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Database: UniProt
Entry: A0A0V0VZ93_9BILA
LinkDB: A0A0V0VZ93_9BILA
Original site: A0A0V0VZ93_9BILA 
ID   A0A0V0VZ93_9BILA        Unreviewed;       665 AA.
AC   A0A0V0VZ93;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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-3 {ECO:0000313|EMBL:KRX68812.1};
GN   ORFNames=T09_8699 {ECO:0000313|EMBL:KRX68812.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX68812.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX68812.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX68812.1};
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:KRX68812.1}.
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DR   EMBL; JYDN01000001; KRX68812.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VZ93; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0070176; C:DRM complex; IEA:InterPro.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 2.
DR   InterPro; IPR018737; DREAM_LIN52.
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:SF101; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF10044; LIN52; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 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:UP000054681};
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        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          134..318
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   DOMAIN          446..534
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|Pfam:PF00652"
SQ   SEQUENCE   665 AA;  76079 MW;  D9026F69B4775426 CRC64;
     MRRKEYCRFA LFVICAWFVI YFVYAMFFAD IGYSESQKVL ISRLHPRINA NFSNGDSALQ
     TLLAAMKSKS PGAGEMGSPV IIQSSLQSEV KARFKENQFN VVASERISLN RTLPDYRSSA
     CRSIKYEKIS LKTSVVIVFH NEAWSTLMRT VQSVINRSSV DYLEEIILVD DASEKDELIA
     LVESFLKTIP VAHTLIRLPQ RSGLIVGRVR GAEIAKGDVL TFLDAHVEVT DGWLEPLLSR
     ISEDRTRVVA PVIDVISDDT FQYVTAAEST WGGFSWTMNF RWYQASAREQ KRRGKNKTTP
     IRTPTIAGGL FSIDRKYFFD IGAYDEGMRI WGGENLEISF RVWMCGGTLE INPCSHVGHV
     FRKQTPYTFE GGTSNVIYGN ARRTAEVWMD EYKEFYYKMT PSAMFAPLGN ISDRIALRKR
     LGCKSFKWYL KNIYPESNIP PTYYSIGYIK NEKNDLCLDT MGRKASGSPA LLTCHNSGGN
     QQCNNDESQI WDYDPDVTYQ FRHRQSRSCL TPSNNMIVMA ECYKENLLQQ WILEGYNGEL
     FPDYHEETRN KETGIKFEDE LRCEESFSGC KSPEIWPEKL PGLMDFTEKE LNYSGQSASN
     VNFQIEACDI QYMNELGQLT PDQLMEHIKT LQESAYQLGL LEQAEIQRGR LLRILETPDQ
     DVAFL
//
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