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
//