Polypeptide N-acetylgalactosaminyltransferase 1

Contribute

Send feedback

Read comments (?) or add your own

Q10473 (GALT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 101. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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

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 Reference proteome
Gene Ontology (GO)
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
Molecular function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from mutant phenotype Ref.3. Source: RGD sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
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_0000223390

Chain

41 – 559

519

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

PRO_0000012263

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

Domain

429 – 551

123

Ricin B-type lectin

Region

115 – 225

111

Catalytic subdomain A

Region

285 – 347

Catalytic subdomain B

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

552

N-linked (GlcNAc...) Potential

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

106

C → A: Loss of function. Ref.2

Mutagenesis

212

C → A: Loss of function due to absence of interaction between UDP moiety and UDP-GalNAC. Ref.2

Mutagenesis

214

C → A: Loss of function due to absence of interaction between UDP moiety and UDP-GalNAC. Ref.2

Mutagenesis

235

C → A: No effect. Ref.2

Mutagenesis

330

C → A: Loss of function. Ref.2

Mutagenesis

339

C → A: Loss of function. Ref.2

Mutagenesis

408

C → A: Loss of function. Ref.2

Mutagenesis

442

C → A: Loss of function. Ref.3

Mutagenesis

444

D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. Ref.3 Ref.4

Mutagenesis

455

G → Q: Induces a decrease in activity. Ref.3

Mutagenesis

457

F → A: Little or no effect. Ref.3

Mutagenesis

459

C → A: Loss of function. Ref.3

Mutagenesis

465

N → A: Little or no effect. Ref.3

Mutagenesis

466

Q → A: Induces a decrease in activity. Ref.3

Mutagenesis

468

F → A: Loss of function. Ref.3

Mutagenesis

468

F → W or Y: Little or no effect. Ref.3

Mutagenesis

482

C → A: Loss of function. Ref.3

Mutagenesis

484

D → A: Loss of function; when associated with A-444 and A-525. Ref.3 Ref.4

Mutagenesis

497

C → A: Loss of function. Ref.3

Mutagenesis

523

C → A: Loss of function. Ref.3

Mutagenesis

525

D → A: Loss of function; when associated with A-444 and A-484. Ref.3 Ref.4

Mutagenesis

540

C → A: Loss of function. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q10473 [UniParc].

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

FASTA

559

64,229

        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: 8748168] [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: 12199709] [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: 12364335] [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: 12419318] [Abstract] Cited for: MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U35890 mRNA. Translation: AAC52511.1.
IPI	IPI00209002.
RefSeq	NP_077349.1. NM_024373.1.
UniGene	Rn.10266.
3D structure databases
ProteinModelPortal	Q10473.
SMR	Q10473. Positions 95-553.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10473.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q10473.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207.
GeneID	79214.
KEGG	rno:79214.
UCSC	NM_024373. rat.
Organism-specific databases
CTD	2589.
RGD	620358. Galnt1.
Phylogenomic databases
eggNOG	roNOG04476.
GeneTree	ENSGT00600000084102.
HOVERGEN	HBG051699.
InParanoid	Q10473.
OMA	IQKPHEG.
OrthoDB	EOG40P46C.
PhylomeDB	Q10473.
Gene expression databases
ArrayExpress	Q10473.
Genevestigator	Q10473.
GermOnline	ENSRNOG00000016207. Rattus norvegicus.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. IPR000772. Ricin_B_lectin. [Graphical view]
KO	K00710.
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	614616.

Entry information

Entry name

GALT1_RAT

Accession

Primary (citable) accession number: Q10473

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 16, 2011
This is version 101 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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents