ID W5M4N6_LEPOC Unreviewed; 380 AA.
AC W5M4N6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003344.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003344.1}
RP IDENTIFICATION.
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; AHAT01003263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006628042.2; XM_006627979.2.
DR AlphaFoldDB; W5M4N6; -.
DR STRING; 7918.ENSLOCP00000003344; -.
DR Ensembl; ENSLOCT00000003351.1; ENSLOCP00000003344.1; ENSLOCG00000002835.1.
DR GeneID; 102692803; -.
DR KEGG; loc:102692803; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000166068; -.
DR HOGENOM; CLU_044391_1_2_1; -.
DR InParanoid; W5M4N6; -.
DR OMA; KNESHHE; -.
DR OrthoDB; 306273at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000002835; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
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:SF42; BETA-1,4-GALACTOSYLTRANSFERASE; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
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 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 100..233
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 238..315
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
SQ SEQUENCE 380 AA; 44404 MW; 66EECCB12EC1F0D3 CRC64;
MQPFFERSQG TSFNSMTRVN RGPVSHCRMT LARTLEKPCF LITLAFLQLV FVAVMYRRGS
SVLHGLFSAS GENWDYAKAQ DVYTNLTFFT PVMKELQRYC PAKSPLLVGP LKVTLLTAPA
LRRIVKKNPY VRRGGLYRPP HCLARYKTAI IVPHRNREVH LRHLLYHLHP FLQRQQLHYR
IYVIHQAGSQ TFNRAKLLNV GVREAMKDED WDCLFLHDID LIPENDYNLY VCDETYPKHF
SSAINKFNYR LPYWTYFGGV SAMTPEQYMK INGFPNTYWG WGGEDDDIAF RVKYAGLRMV
RVPLHIGRYK MVDHKQDKGN EQNNKRFDLL VRSPDKWRED GMNSLEYHLV SKRLMYLYTN
VTVDIGPNPF SSEEKNGTAT
//
