ID A0A0N4TPN9_BRUPA Unreviewed; 333 AA.
AC A0A0N4TPN9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=BPAG_LOCUS10486 {ECO:0000313|EMBL:VDN91672.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0001052401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0001052401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN91672.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368121}.
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DR EMBL; UZAD01013188; VDN91672.1; -; Genomic_DNA.
DR STRING; 6280.A0A0N4TPN9; -.
DR WBParaSite; BPAG_0001052401-mRNA-1; BPAG_0001052401-mRNA-1; BPAG_0001052401.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
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 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:SF30; BETA-1,4-GALACTOSYLTRANSFERASE 7; 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}; 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:UP000278627};
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 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 110..203
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 213..278
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
SQ SEQUENCE 333 AA; 38565 MW; 831D69122A72506E CRC64;
MEIVPTSMAS KCASLSFEGV YLLLWSIVVM IVVLNACSIF KEKNIQWLVF PTKKGYELLI
QFSWSFVLNL DSFICYLFLS CVERGICEEA FDLGLYHLYG SFCDVHNQKH ASLTTVIPTH
MLCVLVPYRD REAELQIFVS YIADFLNKQN VLHKIIVLNQ TDALRFNRAS LINVGWYEAD
RVGCDYLAMH DVDLLPLNPQ LDYSYPGKGI IRHISSPEYH PKYNYTKFVG GILLLTMSDY
KVVNGMSNKY WGWGLEDDEF YLRLRDANLL SSMQRPMNLT TNRSNTFHRI SGLNSVKYHI
VGRNLLNFRK KLVVSVLNIE LECDLKWTNY CRP
//
