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O08912 (GALT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 1

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 1
Short name=GalNAc-T1
Short name=pp-GaNTase 1
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Gene names
Name:Galnt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. Ref.1

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1

Cofactor

Manganese. Ref.1

Pathway

Protein modification; protein glycosylation.

Subcellular location

Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein By similarity.

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted By similarity.

Tissue specificity

Widely expressed at high level. Higher expression in kidney, heart, small intestine and cervix and to a lesser extent in all the other tissues tested. Ref.1 Ref.4

Domain

There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. Ref.3

The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates By similarity. Ref.3

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1
PRO_0000223388
Chain41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
PRO_0000012259

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 2819Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 559531Lumenal Potential
Domain429 – 551123Ricin B-type lectin
Region115 – 225111Catalytic subdomain A
Region285 – 34763Catalytic subdomain B

Sites

Metal binding2091Manganese
Metal binding2111Manganese
Metal binding3441Manganese
Binding site1561Substrate By similarity
Binding site1861Substrate By similarity
Binding site3161Substrate By similarity
Binding site3471Substrate By similarity
Binding site3521Substrate By similarity

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Ref.5
Disulfide bond106 ↔ 339 Ref.5
Disulfide bond330 ↔ 408 Ref.5
Disulfide bond442 ↔ 459 Ref.5
Disulfide bond482 ↔ 497 Ref.5
Disulfide bond523 ↔ 540 Ref.5

Experimental info

Mutagenesis1251H → F: No effect. Ref.3
Mutagenesis1251H → Q: Induces a strong decrease in activity. Ref.3
Mutagenesis1271E → Q: Loss of enzyme activity. Ref.3
Mutagenesis1501E → Q: No effect. Ref.3
Mutagenesis1551D → N: No effect; specificity not affected. Ref.3
Mutagenesis1561D → Q: Loss of enzyme activity. Ref.3
Mutagenesis2091D → N, A or E: Loss of enzyme activity. Ref.3
Mutagenesis2111H → A or D: Loss of enzyme activity. Ref.3
Mutagenesis2131E → Q: Loss of enzyme activity. Ref.3
Mutagenesis3101D → N: Loss of enzyme activity. Ref.3
Mutagenesis3191E → Q: Loss of enzyme activity. Ref.3
Mutagenesis3201N → A: No effect. Ref.3
Mutagenesis3221E → Q: Loss of enzyme activity. Ref.3
Mutagenesis3411H → A, L, V, K or R: Little or no effect. Ref.3
Mutagenesis3751D → A or N: Little or no effect. Ref.3
Mutagenesis3761E → Q: No effect. Ref.3
Mutagenesis4441D → H: Induces a decrease in activity. Ref.3
Mutagenesis4551G → V: Induces a slight decrease in activity. Ref.3
Mutagenesis4571F → H: Induces a slight decrease in activity. Ref.3
Mutagenesis4601H → K or N: Induces a slight decrease in activity. Ref.3
Mutagenesis4641G → A: Induces a slight decrease in activity. Ref.3
Mutagenesis465 – 4662NQ → QN: Induces a decrease in activity. Ref.3
Mutagenesis4651N → A: Little or no effect. Induces a slight decrease in activity; when associated with A-466. Ref.3
Mutagenesis4661Q → A: Little or no effect. Induces a slight decrease in activity; when associated with A-465. Ref.3
Sequence conflict811I → T in AAH56215. Ref.2

Secondary structure

....................................................................................... 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08912 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: AC5AB655D91F83E4

FASTA55964,255
        10         20         30         40         50         60 
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKQER GLPAGDVLEL VQKPHEGPGE 

        70         80         90        100        110        120 
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV 

       130        140        150        160        170        180 
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV 

       190        200        210        220        230        240 
IRMEQRSGLI RARLKGAAVS RGQVITFLDA HCECTAGWLE PLLARIKHDR RTVVCPIIDV 

       250        260        270        280        290        300 
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 

       310        320        330        340        350        360 
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ 

       370        380        390        400        410        420 
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL GLRRKLQCKP FSWYLENIYP 

       430        440        450        460        470        480 
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD 

       490        500        510        520        530        540 
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC 

       550 
TGSRSQQWLL RNVTLPEIF 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A.
J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain and Embryo.
[3]"Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold."
Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A.
J. Biol. Chem. 274:6797-6803(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, MUTAGENESIS OF HIS-125; GLU-127; GLU-150; ASP-155; ASP-156; ASP-209; HIS-211; GLU-213; ASP-310; GLU-319; ASN-320; GLU-322; HIS-341; ASP-375; GLU-376; ASP-444; GLY-455; PHE-457; HIS-460; GLY-464; ASN-465 AND GLN-466.
[4]"Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family."
Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.
Glycobiology 13:549-557(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1."
Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A.
Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559 IN COMPLEX WITH MANGANESE, GLYCOSYLATION AT ASN-552, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73820 mRNA. Translation: AAB58477.1.
BC056215 mRNA. Translation: AAH56215.1.
BC090962 mRNA. Translation: AAH90962.1.
RefSeqNP_001153876.1. NM_001160404.1.
NP_038842.3. NM_013814.3.
XP_006525713.1. XM_006525650.1.
UniGeneMm.30249.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XHBX-ray2.50A88-559[»]
ProteinModelPortalO08912.
SMRO08912. Positions 95-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08912. 1 interaction.
MINTMINT-4095517.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteO08912.

Proteomic databases

PaxDbO08912.
PRIDEO08912.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000430; ENSMUSP00000000430; ENSMUSG00000000420.
ENSMUST00000170243; ENSMUSP00000132142; ENSMUSG00000000420.
ENSMUST00000178605; ENSMUSP00000137427; ENSMUSG00000000420.
GeneID14423.
KEGGmmu:14423.
UCSCuc008egq.2. mouse.

Organism-specific databases

CTD2589.
MGIMGI:894693. Galnt1.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidO08912.
KOK00710.
OMARIKHDRK.
OrthoDBEOG7J9VP2.
PhylomeDBO08912.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressO08912.
BgeeO08912.
GenevestigatorO08912.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT1. mouse.
EvolutionaryTraceO08912.
NextBio286021.
PROO08912.
SOURCESearch...

Entry information

Entry nameGALT1_MOUSE
AccessionPrimary (citable) accession number: O08912
Secondary accession number(s): Q5BKS3, Q7TND1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot