398(1999).
CC -!- FUNCTION: Catalyzes the formation of Forssman glycolipid via the
CC addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to
CC GalNAcb-1,3Gala-1,4Galb-1,4GlcCer (Gb4Cer) (PubMed:8855242,
CC PubMed:10506200). Forssman glycolipid (also called Forssman antigen;
CC FG) probably serves for adherence of some pathogens such as E.coli
CC uropathogenic strains (PubMed:10506200). {ECO:0000269|PubMed:10506200,
CC ECO:0000269|PubMed:8855242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC galactosamine = globoside Forssman (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:22164, ChEBI:CHEBI:15378, ChEBI:CHEBI:18056,
CC ChEBI:CHEBI:18259, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.88;
CC Evidence={ECO:0000269|PubMed:8855242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22165;
CC Evidence={ECO:0000305|PubMed:8855242};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer + UDP-N-acetyl-alpha-D-galactosamine =
CC globoside IV3GalNAc-Gb4Cer + H(+) + UDP; Xref=Rhea:RHEA:56568,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138,
CC ChEBI:CHEBI:88167, ChEBI:CHEBI:90400;
CC Evidence={ECO:0000269|PubMed:10506200, ECO:0000269|PubMed:8855242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56569;
CC Evidence={ECO:0000305|PubMed:8855242};
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {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; U66140; AAC48667.1; -; mRNA.
DR PIR; JC6126; JC6126.
DR RefSeq; NP_001003193.1; NM_001003193.1.
DR AlphaFoldDB; Q95158; -.
DR SMR; Q95158; -.
DR STRING; 9612.ENSCAFP00000029424; -.
DR SwissLipids; SLP:000001913; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR PaxDb; Q95158; -.
DR GeneID; 403833; -.
DR KEGG; cfa:403833; -.
DR CTD; 26301; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR InParanoid; Q95158; -.
DR OrthoDB; 1204439at2759; -.
DR BRENDA; 2.4.1.88; 1153.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Unplaced.
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:0047277; F:globoside alpha-N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0001575; P:globoside metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Globoside alpha-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000157294"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 116..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 208
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 228..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 40265 MW; 66E6119CCD766739 CRC64;
MRCRRLALGL GFSLLSGIAL WSLWIYMETW LPFSYVPYYL PCPEIFNMKL QYKGEKPFQP
VTRSPHPQPK LLEQRPTELL TLTPWLAPIV SEGTFNPELL QHIYQPLNLT IGLTVFAVGK
YTRFVQHFLE SAEQFFMQGY QVYYYIFTND PAGIPRVPLG PGRLLSIIPI QRHSRWEEIS
TRRMETISRH IAQRAHREVD YLFCVDVDMV FRNPWGPETL GDLVAAIHPG YYAVPRQQFP
YERRHISTAF VAENEGDFYY GGAVFGGRVA KVYEFTTGCH MAILADKANG IMAAWQEESH
LNRRFISHKP SKVLSPEYLW DDRKPQPPSL KLIRFSTLDK ATSWLRS
