B3GL1_RAT
ID B3GL1_RAT Reviewed; 331 AA.
AC Q6AY39;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: 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; BC079206; AAH79206.1; -; mRNA.
DR RefSeq; NP_001013176.1; NM_001013158.1.
DR RefSeq; XP_017446356.1; XM_017590867.1.
DR RefSeq; XP_017446357.1; XM_017590868.1.
DR RefSeq; XP_017446358.1; XM_017590869.1.
DR RefSeq; XP_017446359.1; XM_017590870.1.
DR AlphaFoldDB; Q6AY39; -.
DR SMR; Q6AY39; -.
DR STRING; 10116.ENSRNOP00000016012; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q6AY39; 5 sites.
DR iPTMnet; Q6AY39; -.
DR PhosphoSitePlus; Q6AY39; -.
DR PaxDb; Q6AY39; -.
DR Ensembl; ENSRNOT00000016012; ENSRNOP00000016012; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000095435; ENSRNOP00000084772; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000096998; ENSRNOP00000080226; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000098966; ENSRNOP00000079867; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000099448; ENSRNOP00000090410; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000104541; ENSRNOP00000090178; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000104797; ENSRNOP00000082877; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000106160; ENSRNOP00000091655; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000107768; ENSRNOP00000079916; ENSRNOG00000012019.
DR Ensembl; ENSRNOT00000109215; ENSRNOP00000092519; ENSRNOG00000012019.
DR GeneID; 310508; -.
DR KEGG; rno:310508; -.
DR UCSC; RGD:1304797; rat.
DR CTD; 8706; -.
DR RGD; 1304797; B3galnt1.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000162252; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q6AY39; -.
DR OMA; PYCSGMG; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q6AY39; -.
DR TreeFam; TF318639; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6AY39; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012019; Expressed in stomach and 19 other tissues.
DR Genevisible; Q6AY39; RN.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:RGD.
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_0000219158"
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; 39215 MW; A0BF5A919A99339F CRC64;
MAPAVLTAIP NRMSLRSLKW SLLLLSLLSF LVIWYLSLPH YNVIERVNWM YFYEYEPIYR
QDFQFTLREH SNCSQQNPFL VILVTSRPSD VKARQAIRVT WGEKKTWWGH EVLTFFLLGQ
EAEREDKVLA LSLEDEHALY GDIIRQDFLD TYNNLTLKTI MAFRWVIEFC PNAKYVMKTD
TDVFINTGNL VKYLLNLNHS EKFFTGYPLI ENYSYRGFFH KNHISYQEYP FKVFPPYCSG
LGYIMSGDLV PKIYEMMGHV KPIKFEDVYV GICLNLLKVD IHIPEDTNLF FLFRIHLDVC
QLRRVIAAHG FSSKEIITFW QVMLRNTTCH Y
