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Database: UniProt/SWISS-PROT
Entry: B3GT1_PANPA
LinkDB: B3GT1_PANPA
Original site: B3GT1_PANPA 
ID   B3GT1_PANPA             Reviewed;         326 AA.
AC   Q7JK25;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-APR-2018, entry version 59.
DE   RecName: Full=Beta-1,3-galactosyltransferase 1;
DE            Short=Beta-1,3-GalTase 1;
DE            Short=Beta3Gal-T1;
DE            Short=Beta3GalT1;
DE            EC=2.4.1.86 {ECO:0000250|UniProtKB:Q9Y5Z6};
DE   AltName: Full=UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1;
GN   Name=B3GALT1;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
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
RT   genes.";
RL   Mol. Biol. Evol. 21:936-944(2004).
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose
CC       from UDP-galactose to substrates with a terminal beta-N-
CC       acetylglucosamine (beta-GlcNAc) residue. Involved in the
CC       biosynthesis of the carbohydrate moieties of glycolipids and
CC       glycoproteins. {ECO:0000250|UniProtKB:Q9Y5Z6}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
CC       glucosaminyl-R = UDP + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC       glucosaminyl-R. {ECO:0000250|UniProtKB:Q9Y5Z6}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
DR   EMBL; AB041409; BAA94494.1; -; Genomic_DNA.
DR   RefSeq; XP_003824359.1; XM_003824311.3.
DR   RefSeq; XP_008976299.1; XM_008978051.2.
DR   RefSeq; XP_008976300.1; XM_008978052.2.
DR   RefSeq; XP_008976301.1; XM_008978053.2.
DR   ProteinModelPortal; Q7JK25; -.
DR   SMR; Q7JK25; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   GeneID; 100986605; -.
DR   KEGG; pps:100986605; -.
DR   CTD; 8708; -.
DR   HOVERGEN; HBG101354; -.
DR   KO; K07819; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   UniPathway; UPA00378; -.
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:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese;
KW   Membrane; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    326       Beta-1,3-galactosyltransferase 1.
FT                                /FTId=PRO_0000219147.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     26       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     27    326       Lumenal. {ECO:0000255}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   326 AA;  37993 MW;  83271E99B2EE74F5 CRC64;
     MASKVSCLYV LTVVCWASAL WYLSITRPTS SYTGSKPFSH LTVARKNFTF GNIRTRPINP
     HSFEFLINEP NKCEKNIPFL VILISTTHKE FDARQAIRET WGDENNFKGI KIATLFLLGK
     NADPVLNQMV EQESQIFHDI IVEDFIDSYH NLTLKTLMGM RWVATFCSKA KYVMKTDSDI
     FVNMDNLIYK LLKPSTKPRR RYFTGYVING GPIRDVRSKW YMPRDLYPDS NYPPFCSGTG
     YIFSADVAEL IYKTSLHTRL LHLEDVYVGL CLRKLGIHPF QNSGFNHWKM AYSLCRYRRV
     ITVHQISPEE MHRIWNDMSS KKHLRC
//
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