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   24-JAN-2024, entry version 138.
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.ENSSSCP00000004051; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q29121; 2 sites, No reported glycans.
DR   PaxDb; 9823-ENSSSCP00000028297; -.
DR   PeptideAtlas; 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   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; 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: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; 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:SF123; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 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   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
//