ID   B3GL1_PONAB             Reviewed;         331 AA.
AC   Q5RAL7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1;
DE            Short=Beta-1,3-GalNAc-T1;
DE            EC=2.4.1.79 {ECO:0000250|UniProtKB:O75752};
DE   AltName: Full=Beta-1,3-galactosyltransferase 3;
DE            Short=Beta-1,3-GalTase 3;
DE            Short=Beta3Gal-T3;
DE            Short=Beta3GalT3;
DE            Short=b3Gal-T3;
DE   AltName: Full=Beta-3-Gx-T3;
DE   AltName: Full=Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase;
DE   AltName: Full=Globoside synthase;
DE   AltName: Full=UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase;
GN   Name=B3GALNT1; Synonyms=B3GALT3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide.
CC       Plays a critical role in preimplantation stage embryonic development.
CC       {ECO:0000250|UniProtKB:O75752, ECO:0000250|UniProtKB:Q920V1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         galactosamine = globoside Gb4Cer (d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259,
CC         ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:O75752}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O75752}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; CR858998; CAH91193.1; -; mRNA.
DR   RefSeq; NP_001127386.1; NM_001133914.1.
DR   AlphaFoldDB; Q5RAL7; -.
DR   SMR; Q5RAL7; -.
DR   STRING; 9601.ENSPPYP00000015944; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PRIDE; Q5RAL7; -.
DR   GeneID; 100174453; -.
DR   KEGG; pon:100174453; -.
DR   CTD; 8706; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   InParanoid; Q5RAL7; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001595; 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:0047273; F:galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW   Magnesium; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..331
FT                   /note="UDP-GalNAc:beta-1,3-N-
FT                   acetylgalactosaminyltransferase 1"
FT                   /id="PRO_0000219157"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..43
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..331
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  39478 MW;  B1E123188579B585 CRC64;
     MASALWTVLP SRMSLRSLQW SLLLLSLLSF LVMWYLSLPH YNVIERVNWM YFYEYEPIYR
     QDFHFTLREH SNCSHQNPFL VILVTSHPSD VKARQAIRVT WGEKKSWWGY EVLTFFLLGQ
     EAEKEDKMLA LSLEDEHLLY GDIIRQDFLD TYNNLTLKTI MAFRWVTEFC PNAKYVMKTD
     TDVFINTGNL VKYLLNLNHS EKFFTGYPLI DNYSYRGFYQ KTHISYQEYP FKVFPPYCSG
     LGYIMSRDLV PRIYEMMGHV KPIKFEDVYV GICLNLLKVN IHIPEDTNLF FLYRIHLDVC
     QLRRVIAAHG FSSKEIITFW QVMLRNTTCH Y