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Q07537 (GALT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 Ref.3

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1 Ref.3

Cofactor

Manganese. Ref.3

Pathway

Protein modification; protein glycosylation.

Subcellular location

Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein By similarity Ref.3.

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

Tissue specificity

Colostrum contains a soluble form. Ref.3

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 By similarity.

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.

Post-translational modification

N-glycosylated, contains two N-linked oligosaccharides. 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_0000223386
Chain41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
PRO_0000012255

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 559531Lumenal Potential
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
Site1411Not glycosylated Probable

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Probable
Glycosylation5521N-linked (GlcNAc...) Probable
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

Mutagenesis951N → Q: Induces decrease in glycosylation. Ref.4
Mutagenesis1251H → A: Induces a strong decrease in activity. Ref.4
Mutagenesis1371H → A: No effect. Ref.4
Mutagenesis1411N → Q: No effect. Ref.4
Mutagenesis1461H → A: No effect. Ref.4
Mutagenesis1791H → A: No effect. Ref.4
Mutagenesis2111H → A: Loss of enzyme activity. Ref.4
Mutagenesis2281H → A: No effect. Ref.4
Mutagenesis3411H → A: Induces a strong decrease in activity. Ref.4
Mutagenesis3441H → A: Loss of enzyme activity. Ref.4
Mutagenesis4041H → A: No effect. Ref.4
Mutagenesis4271H → A: No effect. Ref.4
Mutagenesis4601H → A: No effect. Ref.4
Mutagenesis4981H → A: No effect. Ref.4
Mutagenesis4991H → A: No effect. Ref.4
Mutagenesis5171H → A: No effect. Ref.4
Mutagenesis5521N → Q: Induces decrease in glycosylation. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q07537 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E3E538C4DE569B40

FASTA55964,192
        10         20         30         40         50         60 
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 

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

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

       190        200        210        220        230        240 
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR KTVVCPIIDV 

       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 GLRHKLQCRP FSWYLENIYP 

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

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

       550 
SGSRSQQWLL RNVTLPEIF 

« Hide

References

[1]"Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
Homa F.L., Hollander T., Lehman D.J., Thomsen D.R., Elhammer A.P.
J. Biol. Chem. 268:12609-12616(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 41-74.
Tissue: Colostrum and Intestine.
[2]"Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase."
Hagen F.K., van Wuyckhuyse B., Tabak L.A.
J. Biol. Chem. 268:18960-18965(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-559, PARTIAL PROTEIN SEQUENCE.
Tissue: Colostrum and Placenta.
[3]"Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells."
Elhammer A., Kornfeld S.
J. Biol. Chem. 261:5249-5255(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
[4]"Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1."
Wragg S., Hagen F.K., Tabak L.A.
Biochem. J. 328:193-197(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASN-95; HIS-125; HIS-137; ASN-141; HIS-146; HIS-179; HIS-211; HIS-228; HIS-341; HIS-344; HIS-404; HIS-427; HIS-460; HIS-498; HIS-499; HIS-517 AND ASN-552.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07780 mRNA. Translation: AAA30532.1.
L17437 mRNA. Translation: AAA68489.1.
PIRA45987.
RefSeqNP_803485.1. NM_177519.2.
UniGeneBt.65693.

3D structure databases

ProteinModelPortalQ07537.
SMRQ07537. Positions 95-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000014882.

Protein family/group databases

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

Proteomic databases

PRIDEQ07537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneID282241.
KEGGbta:282241.

Organism-specific databases

CTD2589.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00730000110345.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ07537.
KOK00710.
OMARIKHDRK.
OrthoDBEOG7J9VP2.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 908.
UniPathwayUPA00378.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
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

NextBio20806060.

Entry information

Entry nameGALT1_BOVIN
AccessionPrimary (citable) accession number: Q07537
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 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