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Database: UniProt
Entry: R7UHT6_CAPTE
LinkDB: R7UHT6_CAPTE
Original site: R7UHT6_CAPTE 
ID   R7UHT6_CAPTE            Unreviewed;       568 AA.
AC   R7UHT6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=CAPTEDRAFT_229009 {ECO:0000313|EMBL:ELU05643.1};
OS   Capitella teleta (Polychaete worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Scolecida; Capitellidae; Capitella.
OX   NCBI_TaxID=283909 {ECO:0000313|EMBL:ELU05643.1};
RN   [1] {ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|Proteomes:UP000014760};
RA   Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA   Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA   Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA   Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA   Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELU05643.1, ECO:0000313|Proteomes:UP000014760}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I ESC-2004 {ECO:0000313|EMBL:ELU05643.1,
RC   ECO:0000313|Proteomes:UP000014760};
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
RN   [3] {ECO:0000313|EnsemblMetazoa:CapteP229009}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361242};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {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}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|RuleBase:RU361242}.
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DR   EMBL; AMQN01001310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB301364; ELU05643.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7UHT6; -.
DR   STRING; 283909.R7UHT6; -.
DR   EnsemblMetazoa; CapteT229009; CapteP229009; CapteG229009.
DR   HOGENOM; CLU_411201_0_0_1; -.
DR   OMA; NIVDEYQ; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000014760; 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:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
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:SF119; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 2; 1.
DR   Pfam; PF00535; Glycos_transf_2; 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|RuleBase:RU361242};
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|RuleBase:RU361242};
KW   Membrane {ECO:0000256|RuleBase:RU361242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014760};
KW   Transferase {ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|RuleBase:RU361242};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361242}.
FT   TRANSMEM        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          135..298
FT                   /note="Glycosyltransferase 2-like"
FT                   /evidence="ECO:0000259|Pfam:PF00535"
FT   REGION          85..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..105
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   568 AA;  64508 MW;  E76E44F1358BB8E9 CRC64;
     MALSWRQLVT SALPVLARSR TIPVPYDREN RRNIVETTPT MLRSKLRGGA FTDFMLIAVL
     VILVYVFITR RGIGAPSDNE VIMNRAAPQE RHKSPISTTS DSESQHMIDS RIKMLPDFRS
     SQCRSAVRKQ TTPVSIVIDF YDYQFYDLKT TISAILHNTP PELIAEMLLI NDGSSLIYIE
     EEAERYVKEL EGGRLLKNDE QMGSPKARMK AFREAKSSIV VFIDHSVIVN DGWLEPLIAG
     LMDKPKSIMV PHYDHVHDPV SYELKSTSDN LVSTFSWRMI TRMTESKLGM SEQYYKSPVL
     RGNIFAVTQQ YFKAIGGYEE NLSEFGGENL ELSVRSWLCG GPIYVNPCSR VGILNLKDPV
     KIQSHKNLRL ITEVWFASYK DIAYRTSNVD SSVSSAEKVI IETMKKKLER STCKTIDWYI
     NDIVKDIASP SEKAKFFGLL RCKTGRCGKV GKDGRVELGQ CSPDKYGAHS SDMLFEYDSD
     RKVKVNGKCL STKSTAYIQA EECVDKDVHQ MYDYTDKLYF KNVWSGYCWM HVTDPDKSTG
     GKRQIAMAQD CETDTSDGQF ISFEFIPL
//
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