ID A0A158PGK5_ANGCS Unreviewed; 513 AA.
AC A0A158PGK5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ACOC_LOCUS5334 {ECO:0000313|EMBL:VDM56919.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000533301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000533301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM56919.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM56919.1,
RC ECO:0000313|Proteomes:UP000267027};
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; UYYA01003864; VDM56919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PGK5; -.
DR STRING; 334426.A0A158PGK5; -.
DR WBParaSite; ACOC_0000533301-mRNA-1; ACOC_0000533301-mRNA-1; ACOC_0000533301.
DR OMA; PVFQPWH; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; 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:SF63; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE; 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, ECO:0000256|RuleBase:RU361242};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027};
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 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 381..502
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 513 AA; 58923 MW; F79328E20CC26894 CRC64;
MLLLLLLLLR LALLLVYIMI FAIIIPNAAT VAVAVAVAVA ITFAVTHHIL SAIHYRLAVM
KLTTTTNDVH ICRCPHSFMT SLPKASIVIC YFNESPSVLI RMINSIVDRT PLELIQEILL
VDDGSEWPEA SLQAADYQRK HPQWNMVKFL HTPSNLGLIR AKVFGARKAR GEVLVFLDSH
CEVNQNWLQP LLERIREKPN RVVCPIIDVI DLDTMKYVES PVCKGGLNWG LTFKWDYPLH
TYFIDPLNYI RPLKSATMAG GLFAIDRTYF FKIGAYDEGM DVWGAENVEI SFRIWLCGGE
LEIIPCSRVG HIFRKKRPYG LESDSISKNS LRAARVWLDE YLPEFFKSRP YLESNTDYGD
ISDRLKLKEN LHCKPFRWYL ENVYPELLPN NIPMSSDIIQ KPFINGKNSS QSHYFIIIRK
IQIRLANTSF CLTAEESPMG LIAKGSRVEM RICHAKRNQQ WRWNDNNEFR PMGSSRLCLD
SLKGLTLLKC HNQGAHQDWK ITVRVFIVSN LMH
//
