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Database: UniProt
Entry: W5NEG8_LEPOC
LinkDB: W5NEG8_LEPOC
Original site: W5NEG8_LEPOC 
ID   W5NEG8_LEPOC            Unreviewed;       537 AA.
AC   W5NEG8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000019027.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000019027.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   EMBL; AHAT01027891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01027892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01027893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01027894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01027895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01027896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NEG8; -.
DR   Ensembl; ENSLOCT00000019059.1; ENSLOCP00000019027.1; ENSLOCG00000015454.1.
DR   GeneTree; ENSGT00940000156958; -.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000018468; Linkage group LG16.
DR   Bgee; ENSLOCG00000015454; Expressed in zone of skin and 13 other cell types or tissues.
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:SF49; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 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   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          407..532
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  60990 MW;  FB9C735E1A532A8A CRC64;
     GGGSVEWKDD WNGAEPLKRK EAQSSDGDDK ARGPETLPPG KVRWQDFDQD LYVGATVVRP
     GQDPYARNKF NQVESDKLRM DRAVPDTRHD HCRRKQWRTD LPASSVVITF HNEARSALLR
     TVVSVLKKSP PHLIKEIILV DDYSDNAEDG ALLAKIEKVR VLRNDRREGL MRSRVRGADA
     AVAKVLTFLD SHCECNEQWL EPLLERVAED RTRVVSPIID VINMDNFQYV GASADLKGGF
     DWNLVFKWDY MTLEQRRARQ GNPIAPIKTP MIAGGLFVMD KDYFEELGKY DMMMDVWGGE
     NLEISFRVWQ CGGSLEIIPC SRVGHVFRKQ HPYTFPGGSG TVFARNTRRA AEVWMDEFKN
     FYYAAVPSAR NVPYGNIQSR MEMKKRLACK PFKWYLENVY PELRVPDHQD IAFGALQQGS
     NCLDTLGHFA DGVVGVYECH NAGGNQEWAL TKDKSVKHMD LCLTVVDRAA GSQIKLQGCR
     ENDSRQKWEQ IENNSKLRHV GSNLCLDSRS ARSGGLTVEV CSPSLTQQWK FTLNLQQ
//
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