GALT1_PIG
ID GALT1_PIG Reviewed; 559 AA.
AC Q29121;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 {ECO:0000250|UniProtKB:Q10472};
DE EC=2.4.1.41 {ECO:0000269|PubMed:8748160};
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Lung;
RX PubMed=8748160; DOI=10.1007/bf00731244;
RA Yoshida A., Hara T., Ikenaga H., Takeuchi M.;
RT "Cloning and expression of a porcine UDP-GalNAc: polypeptide N-
RT acetylgalactosaminyl transferase.";
RL Glycoconj. J. 12:824-828(1995).
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:8748160).
CC Has a broad spectrum of substrates such as apomucin-, MUC5AC-,
CC MUC1- and MUC2-derived peptides (By similarity).
CC {ECO:0000250|UniProtKB:Q10472, ECO:0000269|PubMed:8748160}.
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:8748160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957;
CC Evidence={ECO:0000305|PubMed:8748160};
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:8748160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000305|PubMed:8748160};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O08912};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8748160}.
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 -!- 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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
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DR EMBL; D85389; BAA12800.1; -; mRNA.
DR AlphaFoldDB; Q29121; -.
DR SMR; Q29121; -.
DR STRING; 9823.ENSSSCP00000028297; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR PaxDb; Q29121; -.
DR PeptideAtlas; Q29121; -.
DR PRIDE; Q29121; -.
DR eggNOG; KOG3736; Eukaryota.
DR InParanoid; Q29121; -.
DR BRENDA; 2.4.1.41; 6170.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Secreted;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1"
FT /id="PRO_0000223389"
FT CHAIN 41..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1
FT soluble form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000012261"
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 429..551
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 45..66
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 CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 559 AA; 64119 MW; 68C2D261A51684C6 CRC64;
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE
MGKPVVIPKE DQDKMKEMFK 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 EVWMDEFKTF FYIISPGVTK VDYGDISSRL GLRHKLQCRP FSWYLENIYP
DSQIPRHYSS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC
SGSRSQQWLL RNVTLPEIF
