ID Q6J4T9_TRINI Unreviewed; 421 AA.
AC Q6J4T9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU368121};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
DE AltName: Full=Beta-4-GalNAcT {ECO:0000256|RuleBase:RU368121};
OS Trichoplusia ni (Cabbage looper).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Plusiinae; Trichoplusia.
OX NCBI_TaxID=7111 {ECO:0000313|EMBL:AAT11926.1};
RN [1] {ECO:0000313|EMBL:AAT11926.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15173167; DOI=10.1074/jbc.M404925200;
RA Vadaie N., Jarvis D.L.;
RT "Molecular cloning and functional characterization of a Lepidopteran insect
RT beta4-N-acetylgalactosaminyltransferase with broad substrate specificity, a
RT functional role in glycoprotein biosynthesis, and a potential functional
RT role in glycolipid biosynthesis.";
RL J. Biol. Chem. 279:33501-33518(2004).
CC -!- FUNCTION: Catalyzes the transfer of galactose onto proteins or lipids.
CC {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: Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU368121}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR EMBL; AY601103; AAT11926.1; -; mRNA.
DR AlphaFoldDB; Q6J4T9; -.
DR SMR; Q6J4T9; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR BRENDA; 2.4.1.92; 6461.
DR UniPathway; UPA00378; -.
DR GO; GO:0016020; C: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:SF62; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE; 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}; Manganese {ECO:0000256|RuleBase:RU368121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|RuleBase:RU368121};
KW Signal {ECO:0000256|SAM:SignalP};
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 Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..421
FT /note="Beta-1,4-N-acetylgalactosaminyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004274826"
FT DOMAIN 156..289
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 293..370
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
SQ SEQUENCE 421 AA; 48303 MW; EFF3CC116E8B0DAB CRC64;
MGGRATRALR LLLLLVLALA AVEYLFGSIL DASPLRTYLY TPLYNATQPT LRNVERLAAN
WPKKIPSNYI EDSEEYSIKN ISLSNHTTRA SVVHPPSSIT ETASKLDKNM TIQDGAFAMI
SPTPLLITKL MDSIKSYVTT EDGVKKAEAV VTLPLCDSMP PDLGPITLNK TELELEWVEK
KFPEVEWGGR YSPPNCTARH RVAIIVPYRD RQQHLAIFLN HMHPFLMKQQ IEYGIFIVEQ
EGNKDFNRAK LMNVGFVESQ KLVAEGWQCF VFHDIDLLPL DTRNLYSCPR QPRHMSASID
KLHFKLPYED IFGGVSAMTL EQFTRVNGFS NKYWGWGGED DDMSYRLKKI NYHIARYKMS
IARYAMLDHK KSTPNPKRYQ LLSQTSKTFQ KDGLSTLEYE LVQVVQYHLY THILVNIDER
S
//
