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Database: UniProt
Entry: A0A0V0RJI3_9BILA
LinkDB: A0A0V0RJI3_9BILA
Original site: A0A0V0RJI3_9BILA 
ID   A0A0V0RJI3_9BILA        Unreviewed;       650 AA.
AC   A0A0V0RJI3;
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-5 {ECO:0000313|EMBL:KRX14567.1};
GN   ORFNames=T07_4739 {ECO:0000313|EMBL:KRX14567.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX14567.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX14567.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX14567.1};
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:KRX14567.1}.
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DR   EMBL; JYDL01000156; KRX14567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0RJI3; -.
DR   STRING; 6336.A0A0V0RJI3; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054630; 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:SF131; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9-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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          523..644
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   650 AA;  74722 MW;  8E69162BBB0A2CEA CRC64;
     MNFIRRRRSA LIKLAVTLCT FWLFLAFTIS YRSSGLVGQS EKSWLNEGPP SPMTELEQKP
     NVDYHQQQQQ HQMIRTISPK PTQSSSSWPA RINQSRFVTL NLKKQQFQKM RKKPLGGESM
     QKNVIDVPQS LLHIEAVDIY NYSPDMPGEN GTAVVIKKED LPPKERALYD VGWQKNAFNQ
     YVSDRISIYR KLPKVPDASC YKKQYNDNLP KTSVIICFHN EAWSVLLRTV HSVLSRSPAN
     LLQEIILVDD FSDAEHLKNQ LDVYMDRLGI VKIVRLQKRE GLIRARLSGA AVAIGPVLTF
     LDSHCECLEG WLPPLLSRIK ENWSNVVCPV IDVIDDDTFK YHCGKSWMTN VGGFDWNLQF
     NWHPIPERVR KSRSDPTAPV ESPTMAGGLF SIDKQYFQHL GTYDPGFDIW GGENLELSFK
     VWMCGGKLEI VPCSHVGHIF RKRSPYKWRP GVNVVKRNTV RLAEVWLDDY KNYYYERINF
     NLGEFGDVSD RIALRQRLNC SSFEWYIKNV YPELFVPGNS IAKGEIRCMG QNKRHCLDFA
     SGRKEHNKPI SMYPCHGEGG NQYWMLSPTG EIRRDESCVD YAGQKVFLSG CHGLKGNQEW
     KYNFKDKTLT HVISGLCLEM NHDATGVIMA SCDSQNLNQQ WTFGEVVKQR
//
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