UniProt: A0A2D0RH19

Database: UniProt
Entry: A0A2D0RH19_ICTPU

LinkDB:  A0A2D0RH19_ICTPU 
Original site:  A0A2D0RH19_ICTPU

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Ontology (4)   
   GO (4)   
Gene (5)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
All databases (21)   

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ID   A0A2D0RH19_ICTPU        Unreviewed;       606 AA.
AC   A0A2D0RH19;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644, 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=LOC108268952 {ECO:0000313|RefSeq:XP_017329824.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017329824.1};
RN   [1] {ECO:0000313|RefSeq:XP_017329824.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017329824.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU361242}; Single-pass type II membrane protein
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   RefSeq; XP_017329824.1; XM_017474335.3.
DR   AlphaFoldDB; A0A2D0RH19; -.
DR   STRING; 7998.ENSIPUP00000016923; -.
DR   Ensembl; ENSIPUT00000017637; ENSIPUP00000016923; ENSIPUG00000011484.
DR   GeneID; 108268952; -.
DR   KEGG; ipu:108268952; -.
DR   OMA; FANAHAF; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000221080; Chromosome 8.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
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; IPR027791; Galactosyl_T_C.
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:SF50; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 8-RELATED; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   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   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          471..600
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   606 AA;  69576 MW;  6B7CC9F94262ADAD CRC64;
     MRIRSIAKAA CLLGAFALLL CTMFYVMLLS NQSLDLLPRL ERTAEHTILD KLDGLERQIN
     QIAKSLQLSM QKVSQSIEQQ PAVEKKKPLV NKLFPNSELF KKWGDELSKE EQKDAEHLFQ
     LYGYNVFLSD RIPLNRTIPD TRDFRCATKV YPEQLPSLSV VLIYLNEALS ILKRAIHSIV
     DRTPAHLLKE IILVDDHSTN DDLKEKLHEF IDQVHQQRPG LLKKVTHRKK LGLTQARISG
     WKAAVGDVVA ILDAHIEVHK QWAEPLLARI KADRTVLLSP VFDRVEYDTL EVNPYFANAH
     AFDWQLWCMY ESFRPDWYQL EDPSKPGKSP SVMGILVADR KFLGEIGGLD KGMEIYGGEN
     VELGIRVWLC GGSIEIIPCS KIAHIERAHK PYAPDLAEPM RRNALRVAEI WMDEYKRNVY
     VSWNLPLKDH GIDIGNVTER KKLRKQLKCK PFSWYLKNVY PELDTWDDLL GYGTIQSGLL
     ENNCIDQGPV PGSVPVLYQC HFQSPQHCYY KSNGELYIGG IKSHTYNNNR CLVDPGEGNT
     PTLHDCKIAK EKGFHMHWDF KQGHAIKNKD TRKCLEIAQG EDSFYQLVLQ ACSGQKWRIQ
     HVIKEF
//

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