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Database: UniProt
Entry: A0A091F740_CORBR
LinkDB: A0A091F740_CORBR
Original site: A0A091F740_CORBR 
ID   A0A091F740_CORBR        Unreviewed;       343 AA.
AC   A0A091F740;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 20.
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};
DE   Flags: Fragment;
GN   ORFNames=N302_08020 {ECO:0000313|EMBL:KFO57690.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO57690.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO57690.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO57690.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK718610; KFO57690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091F740; -.
DR   STRING; 85066.A0A091F740; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000052976; 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:SF9; BETA-1,4-GALACTOSYLTRANSFERASE 4; 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:UP000052976};
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..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368121"
FT   DOMAIN          80..212
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          216..292
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO57690.1"
FT   NON_TER         343
FT                   /evidence="ECO:0000313|EMBL:KFO57690.1"
SQ   SEQUENCE   343 AA;  39963 MW;  58D47881F240736D CRC64;
     LGLNVYHLFY KFKVLVLVTS LLMVLWTTFS YLVDTRQEIP KAKSMVEFFR KVTSLEHSQK
     EEKIKSTADI PMVKSFQGPC PAVSPYLRGA SKLSFKPSVT LEEVQKENPQ VAKGRYHPVE
     CSALQHVAIL IPHRNREKHL LYLLQHLHPF LQRQQLDYGI YVIHQAGNTK FNRAKLLNVG
     YLEALKEASW DCFIFHDVDL VPENDFNIYM CDTQPKHLVV GRNNTGYRLR YRGYFGGVTA
     LTRDQFSKVN GFSNSYWGWG GEDDDLRIRV EMQKMKVVRP PADVARYTMI FHNRDHGNEE
     NRERMKLLRQ VSRTWKTDGL NSCSYKLLSV EHNPLYINIT VDF
//
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