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Database: UniProt
Entry: A0A0V0XRC4_TRIPS
LinkDB: A0A0V0XRC4_TRIPS
Original site: A0A0V0XRC4_TRIPS 
ID   A0A0V0XRC4_TRIPS        Unreviewed;       551 AA.
AC   A0A0V0XRC4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Name=gly-10 {ECO:0000313|EMBL:KRX90495.1};
GN   ORFNames=T4E_4137 {ECO:0000313|EMBL:KRX90495.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX90495.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX90495.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX90495.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX90495.1}.
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DR   EMBL; JYDU01000163; KRX90495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XRC4; -.
DR   STRING; 6337.A0A0V0XRC4; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
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   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF134; N-ACETYLGALACTOSAMINYLTRANSFERASE 4-RELATED; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 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|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU361242};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000256|RuleBase:RU361242};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          418..546
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   551 AA;  62781 MW;  54A70A6C6E03DDD1 CRC64;
     MALGRWLRRR LVLLIGCVFG GAFMLLSYIN SSSSELEIAQ LAQPSSIQLA KHFIDNVDGK
     IDWEDYVQLA ADSVRQGPGE QGEAFYLPTD NSVDHKKDML YKSNGFNALA SDYLALNRSI
     KDLRPKQCIG RSYLAKLEKV SVVIPFYNEH WSTLLRTVHS VVNRSPVELL QEVILADDFS
     DKPFLKQPLE AYVRDTWPGL VRIVRAQKRE GLIRARLLGS KAAISSVLVF LDSHSECGYN
     WLPPLLEPVA LNYRTVTCPF VDVIDHSTFL YRLQDHGARG SFDWELYYKR LPLLPEDAAH
     PDLPFNSPVM AGGYFAISTK WFWELGGYDE GLDIWGGEQY ELSFKIWQCG GTLIDVPCSH
     VGHIYREFSP FVNPGAGDFV GRNYKRVAEV WMDEYKEYVI AFDQSVRYPP VEVVDVREGE
     IRSIQSGLCV TVQFVVEHSV VGLADCSKGH DDAAVGEQFF KYTTRKEIKF KNRRLCFDVP
     ENRLKAPVIL YSCHDMQGNQ AWRYNSKTMQ IVHPVTNMCL DADFSRREVF MQSCNLNLLS
     QRWSFGAIVD S
//
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