ID A0A0N4W9B2_HAEPC Unreviewed; 692 AA.
AC A0A0N4W9B2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=HPLM_LOCUS6859 {ECO:0000313|EMBL:VDO30241.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000686701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000686701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO30241.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO30241.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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}.
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DR EMBL; UZAF01016560; VDO30241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4W9B2; -.
DR STRING; 6290.A0A0N4W9B2; -.
DR WBParaSite; HPLM_0000686701-mRNA-1; HPLM_0000686701-mRNA-1; HPLM_0000686701.
DR OMA; HRLIMAP; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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:SF137; N-ACETYLGALACTOSAMINYLTRANSFERASE 6-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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000268014};
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 541..675
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 692 AA; 79285 MW; 96DC6F1F69F4AA73 CRC64;
MAFMRSLSDP KEASPRIWFG PYENGNEFYL ISFLRRVVHV NDLLLPAGSA LNINSSPKFT
TSTKPERPLR GGRGVQVVVG HYNGNLPQEK LRNLTDESEW RAGERLRLKF FSEEINANNF
NPIGWGEGGE PVRLSKEDER LSDETFGINQ FSLFVSDRIA LNRSLDDYRK PSCRVKKYRD
VSELPSTSVI IVYHNEAFST LLRTTQSVVN RSPRALLKEI ILVDDFSNRT FLKYPTLDEA
VRDYPVPVKI LRTKQRVGLI RARLMGAQEA IGDVLTFLDS HCECTEGWLE PLLDRIKDNR
KAVVCPVIDV INDRTFQYQK GLDVFRGGFN WNLQFRWYAI PSDMVKKRLA NPTAPIPSPT
MAGGLFSIDR HYFEELGTYD HGMDIWGGEN IEISFRIWQC GGRVEILPCS HVGHIFRHSS
PHDIPGSSSG KVLDGNMVRV AEVWMDEWKF LFYKLAPQTG KLRTSVDLSE RLELRRRLGC
KSFRWYLENV FIDHHLPMTG DFFGRIQFPA DTSNGTCLAW ALAMSGIKKA TQASCTDNID
RAQISLVSYQ LCMVNRPGEP GTKKHRLIMA PCTLGFDHWQ FWIYTKNGHL KSDEHMCLTA
NQVVHTNGEW MVQLKECAGY DTELWEYNRK RHTFKHRKSG LCLTQRDPDM EKVDNLSPPT
LTSCGRGHEQ QVRGLHRRSI ALKAQYTSKN IV
//
