ID L5M0C0_MYODS Unreviewed; 369 AA.
AC L5M0C0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ORFNames=MDA_GLEAN10014379 {ECO:0000313|EMBL:ELK31153.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31153.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|ARBA:ARBA00001936,
CC 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; KB106370; ELK31153.1; -; Genomic_DNA.
DR RefSeq; XP_006762690.1; XM_006762627.2.
DR RefSeq; XP_006762691.1; XM_006762628.2.
DR AlphaFoldDB; L5M0C0; -.
DR GeneID; 102774860; -.
DR KEGG; myd:102774860; -.
DR CTD; 8704; -.
DR eggNOG; KOG3916; Eukaryota.
DR OrthoDB; 306273at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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:SF32; BETA-1,4-GALACTOSYLTRANSFERASE 2; 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:UP000010556};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 94..227
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 232..309
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT REGION 57..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41799 MW; 7F263EF20E87B8E8 CRC64;
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDIYAQHLA FFSRFSARGP ARVLHPAASS
SSNCSRPNAT APSSGLAEAP SVRPGSSAPI LPPCPDSPPG LVGRLLIEFT SPMPLERVQR
ENPGVLLGGR YTPPDCTPAQ TVAVIIPFRH REHHLRYWLH YLHPILRRQR LRYGIYVINQ
HGEDTFNRAK LLNVGFLEAL KEDASYDCFI FSDVDLVPMD DRNLYRCGDQ PRHFAIAMDK
FGFRLPYAGY FGGVSGLSKA QFLRINGFPN EYWGWGGEDD DIFNRISLTG MKISRPDVRI
GRYRMIKHDR DKHNEPNPQR FTKIQNTKLT MKRDGIASVR YQVLEVSRQP LFTNITVDIG
RPPSWPPRG
//
