GALT1_RAT
ID GALT1_RAT Reviewed; 559 AA.
AC Q10473;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.41 {ECO:0000269|PubMed:12199709, ECO:0000269|PubMed:12364335, ECO:0000269|PubMed:12419318};
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:0000312|RGD:620358};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Sublingual gland;
RX PubMed=8748168; DOI=10.1007/bf00731252;
RA Hagen F., Gregorie C.A., Tabak L.A.;
RT "Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase.";
RL Glycoconj. J. 12:901-909(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MUTAGENESIS OF CYS-106; CYS-212; CYS-214; CYS-235; CYS-330; CYS-339 AND
RP CYS-408.
RX PubMed=12199709; DOI=10.1046/j.1432-1033.2002.03123.x;
RA Tenno M., Toba S., Kezdy F.J., Elhammer A.P., Kurosaka A.;
RT "Identification of two cysteine residues involved in the binding of UDP-
RT GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
RT (GalNAc-T1).";
RL Eur. J. Biochem. 269:4308-4316(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MUTAGENESIS OF CYS-442; ASP-444; GLY-455; PHE-457; CYS-459; ASN-465;
RP GLN-466; PHE-468; CYS-482; ASP-484; CYS-497; CYS-523; ASP-525 AND CYS-540.
RX PubMed=12364335; DOI=10.1074/jbc.m207369200;
RA Tenno M., Saeki A., Kezdy F.J., Elhammer A.P., Kurosaka A.;
RT "The lectin domain of UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a
RT polypeptide with multiple acceptor sites.";
RL J. Biol. Chem. 277:47088-47096(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.
RX PubMed=12419318; DOI=10.1016/s0006-291x(02)02549-4;
RA Tenno M., Kezdy F.J., Elhammer A.P., Kurosaka A.;
RT "Function of the lectin domain of polypeptide N-
RT acetylgalactosaminyltransferase 1.";
RL Biochem. Biophys. Res. Commun. 298:755-759(2002).
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:12199709,
CC PubMed:12364335, PubMed:12419318). Has a broad spectrum of substrates
CC such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides (By
CC similarity). {ECO:0000250|UniProtKB:Q10472,
CC ECO:0000269|PubMed:12199709, ECO:0000269|PubMed:12364335,
CC ECO:0000269|PubMed:12419318}.
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 -!- 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:12199709, ECO:0000269|PubMed:12364335,
CC ECO:0000269|PubMed:12419318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000305|PubMed:12364335, ECO:0000305|PubMed:12419318};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O08912};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 uM for UDP-N-acetyl-alpha-D-galactosamine
CC {ECO:0000269|PubMed:12199709, ECO:0000269|PubMed:12364335,
CC ECO:0000269|PubMed:12419318};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:12199709, ECO:0000269|PubMed:12364335,
CC ECO:0000269|PubMed:12419318}.
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: Heart, brain, spleen, liver, skeletal muscle and
CC kidney.
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 -!- 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.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
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DR EMBL; U35890; AAC52511.1; -; mRNA.
DR RefSeq; NP_077349.1; NM_024373.1.
DR RefSeq; XP_006254533.1; XM_006254471.3.
DR AlphaFoldDB; Q10473; -.
DR SMR; Q10473; -.
DR STRING; 10116.ENSRNOP00000022117; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q10473; 2 sites.
DR PaxDb; Q10473; -.
DR PRIDE; Q10473; -.
DR Ensembl; ENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207.
DR GeneID; 79214; -.
DR KEGG; rno:79214; -.
DR UCSC; RGD:620358; rat.
DR CTD; 2589; -.
DR RGD; 620358; Galnt1.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000154732; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q10473; -.
DR OMA; VAEVWMC; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q10473; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 5301.
DR Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q10473; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000016207; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q10473; RN.
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; ISO:RGD.
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 GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:RGD.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO:RGD.
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_0000223390"
FT CHAIN 41..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1
FT soluble form"
FT /id="PRO_0000012263"
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 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"
FT MUTAGEN 106
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 212
FT /note="C->A: Loss of enzyme activity due to absence of
FT interaction between UDP moiety and UDP-GalNAC."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 214
FT /note="C->A: Loss of enzyme activity due to absence of
FT interaction between UDP moiety and UDP-GalNAC."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 235
FT /note="C->A: No effect."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 330
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 339
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 408
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12199709"
FT MUTAGEN 442
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 444
FT /note="D->A: Induces a strong decrease in activity; loss of
FT function; when associated with A-484 and A-525."
FT /evidence="ECO:0000269|PubMed:12364335,
FT ECO:0000269|PubMed:12419318"
FT MUTAGEN 455
FT /note="G->Q: Induces a decrease in activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 457
FT /note="F->A: Little or no effect."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 459
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 465
FT /note="N->A: Little or no effect."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 466
FT /note="Q->A: Induces a decrease in activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 468
FT /note="F->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 468
FT /note="F->W,Y: Little or no effect."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 482
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 484
FT /note="D->A: Loss of enzyme activity; when associated with
FT A-444 and A-525."
FT /evidence="ECO:0000269|PubMed:12364335,
FT ECO:0000269|PubMed:12419318"
FT MUTAGEN 497
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 523
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
FT MUTAGEN 525
FT /note="D->A: Loss of enzyme activity; when associated with
FT A-444 and A-484."
FT /evidence="ECO:0000269|PubMed:12364335,
FT ECO:0000269|PubMed:12419318"
FT MUTAGEN 540
FT /note="C->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:12364335"
SQ SEQUENCE 559 AA; 64229 MW; 5E36A95D9422C853 CRC64;
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD VRLEGCKTKV YPDSLPTTSV
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV GLRHKLQCKP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC
TGSRSQQWLL RNVTLPEIF
