GALT1_BOVIN
ID GALT1_BOVIN Reviewed; 559 AA.
AC Q07537;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 {ECO:0000250|UniProtKB:Q10472};
DE EC=2.4.1.41 {ECO:0000269|PubMed:3082881, ECO:0000269|PubMed:7685345};
DE AltName: Full=Polypeptide GalNAc transferase 1;
DE Short=GalNAc-T1;
DE Short=pp-GaNTase 1;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 1;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1;
DE Contains:
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 soluble form;
GN Name=GALNT1 {ECO:0000250|UniProtKB:Q10472};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-74, FUNCTION, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC TISSUE=Colostrum, and Intestine;
RX PubMed=7685345; DOI=10.1016/s0021-9258(18)31432-7;
RA Homa F.L., Hollander T., Lehman D.J., Thomsen D.R., Elhammer A.P.;
RT "Isolation and expression of a cDNA clone encoding a bovine UDP-
RT GalNAc:polypeptide N-acetylgalactosaminyltransferase.";
RL J. Biol. Chem. 268:12609-12616(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-559, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Colostrum, and Placenta;
RX PubMed=8360184; DOI=10.1016/s0021-9258(17)46720-2;
RA Hagen F.K., van Wuyckhuyse B., Tabak L.A.;
RT "Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide
RT N-acetyl-galactosaminyltransferase.";
RL J. Biol. Chem. 268:18960-18965(1993).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RX PubMed=3082881; DOI=10.1016/s0021-9258(19)57206-4;
RA Elhammer A., Kornfeld S.;
RT "Purification and characterization of UDP-N-acetylgalactosamine:
RT polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and
RT murine lymphoma BW5147 cells.";
RL J. Biol. Chem. 261:5249-5255(1986).
RN [4]
RP MUTAGENESIS OF ASN-95; HIS-125; HIS-137; ASN-141; HIS-146; HIS-179;
RP HIS-211; HIS-228; HIS-341; HIS-344; HIS-404; HIS-427; HIS-460; HIS-498;
RP HIS-499; HIS-517 AND ASN-552.
RX PubMed=9359852; DOI=10.1042/bj3280193;
RA Wragg S., Hagen F.K., Tabak L.A.;
RT "Identification of essential histidine residues in UDP-N-acetyl-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1.";
RL Biochem. J. 328:193-197(1997).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor (PubMed:3082881,
CC PubMed:7685345). Has a broad spectrum of substrates such as apomucin-,
CC MUC5AC-, MUC1- and MUC2-derived peptides (By similarity).
CC {ECO:0000250|UniProtKB:Q10472, ECO:0000269|PubMed:3082881,
CC ECO:0000269|PubMed:7685345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:3082881, ECO:0000269|PubMed:7685345};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:3082881, ECO:0000269|PubMed:7685345};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:3082881};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:3082881, ECO:0000269|PubMed:7685345}.
CC -!- SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase
CC 1]: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1
CC soluble form]: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Colostrum contains a soluble form.
CC {ECO:0000269|PubMed:3082881}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain directs the glycopeptide
CC specificity. It is required in the glycopeptide specificity of enzyme
CC activity but not for activity with naked peptide substrates, suggesting
CC that it triggers the catalytic domain to act on GalNAc-glycopeptide
CC substrates (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated, contains two N-linked oligosaccharides.
CC {ECO:0000269|PubMed:3082881}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07780; AAA30532.1; -; mRNA.
DR EMBL; L17437; AAA68489.1; -; mRNA.
DR PIR; A45987; A45987.
DR RefSeq; NP_803485.1; NM_177519.3.
DR RefSeq; XP_010816977.1; XM_010818675.2.
DR AlphaFoldDB; Q07537; -.
DR SMR; Q07537; -.
DR STRING; 9913.ENSBTAP00000014882; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; Q07537; -.
DR PaxDb; Q07537; -.
DR PRIDE; Q07537; -.
DR Ensembl; ENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
DR Ensembl; ENSBTAT00000069475; ENSBTAP00000066267; ENSBTAG00000011206.
DR Ensembl; ENSBTAT00000081582; ENSBTAP00000067739; ENSBTAG00000011206.
DR GeneID; 282241; -.
DR KEGG; bta:282241; -.
DR CTD; 2589; -.
DR VEuPathDB; HostDB:ENSBTAG00000011206; -.
DR VGNC; VGNC:29222; GALNT1.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000154732; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q07537; -.
DR OMA; VAEVWMC; -.
DR OrthoDB; 606683at2759; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 908.
DR Reactome; R-BTA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000011206; Expressed in thymus and 109 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IEA:Ensembl.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IEA:Ensembl.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW Metal-binding; Reference proteome; Secreted; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1"
FT /id="PRO_0000223386"
FT CHAIN 41..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1
FT soluble form"
FT /id="PRO_0000012255"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..559
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 431..551
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..225
FT /note="Catalytic subdomain A"
FT REGION 285..347
FT /note="Catalytic subdomain B"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 141
FT /note="Not glycosylated"
FT /evidence="ECO:0000305"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3082881"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3082881"
FT DISULFID 106..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 330..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 442..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 482..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 523..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT MUTAGEN 95
FT /note="N->Q: Induces decrease in glycosylation."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 125
FT /note="H->A: Induces a strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 137
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 141
FT /note="N->Q: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 146
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 179
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 211
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 228
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 341
FT /note="H->A: Induces a strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 344
FT /note="H->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 404
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 427
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 460
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 498
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 499
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 517
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:9359852"
FT MUTAGEN 552
FT /note="N->Q: Induces decrease in glycosylation."
FT /evidence="ECO:0000269|PubMed:9359852"
SQ SEQUENCE 559 AA; 64192 MW; E3E538C4DE569B40 CRC64;
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV
VIVFHNEAWS TLLRTVHSVI NRSPRHMLEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR KTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL GLRHKLQCRP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATDE DSQVPSIRDC
SGSRSQQWLL RNVTLPEIF
