ID   B3GT5_PANTR             Reviewed;         297 AA.
AC   Q9N295;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Beta-1,3-galactosyltransferase 5;
DE            Short=Beta-1,3-GalTase 5;
DE            Short=Beta3Gal-T5;
DE            Short=Beta3GalT5;
DE            Short=b3Gal-T5;
DE            EC=2.4.1.-;
DE   AltName: Full=Beta-3-Gx-T5;
DE   AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5;
DE   AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5;
DE   Flags: Fragment;
GN   Name=B3GALT5;
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 Gal to GlcNAc-based acceptors with
CC       a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc
CC       structure. Can use glycolipid LC3Cer as an efficient acceptor (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=globoside Gb4Cer (d18:1(4E)) + UDP-alpha-D-galactose =
CC         globoside GalGb4Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41996,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:18259, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:62571, ChEBI:CHEBI:66914;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2C3};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41997;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y2C3};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; AB041414; BAA94499.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9N295; -.
DR   SMR; Q9N295; -.
DR   STRING; 9598.ENSPTRP00000053952; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q9N295; -.
DR   eggNOG; KOG2287; Eukaryota.
DR   InParanoid; Q9N295; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002277; Unplaced.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IBA:GO_Central.
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: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   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..>297
FT                   /note="Beta-1,3-galactosyltransferase 5"
FT                   /id="PRO_0000219167"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..>297
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         297
SQ   SEQUENCE   297 AA;  34851 MW;  BB7963250A837A28 CRC64;
     MAFPKMRLMY VCLLVLGALC VYFSMYSLNL FKEQSFVYKK DGNFLKLPDT DCRQTPPFLV
     LLVTSSHRQL AERMAIRQTW GKERTVKGKQ LKTFFLLGTT SSAAETKEVD QESQRHGDII
     QKDFLDVYYN LTLKTMMGIE WVHRFCPQAA FVMKTDSDMF INVDYLTELL LKKNRTTRFF
     TGFLKLNEFP IRQPFSKWFV SKSEYPWDRY PPFCSGTGYV FSGDVASQVY NVSESVPYIK
     LEDVFVGLCL ERLNIRLEEL HSQPTFFPGG LRFSVCRFRR IVACHFIKPR TLLDYWQ