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Database: UniProt
Entry: A0A3B4BNI5_PYGNA
LinkDB: A0A3B4BNI5_PYGNA
Original site: A0A3B4BNI5_PYGNA 
ID   A0A3B4BNI5_PYGNA        Unreviewed;       580 AA.
AC   A0A3B4BNI5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
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};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000001138.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000001138.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_017550181.1; XM_017694692.1.
DR   RefSeq; XP_017550191.1; XM_017694702.1.
DR   AlphaFoldDB; A0A3B4BNI5; -.
DR   STRING; 42514.ENSPNAP00000001138; -.
DR   Ensembl; ENSPNAT00000012662.1; ENSPNAP00000001138.1; ENSPNAG00000007977.1.
DR   GeneID; 108425761; -.
DR   CTD; 503760; -.
DR   GeneTree; ENSGT00940000163607; -.
DR   OMA; DWNNFEF; -.
DR   OrthoDB; 202750at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000261440; Unplaced.
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; 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:SF7; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 4; 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          447..580
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          60..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  67077 MW;  62CEE49F2D3A089C CRC64;
     MRVRWSRKVT LLTKACFLFS VLWLFYLLLF RFSTVAPSGD DAAHNILVRQ FSPQAEENTE
     RLQQPIYMKS PPDPNAPGEW GKATRLSLNS EEKKQEEDSI ERYAINIFIS DRISLHRHIQ
     DNRMHECKSQ KYDIHRLPTT SVIIAFYNEA WSTLLRTIHS VLETTPAVLL KEVILIDDFS
     DRGYLKSQLE DYISNLERVR LIRTNKREGL VRARLIGATY ATGEVLTFLD CHCECVPGWI
     EPLLDRIRQN ESTIICPVID TIDWNTFEFY MQTEEPMVGG FDWRLTFQWH SVPEVDRQRR
     KSRTDPIRSP TMAGGLFAVS KAYFEYLGTY DMGMEVWGGE NLELSFRVWQ CGGSLEIHPC
     SHVGHVFPKK APYARPNFLQ NTVRAAEVWM DSYKKHFYNR NPPARKVTYG DISDRTVLRD
     RLKCRSFDWY LNNIYPDLHV PEDRPGWHGA VRSGGIPSEC LDYNAPDHSP TGAHLSLFGC
     HGQGGNQYFE YTSNKEIRFN SVTELCAEVP AGQNYIGMKH CPKDGEPIPP TIVWEFKDDG
     SIYHPHSDMC ITSYRTSQGR TDVQMSRCST GDKHQQWKFE
//
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