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Database: UniProt
Entry: H3D9L1_TETNG
LinkDB: H3D9L1_TETNG
Original site: H3D9L1_TETNG 
ID   H3D9L1_TETNG            Unreviewed;       382 AA.
AC   H3D9L1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000017202.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000017202.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   AlphaFoldDB; H3D9L1; -.
DR   STRING; 99883.ENSTNIP00000017202; -.
DR   Ensembl; ENSTNIT00000017418.1; ENSTNIP00000017202.1; ENSTNIG00000014190.1.
DR   GeneTree; ENSGT00940000159367; -.
DR   HOGENOM; CLU_044391_0_0_1; -.
DR   InParanoid; H3D9L1; -.
DR   OMA; RPMYTNV; -.
DR   TreeFam; TF312834; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007303; 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:UP000007303};
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          108..240
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          245..322
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
FT   REGION          83..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  44416 MW;  9C658306D9D0678E CRC64;
     MTRLMLGRTL ERICKGVLLL CLLHFLIMMI LYFDVYSQRF DLFSRFNNAR NGSRNNSTAA
     GNAHHFYYYN ISRPNATSTS YLAAGEQSAQ SAQPDANQTP SPKPLPPCPE NPPGLVGRLL
     IEFSSQMTME RVQKENPNVT EGGRYTPPDC RPRWKVAIII PFRHRENHLK YWLHYLHPIL
     RRQKIDYGIY IINQLGEDTF NRAKLLNVGY REALKEAAYD CFIFSDVDLI PMDDRNLYHC
     YDQPRHFAIA MDKFGFRLPY AGYFGGVSGL SKKQFLKING FPNEYWGWGG EDDDIYNRIT
     LNGMKVSRPD VRIGRFRMIK HERDKHNEPN PQRFNKIQNT KNTMKKDGIS SLTYRLVQVR
     KYPLYTNISV EIGKPPPRPF KG
//
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