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Q10473 (GALT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Catalytic activity

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

Cofactor

Manganese.

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

Heart, brain, spleen, liver, skeletal muscle and kidney.

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.

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.

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_0000223390
Chain41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
PRO_0000012263

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; 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 By similarity
Metal binding2111Manganese By similarity
Metal binding3441Manganese By similarity
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...) Potential
Disulfide bond106 ↔ 339 By similarity
Disulfide bond330 ↔ 408 By similarity
Disulfide bond442 ↔ 459 By similarity
Disulfide bond482 ↔ 497 By similarity
Disulfide bond523 ↔ 540 By similarity

Experimental info

Mutagenesis1061C → A: Loss of enzyme activity. Ref.2
Mutagenesis2121C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. Ref.2
Mutagenesis2141C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. Ref.2
Mutagenesis2351C → A: No effect. Ref.2
Mutagenesis3301C → A: Loss of enzyme activity. Ref.2
Mutagenesis3391C → A: Loss of enzyme activity. Ref.2
Mutagenesis4081C → A: Loss of enzyme activity. Ref.2
Mutagenesis4421C → A: Loss of enzyme activity. Ref.3
Mutagenesis4441D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. Ref.3 Ref.4
Mutagenesis4551G → Q: Induces a decrease in activity. Ref.3
Mutagenesis4571F → A: Little or no effect. Ref.3
Mutagenesis4591C → A: Loss of enzyme activity. Ref.3
Mutagenesis4651N → A: Little or no effect. Ref.3
Mutagenesis4661Q → A: Induces a decrease in activity. Ref.3
Mutagenesis4681F → A: Loss of enzyme activity. Ref.3
Mutagenesis4681F → W or Y: Little or no effect. Ref.3
Mutagenesis4821C → A: Loss of enzyme activity. Ref.3
Mutagenesis4841D → A: Loss of enzyme activity; when associated with A-444 and A-525. Ref.3 Ref.4
Mutagenesis4971C → A: Loss of enzyme activity. Ref.3
Mutagenesis5231C → A: Loss of enzyme activity. Ref.3
Mutagenesis5251D → A: Loss of enzyme activity; when associated with A-444 and A-484. Ref.3 Ref.4
Mutagenesis5401C → A: Loss of enzyme activity. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q10473 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5E36A95D9422C853

FASTA55964,229
        10         20         30         40         50         60 
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL VQKPHEGPGE 

        70         80         90        100        110        120 
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD VRLEGCKTKV YPDSLPTTSV 

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

       190        200        210        220        230        240 
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE 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 VDYGDISSRV GLRHKLQCKP 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

[1]"Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
Hagen F., Gregorie C.A., Tabak L.A.
Glycoconj. J. 12:901-909(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Sublingual gland.
[2]"Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)."
Tenno M., Toba S., Kezdy F.J., Elhammer A.P., Kurosaka A.
Eur. J. Biochem. 269:4308-4316(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-106; CYS-212; CYS-214; CYS-235; CYS-330; CYS-339 AND CYS-408.
[3]"The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites."
Tenno M., Saeki A., Kezdy F.J., Elhammer A.P., Kurosaka A.
J. Biol. Chem. 277:47088-47096(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-442; ASP-444; GLY-455; PHE-457; CYS-459; ASN-465; GLN-466; PHE-468; CYS-482; ASP-484; CYS-497; CYS-523; ASP-525 AND CYS-540.
[4]"Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1."
Tenno M., Kezdy F.J., Elhammer A.P., Kurosaka A.
Biochem. Biophys. Res. Commun. 298:755-759(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U35890 mRNA. Translation: AAC52511.1.
RefSeqNP_077349.1. NM_024373.1.
XP_006254533.1. XM_006254471.1.
UniGeneRn.10266.

3D structure databases

ProteinModelPortalQ10473.
SMRQ10473. Positions 95-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4566270.
STRING10116.ENSRNOP00000022117.

Protein family/group databases

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

Proteomic databases

PaxDbQ10473.
PRIDEQ10473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207.
GeneID79214.
KEGGrno:79214.
UCSCRGD:620358. rat.

Organism-specific databases

CTD2589.
RGD620358. Galnt1.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ10473.
KOK00710.
OMARIKHDRK.
OrthoDBEOG7J9VP2.
PhylomeDBQ10473.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ10473.

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

NextBio614616.
PROQ10473.

Entry information

Entry nameGALT1_RAT
AccessionPrimary (citable) accession number: Q10473
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 119 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

PATHWAY comments

Index of metabolic and biosynthesis pathways