ID   Q7Z2I1_HUMAN            Unreviewed;       352 AA.
AC   Q7Z2I1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Lactosylceramide 4-alpha-galactosyltransferase {ECO:0000256|ARBA:ARBA00040835};
DE            EC=2.4.1.228 {ECO:0000256|ARBA:ARBA00039051};
DE   AltName: Full=Alpha-1,4-N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00043186};
DE   AltName: Full=Alpha-1,4-galactosyltransferase {ECO:0000256|ARBA:ARBA00041849};
DE   AltName: Full=Globotriaosylceramide synthase {ECO:0000256|ARBA:ARBA00043154};
DE   AltName: Full=UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase {ECO:0000256|ARBA:ARBA00041556};
GN   Name=A4GALT {ECO:0000313|EMBL:AAP47167.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAP47167.1};
RN   [1] {ECO:0000313|EMBL:AAP47167.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hellberg A., Poole J., Olsson M.L.;
RT   "Additional Molecular Bases of the Clinically Important p Phenotype.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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 = a 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:0000256|ARBA:ARBA00043770};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11925;
CC         Evidence={ECO:0000256|ARBA:ARBA00043770};
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:0000256|ARBA:ARBA00036489};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60045;
CC         Evidence={ECO:0000256|ARBA:ARBA00036489};
CC   -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000256|ARBA:ARBA00004934}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
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DR   EMBL; AF513326; AAP47167.1; -; Genomic_DNA.
DR   EMBL; AF513327; AAP47168.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z2I1; -.
DR   CAZy; GT32; Glycosyltransferase Family 32.
DR   PeptideAtlas; Q7Z2I1; -.
DR   ChiTaRS; A4GALT; human.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.550.20; -; 1.
DR   InterPro; IPR007652; A1-4-GlycosylTfrase_dom.
DR   InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12042:SF17; LACTOSYLCERAMIDE 4-ALPHA-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12042; LACTOSYLCERAMIDE 4-ALPHA-GALACTOSYLTRANSFERASE ALPHA- 1,4-GALACTOSYLTRANSFERASE; 1.
DR   Pfam; PF04572; Gb3_synth; 1.
DR   Pfam; PF04488; Gly_transf_sug; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:AAP47167.1};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:AAP47167.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          221..347
FT                   /note="Alpha 1,4-glycosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04572"
SQ   SEQUENCE   352 AA;  40352 MW;  4B82289F0F4DC047 CRC64;
     MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG QLYNLPAEIP
     CPTLTPPTPP SHGPTPGNIF LETSDRTNPN FLFMCSVESA ARTHPESHVL VLMKGLPGGN
     ASLPRHLGIS LLSCFPNVQM LPLDLRELFR DTPLADWYAA VQGRWEPYLL PVLSDASRIA
     LMWKFGGIYL DTDFIVLKNL RNLTNVLGTQ SRYVLNGAFL AFERRHEFMA LCMRDFVDHY
     NGWIWGHQGP QLLTRVFKKW CSIRSLAESR ACRGVTTLPP EAFYPIPWQD WKKYFEDINP
     EELPRLLSAT YAVHVWNKKS QGTRFEATSR ALLAQLHARY CPTTHEAMKM YL
//