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Database: UniProt
Entry: A0A3B4T3A7_SERDU
LinkDB: A0A3B4T3A7_SERDU
Original site: A0A3B4T3A7_SERDU 
ID   A0A3B4T3A7_SERDU        Unreviewed;       558 AA.
AC   A0A3B4T3A7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, 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=GALNT8 {ECO:0000313|Ensembl:ENSSDUP00000000482.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000482.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000000482.1}
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   AlphaFoldDB; A0A3B4T3A7; -.
DR   Ensembl; ENSSDUT00000000523.1; ENSSDUP00000000482.1; ENSSDUG00000000286.1.
DR   GeneTree; ENSGT00940000160161; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000261420; 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:SF50; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 8-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.
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          421..543
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   558 AA;  63766 MW;  C9C84E482A3BBC74 CRC64;
     HCSCLQITDW FSNINLMNKI EKKEQAAPQN AKTKKERKVV RKLFPNSALF MRWGDELSEE
     EQKEAEKLFQ RYGYNAFLSD RLPLNREIPD TRPSRCAERK YPEDLPTVSV VLIYLDEALS
     IIKRAIRSIM DKTPARLLKE IILVDDHSSN EDLMEKLDEY ITLIHEERPG LVKKVRHSQQ
     LGLTQARLSG WEAAVGDVVA ILDAHIEVHV QWAEPLLSRI KEDRTVILTP VFDKVNYDDL
     KLIPYIPAAD AFDWALWCMY ESFRPEWYSL KDESQPGKSP SIMGILVADR KFFGEIGSLD
     GGMKIYGGEN VELGIRVWLC GGSIEVIPCS KIAHIERATK PYLPDLSVMV KRNALRVAEV
     WLDEYKYNVN IAWNLPVENH GIDIGDVSER KKLRERLNCK PFKWYLDNVY PLLDPLHDVL
     GYGALISDLQ SGLCIDQGPV PGNTPIAYAC HYFSPQHCFY RTNGQLYIGG IKSHKYNSNR
     CLVDTGSGVR LSGEKETDNK MFSTQDGPIQ NRETKRCLEV AMGEDSNYKL VVQQCSGQGW
     KIQNLIKDRL VGKSQKTR
//
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