GBGT1_CHICK
ID GBGT1_CHICK Reviewed; 343 AA.
AC Q5ZLK4;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 {ECO:0000250|UniProtKB:Q8N5D6};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8N5D6};
DE AltName: Full=Forssman glycolipid synthase-like protein;
GN Name=GBGT1 {ECO:0000250|UniProtKB:Q8N5D6}; ORFNames=RCJMB04_5m5;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
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: May catalyze the formation of some glycolipid via the
CC addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to some
CC substrate. Glycolipids probably serve for adherence of some pathogens
CC (By similarity). {ECO:0000250|UniProtKB:Q8N5D6}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P14769};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P14769};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- DOMAIN: The conserved DXD motif is involved in cofactor binding. The
CC manganese ion interacts with the beta-phosphate group of UDP and may
CC also have a role in catalysis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 6 family. {ECO:0000305}.
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DR EMBL; AJ719730; CAG31389.1; -; mRNA.
DR RefSeq; NP_001025854.1; NM_001030683.1.
DR AlphaFoldDB; Q5ZLK4; -.
DR SMR; Q5ZLK4; -.
DR STRING; 9031.ENSGALP00000005275; -.
DR CAZy; GT6; Glycosyltransferase Family 6.
DR PaxDb; Q5ZLK4; -.
DR PRIDE; Q5ZLK4; -.
DR GeneID; 417163; -.
DR KEGG; gga:417163; -.
DR CTD; 26301; -.
DR VEuPathDB; HostDB:geneid_417163; -.
DR eggNOG; ENOG502QQAJ; Eukaryota.
DR InParanoid; Q5ZLK4; -.
DR OrthoDB; 1204439at2759; -.
DR PhylomeDB; Q5ZLK4; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q5ZLK4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005076; Glyco_trans_6.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR10462; PTHR10462; 1.
DR Pfam; PF03414; Glyco_transf_6; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Globoside alpha-1,3-N-
FT acetylgalactosaminyltransferase 1"
FT /id="PRO_0000157297"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 112..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 202..204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 204
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT BINDING 224..227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14769"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 343 AA; 39652 MW; C5000B26218649C8 CRC64;
MISRKALGSL VCLSAVATLI WIASGNWKVH YLPYYLPCPG IFSKKLQYLG DKPVQLFPQL
FYQQPRVLAP KRQDVLTVTP WLAPIVWEGT FSPEILDSAY MPLNLTIGVT AFAVGKYTRF
VSRFLKSAEM HFMKGYRVNY YIFTDNPKMI PDVQLQPGRR FDVVHIKKYS SWQEISVRRM
EAINLHIAER SHREVDYLFC LDIDMVFHNA WGAETLGDMV AAIHPGYFNV PRSQFPYERR
SSSAAYIPDG EGDFYYGGAV FGGLVKKVYE FTKICHMTIL ADKANGIMAA WQEESHLNRH
FLTHKPSKLL SPEYLWDDRK PKPPEIFLIR FSTVDKNYQE VRN
