A4GAT_PANTR
ID A4GAT_PANTR Reviewed; 353 AA.
AC Q9N291;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Lactosylceramide 4-alpha-galactosyltransferase;
DE EC=2.4.1.228 {ECO:0000250|UniProtKB:Q9NPC4};
DE AltName: Full=Alpha-1,4-N-acetylglucosaminyltransferase;
DE AltName: Full=Alpha-1,4-galactosyltransferase;
DE AltName: Full=Globotriaosylceramide synthase;
DE Short=Gb3 synthase;
DE AltName: Full=UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase;
GN Name=A4GALT; Synonyms=A14GALT, A4GALT1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
CC -!- FUNCTION: Catalyzes the transfer of galactose from UDP-alpha-D-
CC galactose to lactosylceramide/beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1)-ceramide(d18:1(4E)) to produce globotriaosylceramide/globoside
CC Gb3Cer (d18:1(4E)). Also able to transfer galactose to
CC galactosylceramide/beta-D-Gal-(1<->1')-Cer. Globoside Gb3Cer is a
CC glycosphingolipid of the globo serie, one of the major types of neutral
CC root structures of glycosphingolipids, that constitute a significant
CC portion of mammalian cell membranes. {ECO:0000250|UniProtKB:Q9NPC4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-
CC alpha-D-galactose = globoside Gb3Cer (d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:11924, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950,
CC ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914;
CC EC=2.4.1.228; Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11925;
CC Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Gal-(1<->1')-Cer + UDP-alpha-D-galactose = alpha-D-Gal-
CC (1->4)-beta-D-Gal-(1<->1')-Cer + H(+) + UDP; Xref=Rhea:RHEA:60044,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:143593, ChEBI:CHEBI:143594;
CC Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60045;
CC Evidence={ECO:0000250|UniProtKB:Q9NPC4};
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q9NPC4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; AB041419; BAA94504.1; -; Genomic_DNA.
DR RefSeq; NP_001009123.1; NM_001009123.1.
DR AlphaFoldDB; Q9N291; -.
DR STRING; 9598.ENSPTRP00000054880; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR PRIDE; Q9N291; -.
DR GeneID; 470230; -.
DR KEGG; ptr:470230; -.
DR CTD; 53947; -.
DR eggNOG; KOG1928; Eukaryota.
DR InParanoid; Q9N291; -.
DR Proteomes; UP000002277; 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:0008378; F:galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050512; F:lactosylceramide 4-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR007652; A1-4-GlycosylTfrase_dom.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF04572; Gb3_synth; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="Lactosylceramide 4-alpha-galactosyltransferase"
FT /id="PRO_0000080580"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..353
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 192..194
FT /note="DXD motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 40487 MW; F9D9F58B7AE2BFD4 CRC64;
MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG QLYNLPAEIP
CPTLTPPTPP SHGPTPGNIF FLETSDRTNP NFLFMCSVES AARTHPESHV LVLMKGLPGG
NASLPRHLGI SLLSCFPNVQ MLPLDLRELF QDTPLADWYA AVQGRWEPYL LPVLSDASRI
ALMWKFGGIY LDTDFIVLKN LRNLTNVLGT QSRYVLNGAF LAFERRHEFM ALCMRDFVDH
YNGWIWGHQG PQLLTRVFKK WCSIRSLAES RSCRGVTTLP PEAFYPIPWQ DWKKYFEDIN
PEELPRLLSA TYAVHVWNKK SQGTRFEATS RALLAQLHAR YCPTTHEAMK MYL
