Polypeptide N-acetylgalactosaminyltransferase 1

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Q07537 (GALT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Cleaved into the following chain:

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

Gene names

Name:

GALNT1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Calcium.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted By similarity.
Tissue specificity	Colostrum contains a soluble form.
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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein O-linked glycosylation via serine Inferred from electronic annotation. Source: Compara protein O-linked glycosylation via threonine Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	manganese ion binding Inferred from electronic annotation. Source: Compara polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 559

559

Polypeptide N-acetylgalactosaminyltransferase 1

PRO_0000223386

Chain

41 – 559

519

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

PRO_0000012255

Regions

Topological domain

1 – 8

Cytoplasmic Potential

Transmembrane

9 – 28

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

29 – 559

531

Lumenal Potential

Region

115 – 225

111

Catalytic subdomain A

Region

285 – 347

Catalytic subdomain B

Sites

Site

141

Not glycosylated Probable

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Probable

Glycosylation

552

N-linked (GlcNAc...) Probable

Disulfide bond

106 ↔ 339

By similarity

Disulfide bond

330 ↔ 408

By similarity

Disulfide bond

442 ↔ 459

By similarity

Disulfide bond

482 ↔ 497

By similarity

Disulfide bond

523 ↔ 540

By similarity

Experimental info

Mutagenesis

N → Q: Induces decrease in glycosylation. Ref.3

Mutagenesis

125

H → A: Induces a strong decrease in activity. Ref.3

Mutagenesis

137

H → A: No effect. Ref.3

Mutagenesis

141

N → Q: No effect. Ref.3

Mutagenesis

146

H → A: No effect. Ref.3

Mutagenesis

179

H → A: No effect. Ref.3

Mutagenesis

211

H → A: Loss of function. Ref.3

Mutagenesis

228

H → A: No effect. Ref.3

Mutagenesis

341

H → A: Induces a strong decrease in activity. Ref.3

Mutagenesis

344

H → A: Loss of function. Ref.3

Mutagenesis

404

H → A: No effect. Ref.3

Mutagenesis

427

H → A: No effect. Ref.3

Mutagenesis

460

H → A: No effect. Ref.3

Mutagenesis

498

H → A: No effect. Ref.3

Mutagenesis

499

H → A: No effect. Ref.3

Mutagenesis

517

H → A: No effect. Ref.3

Mutagenesis

552

N → Q: Induces decrease in glycosylation. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q07537 [UniParc].

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

FASTA

559

64,192

        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

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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], 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]	"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.
IPI	IPI00718170.
PIR	A45987.
RefSeq	NP_803485.1. NM_177519.2.
UniGene	Bt.65693.
3D structure databases
ProteinModelPortal	Q07537.
SMR	Q07537. Positions 95-553.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000014882.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneID	282241.
KEGG	bta:282241.
Organism-specific databases
CTD	2589.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104138.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q07537.
KO	K00710.
OMA	RIKHDRK.
OrthoDB	EOG40P46C.
Enzyme and pathway databases
BRENDA	2.4.1.41. 908.
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20806060.

Entry information

Entry name

GALT1_BOVIN

Accession

Primary (citable) accession number: Q07537

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents