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
//