ID Q92074_CHICK Unreviewed; 362 AA.
AC Q92074; F1NNJ4;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Beta-1,4-galactosyltransferase {ECO:0000256|RuleBase:RU368121};
DE Short=Beta-1,4-GalTase {ECO:0000256|RuleBase:RU368121};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
GN Name=CKI {ECO:0000313|EMBL:AAB05218.1};
GN Synonyms=B4GALT1 {ECO:0000313|Ensembl:ENSGALP00010013075.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|EMBL:AAB05218.1};
RN [1] {ECO:0000313|EMBL:AAB05218.1}
RP NUCLEOTIDE SEQUENCE.
RA Shaper J.H.;
RT "Characterization of G. gallus CKII and CKI genes encoding beta-1,4-
RT galactosyltransferase.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGALP00010013075.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010013075.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. {ECO:0000256|RuleBase:RU368121}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU368121};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU368121}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR EMBL; U19890; AAB05218.1; -; mRNA.
DR RefSeq; NP_990533.1; NM_205202.1.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR PaxDb; 9031-ENSGALP00000029057; -.
DR Ensembl; ENSGALT00010022655.1; ENSGALP00010013075.1; ENSGALG00010009486.1.
DR GeneID; 396121; -.
DR KEGG; gga:396121; -.
DR CTD; 2683; -.
DR VEuPathDB; HostDB:geneid_396121; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000155244; -.
DR HOGENOM; CLU_044391_0_0_1; -.
DR OMA; NAMVGKC; -.
DR BRENDA; 2.4.1.38; 1306.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000002022; Expressed in granulocyte and 13 other cell types or tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR CDD; cd00899; b4GalT; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19300:SF5; BETA-1,4-GALACTOSYLTRANSFERASE 1; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 1: Evidence at protein level;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU368121};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368121};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU368121}; Manganese {ECO:0000256|RuleBase:RU368121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368121};
KW Metal-binding {ECO:0000256|RuleBase:RU368121};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q92074};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU368121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368121};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368121}.
FT TRANSMEM 17..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 93..225
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 230..306
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT REGION 39..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 40929 MW; E481063638EBBC9A CRC64;
MKEPALPGTS LQRACRLLVA FCALHLSATL LYYLAGSSLT PPRSPEPPPR RPPPANLSLP
PSRPPPPPAA RPRPGPVSAQ PRNLPDSAPS GLCPDPSPLL VGPLRVEFSQ PVNLEEVAST
NPEVREGGRF APKDCKALQK VAIIIPFRNR EEHLKYWLYY MHPILQRQQL DYGVYVINQD
GDEEFNRAKL LNVGFTEALK EYDYDCFVFS DVDLIPMDDR NTYKCYSQPR HLSVSMDKFG
FRLPYNQYFG GVSALSKEQF TKINGFPNNY WGWGGEDDDI YNRLVFKGMG ISRPDAVIGK
CRMIRHSRDR KNEPNPERFD RIAHTRETMS SDGLNSLSYE VLRTDRFPLY TRITVDIGAP
GS
//
