ID E1BBP1_BOVIN Unreviewed; 633 AA.
AC E1BBP1;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 89.
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=GALNT3 {ECO:0000313|Ensembl:ENSBTAP00000018541.6,
GN ECO:0000313|VGNC:VGNC:29232};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000018541.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000018541.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018541.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000018541.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018541.6};
RG Ensembl;
RL Submitted (NOV-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; NP_001179787.1; NM_001192858.1.
DR AlphaFoldDB; E1BBP1; -.
DR SMR; E1BBP1; -.
DR STRING; 9913.ENSBTAP00000018541; -.
DR PaxDb; 9913-ENSBTAP00000018541; -.
DR Ensembl; ENSBTAT00000018541.6; ENSBTAP00000018541.6; ENSBTAG00000013957.6.
DR GeneID; 535458; -.
DR KEGG; bta:535458; -.
DR CTD; 2591; -.
DR VEuPathDB; HostDB:ENSBTAG00000013957; -.
DR VGNC; VGNC:29232; GALNT3.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156609; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; E1BBP1; -.
DR OMA; NPLFKMC; -.
DR TreeFam; TF313267; -.
DR Reactome; R-BTA-190372; FGFR3c ligand binding and activation.
DR Reactome; R-BTA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000013957; Expressed in spermatid and 99 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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:SF33; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 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, ECO:0000256|RuleBase:RU361242};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361242};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361242}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361242"
FT DOMAIN 506..630
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 72699 MW; 938734C978BA0571 CRC64;
MAHLKRLVKL HLKRHYHKKF WKLGAVVFFF IIFLILMQRE VSVQYSKEES RMERNMKNKN
KMFDLMIEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG YYTAAELKPV LDRPPQDSNA
PGASGKAFKT TNLSAEEQKE KERGEAKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR
CPPLPTTSVI IVFHNEAWST LLRTVYSVLY SSPAILLKEI ILVDDASVDE YLHDKLEEYI
KQFSIVKIVR QKERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE TLPDHEKQRR KDETYPIKTP
TFAGGLFSIS KDYFEYIGTY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK
SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKSFGDL SKRFEIKHRL
QCKNFTWYLN NIYPEVYVPD LNPVISGYIK SVGRPLCLDV GENNQGGKPL ILYTCHGLGG
NQYFEYSAQH EIRHNIQKEL CLHAALGAVQ LKACAYKGHK TVAIGEQIWE IQKDQLLYNP
FFKMCLSASG EHPSLVSCNP SDSLQKWIFN QND
//
