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Q29121 (GALT1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

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.

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.

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_0000223389
Chain41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble form By similarity
PRO_0000012261

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

Sequences

Sequence LengthMass (Da)Tools
Q29121 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 68C2D261A51684C6

FASTA55964,119
        10         20         30         40         50         60 
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 

        70         80         90        100        110        120 
MGKPVVIPKE DQDKMKEMFK 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 EVWMDEFKTF FYIISPGVTK VDYGDISSRL GLRHKLQCRP FSWYLENIYP 

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

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

       550 
SGSRSQQWLL RNVTLPEIF 

« Hide

References

[1]"Cloning and expression of a porcine UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferase."
Yoshida A., Hara T., Ikenaga H., Takeuchi M.
Glycoconj. J. 12:824-828(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85389 mRNA. Translation: BAA12800.1.

3D structure databases

ProteinModelPortalQ29121.
SMRQ29121. Positions 95-553.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000004051.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.

Enzyme and pathway databases

BRENDA2.4.1.41. 6170.
UniPathwayUPA00378.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGALT1_PIG
AccessionPrimary (citable) accession number: Q29121
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 105 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