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Database: UniProt
Entry: Q5F3E5_CHICK
LinkDB: Q5F3E5_CHICK
Original site: Q5F3E5_CHICK 
ID   Q5F3E5_CHICK            Unreviewed;       368 AA.
AC   Q5F3E5; E1C5M2;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 106.
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=RCJMB04_19h3 {ECO:0000313|EMBL:CAH65339.1};
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:CAH65339.1};
RN   [1] {ECO:0000313|EMBL:CAH65339.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CB {ECO:0000313|EMBL:CAH65339.1};
RC   TISSUE=Bursa {ECO:0000313|EMBL:CAH65339.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ851705; CAH65339.1; -; mRNA.
DR   RefSeq; NP_001026187.1; NM_001031016.1.
DR   AlphaFoldDB; Q5F3E5; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GeneID; 421092; -.
DR   KEGG; gga:421092; -.
DR   CTD; 9331; -.
DR   VEuPathDB; HostDB:geneid_421092; -.
DR   eggNOG; KOG3916; Eukaryota.
DR   HOGENOM; CLU_044391_6_0_1; -.
DR   PhylomeDB; Q5F3E5; -.
DR   UniPathway; UPA00378; -.
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:SF47; BETA-1,4-GALACTOSYLTRANSFERASE 6; 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   2: Evidence at transcript 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   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        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368121"
FT   DOMAIN          94..228
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          233..310
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   368 AA;  43179 MW;  0FC6497A83D4B8EC CRC64;
     MLAFIFFFSF SSSCLYFIYV APGIANTYLF MVQARGIMLR ENVKTIGHMI RLYTNKNTTL
     NGTDYPEGNN SSDCVAQTTM YLPENFTYSP YQACPEKLPY MRGLIDVNMS EISFDEIQQL
     FSKDLDIKPG GHWKPKDCKP RWKVAIIIPF RNRHEHLPIF FRHLIPMLQK QRLEFAFYVV
     EQTGTQPFNR AMLFNVGFKE AMKDVVWDCI IFHDVDHLPE NDRNYYGCGE MPRHFAAKLD
     KYMYILPYNE FFGGVSGLTV EQFKKINGFP NAFWGWGGED DDLWNRVHYA GYNVTRPEGD
     LGKYKSIPHH HRGEVQFLGR YKLLRYSRER QYIDGLNNLV YTPKILVSRL YKNVTVNLMP
     ELAPIRDY
//
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