GenomeNet

Database: UniProt
Entry: A0A077ZGV5_TRITR
LinkDB: A0A077ZGV5_TRITR
Original site: A0A077ZGV5_TRITR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system