ID A0A1I7RQP7_BURXY Unreviewed; 598 AA.
AC A0A1I7RQP7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BXYJ_LOCUS5731 {ECO:0000313|EMBL:CAD5219543.1};
OS Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS xylophilus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC Bursaphelenchus.
OX NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_0304200.1};
RN [1] {ECO:0000313|WBParaSite:BXY_0304200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:CAD5219543.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ka4C1 {ECO:0000313|EMBL:CAD5219543.1};
RA Kikuchi T.;
RL Submitted (SEP-2020) 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; CAJFDI010000003; CAD5219543.1; -; Genomic_DNA.
DR EMBL; CAJFCV020000003; CAG9104927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7RQP7; -.
DR WBParaSite; BXY_0304200.1; BXY_0304200.1; BXY_0304200.
DR eggNOG; KOG3736; Eukaryota.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000095284; Unplaced.
DR Proteomes; UP000582659; Unassembled WGS sequence.
DR Proteomes; UP000659654; 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:SF139; 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 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:UP000659654};
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 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 467..594
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 598 AA; 68487 MW; D5D9DCAEA0E0CD52 CRC64;
MPRIPIKWLR VVTAITLVFF IYILANLFNI GPLESSFSAQ NSNRDLENRA ADFQNEQKTV
RNEGKFSIID YAGEGTHFSP EEYEKMEARM KGPGEQGAAV QLTGPLKEAG EKSKKEWFMN
LVASDKISLD RSLRDQRHQD CRILQYDARL PAASVIIVFT DEAWTPLLRT VHSVFNRTPR
NLLHQVVIVD DFSQREDLHE KLEEYLARFG SKLRLVRSKE RLGLIRARAT GAKYATGEVI
IFLDAHCEAS KGWIEPLLQR LKDAPYAFIC PVIDSISDQD MEYQGGSAGG IGSFWWSLHY
KMDNIPEAER KRRKNPHVDL LLTPTMAGGL FAVRRDTFFE FGAYDEEMDI WGGENLEISF
RAWMCGGSVE IIPCSHVGHI YRNGHPYNMT GRGGNKDVHG TNSKRLAEVW MDDYKKFYYL
HRSELKNKDV GDLTPRHALR RSLNCKSFKW YLHNVAYEKF IPDENVKAYG RVKNPHSGLC
FDTLQRNEFK HSIVMGVYHC QYPSSSAQMF SLTNDGILRR ETVCSGAKTE DGKEKLDLQE
CGIHGNGKVF EYRNGHLKLT TINKCLTVEN LKAGDDLHFD ECKEDSKDQL WEFEAPDL
//
