ID A0A077ZGV5_TRITR Unreviewed; 485 AA.
AC A0A077ZGV5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361242};
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
GN ORFNames=TTRE_0000615101 {ECO:0000313|EMBL:CDW57855.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57855.1};
RN [1] {ECO:0000313|EMBL:CDW57855.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW57855.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361242};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361242}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU361242}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323,
CC ECO:0000256|RuleBase:RU361242}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC ECO:0000256|RuleBase:RU361242}.
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DR EMBL; HG806224; CDW57855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZGV5; -.
DR STRING; 36087.A0A077ZGV5; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11675:SF101; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU361242};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361242};
KW Golgi apparatus {ECO:0000256|RuleBase:RU361242};
KW Lectin {ECO:0000256|RuleBase:RU361242};
KW Manganese {ECO:0000256|RuleBase:RU361242};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361242};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361242}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 149..253
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 281..339
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
SQ SEQUENCE 485 AA; 54663 MW; AE1B1951BA496948 CRC64;
MRRRTYVRIV ISGSVVWLLV YAAYVVFMMD RSATTSNAPN VVSFSAQEKN PGLLELMLKG
DFLARFAQPF EVLLLILTSG RRHGEKNVGE MGGPVILNED ERNEATRRFQ ENQFNVVASE
HVSLNRSLPN YNAVCRKSGN YLKKLPATSV VIVFHNEAWS TLLRTIHSVL NRSPQNLLEE
IVLVDDASSQ DHLKKPLEAY LQMLGSKIRL VRLQARSGLI TARIRGALLA KGKVLTFLDA
HVEVTPGWLE PTVLGEASAG IYHFGGIRRL PRRGMNFAPV CRTPTIAGGL FSVDRQYFFD
IGAYDEGMKI WGAENLELSF RVWTCGGSLE IHPCSHVGHV FRKRTPYTFV GGANNVIYGN
ARRVAEVWLD SYKSFFYLAS PAALKVDAGD YSKRQKLRSR LGCKSFRWYL ENVYPESNIP
ITYYSIGFVN WRFTVVQCFQ GWSYTGSGQI RSSEQCLGSR LNVDIILEKC ILNGPSLFWD
YNGTV
//