ID   GBGT1_MOUSE             Reviewed;         347 AA.
AC   Q8VI38; Q3KPA1; Q8CJF3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE            EC=2.4.1.88 {ECO:0000250|UniProtKB:Q95158};
DE   AltName: Full=Forssman glycolipid synthase;
GN   Name=Gbgt1 {ECO:0000312|MGI:MGI:2449143}; Synonyms=Fgs;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14573676; DOI=10.1128/iai.71.11.6543-6552.2003;
RA   Elliott S.P., Yu M., Xu H., Haslam D.B.;
RT   "Forssman synthetase expression results in diminished shiga toxin
RT   susceptibility: a role for glycolipids in determining host-microbe
RT   interactions.";
RL   Infect. Immun. 71:6543-6552(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Watanobe T., Shimizu M., Nakano M., Handa S., Yoshida M., Kushi Y.;
RT   "Preferential expression of Forssman glycolipid in undifferentiated ES
RT   cells and its chromosomal localization in mouse.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 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:14573676). Forssman
CC       glycolipid (also called Forssman antigen; FG) probably serves for
CC       adherence of some pathogens (PubMed:14573676). Conversely, it
CC       diminishes Shiga toxins susceptibility (PubMed:14573676).
CC       {ECO:0000269|PubMed:14573676}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a globoside Gb4Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         galactosamine = a 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:0000250|UniProtKB:Q95158};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22165;
CC         Evidence={ECO:0000250|UniProtKB:Q95158};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a globoside Gb4Cer + UDP-N-acetyl-alpha-D-galactosamine = a
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:14573676};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56569;
CC         Evidence={ECO:0000305|PubMed:14573676};
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}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Globoside
CC       alpha-1,3-N-acetylgalactosaminyltransferase 1;
CC       URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_504";
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DR   EMBL; AF292399; AAL37034.1; -; mRNA.
DR   EMBL; AB084789; BAC23060.2; -; mRNA.
DR   EMBL; AL772249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC106831; AAI06832.1; -; mRNA.
DR   CCDS; CCDS15839.1; -.
DR   RefSeq; NP_631936.2; NM_139197.2.
DR   RefSeq; XP_006497981.1; XM_006497918.2.
DR   AlphaFoldDB; Q8VI38; -.
DR   SMR; Q8VI38; -.
DR   STRING; 10090.ENSMUSP00000127071; -.
DR   SwissLipids; SLP:000001914; -.
DR   CAZy; GT6; Glycosyltransferase Family 6.
DR   GlyCosmos; Q8VI38; 1 site, No reported glycans.
DR   GlyGen; Q8VI38; 1 site.
DR   PhosphoSitePlus; Q8VI38; -.
DR   MaxQB; Q8VI38; -.
DR   PaxDb; 10090-ENSMUSP00000127071; -.
DR   ProteomicsDB; 266779; -.
DR   Antibodypedia; 63936; 65 antibodies from 16 providers.
DR   DNASU; 227671; -.
DR   Ensembl; ENSMUST00000028172.2; ENSMUSP00000028172.2; ENSMUSG00000026829.10.
DR   Ensembl; ENSMUST00000163121.8; ENSMUSP00000127071.2; ENSMUSG00000026829.10.
DR   GeneID; 227671; -.
DR   KEGG; mmu:227671; -.
DR   UCSC; uc008iyl.2; mouse.
DR   AGR; MGI:2449143; -.
DR   CTD; 26301; -.
DR   MGI; MGI:2449143; Gbgt1.
DR   VEuPathDB; HostDB:ENSMUSG00000026829; -.
DR   eggNOG; ENOG502QQAJ; Eukaryota.
DR   GeneTree; ENSGT00950000182858; -.
DR   HOGENOM; CLU_062445_0_1_1; -.
DR   InParanoid; Q8VI38; -.
DR   OMA; RRLITHK; -.
DR   OrthoDB; 4223357at2759; -.
DR   PhylomeDB; Q8VI38; -.
DR   TreeFam; TF330991; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 227671; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Gbgt1; mouse.
DR   PRO; PR:Q8VI38; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8VI38; Protein.
DR   Bgee; ENSMUSG00000026829; Expressed in mesodermal cell in embryo and 58 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02515; Glyco_transf_6; 1.
DR   InterPro; IPR005076; Glyco_trans_6.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR10462:SF49; GLOBOSIDE ALPHA-1,3-N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR10462; GLYCOSYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF03414; Glyco_transf_6; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   Genevisible; Q8VI38; MM.
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_0000157296"
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..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"
FT   CONFLICT        337
FT                   /note="S -> P (in Ref. 1; AAL37034)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  40502 MW;  69C7E141334A5F44 CRC64;
     MTRPRLAQGL AFFLLGGTGL WVLWKFIKDW LLVSYIPYYL PCPEFFNMKL PFRKEKPLQP
     VTQLQYPQPK LLEHGPTELL TLTPWLAPIV SEGTFDPELL KSMYQPLNLT IGVTVFAVGK
     YTCFIQRFLE SAEEFFMRGY QVHYYLFTHD PTAVPRVPLG PGRLLSIIPI QGYSRWEEIS
     MRRMETINKH IAKRAHKEVD YLFCVDVDMV FRNPWGPETL GDLVAAIHPG YFAVPRRKFP
     YERRQVSSAF VADNEGDFYY GGALFGGRVA RVYEFTRACH MAILADKANS IMAAWQEESH
     LNRHFIWHKP SKVLSPEYLW DERKPRPRSL KMIRFSSVKK NANWLRT
//