Reviewed, UniProtKB/Swiss-Prot O08912 (GALT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 1
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
    Polypeptide GalNAc transferase 1
      Short name=pp-GaNTase 1
      Short name=GalNAc-T1
Cleaved into the following chain:
    1- Recommended name:
            Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

Gene names

Name:

Galnt1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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. Ref.1
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
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	Widely expressed at high level. Higher expression in kidney, heart, small intestine and cervix and to a lesser extent in all the other tissues tested. Ref.1 Ref.4
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. Ref.3 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
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid O-linked glycosylation Inferred from direct assay. Source: MGI
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay. Source: MGI 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_0000223388

Chain

41 – 559

519

Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

PRO_0000012259

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 28

19

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

63

Catalytic subdomain B

Amino acid modifications

Glycosylation

95

1

N-linked (GlcNAc...) Potential

Glycosylation

552

1

N-linked (GlcNAc...) Ref.5

Disulfide bond

106 ↔ 339

Ref.5

Disulfide bond

330 ↔ 408

Ref.5

Disulfide bond

442 ↔ 459

Ref.5

Disulfide bond

482 ↔ 497

Ref.5

Disulfide bond

523 ↔ 540

Ref.5

Experimental info

Mutagenesis

125

1

H → F: No effect. Ref.3

Mutagenesis

125

1

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

Mutagenesis

127

1

E → Q: Loss of function. Ref.3

Mutagenesis

150

1

E → Q: No effect. Ref.3

Mutagenesis

155

1

D → N: No effect; specificity not affected. Ref.3

Mutagenesis

156

1

D → Q: Loss of function. Ref.3

Mutagenesis

209

1

D → N, A or E: Loss of function. Ref.3

Mutagenesis

211

1

H → A or D: Loss of function. Ref.3

Mutagenesis

213

1

E → Q: Loss of function. Ref.3

Mutagenesis

310

1

D → N: Loss of function. Ref.3

Mutagenesis

319

1

E → Q: Loss of function. Ref.3

Mutagenesis

320

1

N → A: No effect. Ref.3

Mutagenesis

322

1

E → Q: Loss of function. Ref.3

Mutagenesis

341

1

H → A, L, V, K or R: Little or no effect. Ref.3

Mutagenesis

375

1

D → A or N: Little or no effect. Ref.3

Mutagenesis

376

1

E → Q: No effect. Ref.3

Mutagenesis

444

1

D → H: Induces a decrease in activity. Ref.3

Mutagenesis

455

1

G → V: Induces a slight decrease inactivity. Ref.3

Mutagenesis

457

1

F → H: Induces a slight decrease in activity. Ref.3

Mutagenesis

460

1

H → K or N: Induces a slight decrease in activity. Ref.3

Mutagenesis

464

1

G → A: Induces a slight decrease in activity. Ref.3

Mutagenesis

465 – 466

2

NQ → QN: Induces a decrease in activity. Ref.3

Mutagenesis

465

1

N → A: Little or no effect. Induces a slight decrease in activity; when associated with A-466. Ref.3

Mutagenesis

466

1

Q → A: Little or no effect. Induces a slight decrease in activity; when associated with A-465. Ref.3

Sequence conflict

81

1

I → T in AAH56215. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

559

Helix Strand Turn

Details...

Helix

104 – 107

4

Beta strand

118 – 126

9

Helix

129 – 141

13

Helix

145 – 147

3

Beta strand

148 – 155

8

Helix

161 – 163

3

Helix

165 – 172

8

Beta strand

173 – 176

4

Beta strand

178 – 182

5

Helix

189 – 199

11

Beta strand

202 – 214

13

Helix

219 – 228

10

Beta strand

232 – 241

10

Beta strand

243 – 245

3

Beta strand

255 – 259

5

Beta strand

265 – 269

5

Helix

272 – 277

6

Turn

278 – 280

3

Beta strand

293 – 299

7

Helix

300 – 305

6

Helix

322 – 329

8

Beta strand

333 – 345

13

Helix

360 – 373

14

Helix

375 – 378

4

Helix

379 – 383

5

Helix

388 – 390

3

Helix

397 – 405

9

Helix

411 – 417

7

Beta strand

426 – 432

7

Beta strand

434 – 436

3

Turn

437 – 439

3

Beta strand

441 – 444

4

Beta strand

455 – 458

4

Helix

464 – 466

3

Beta strand

468 – 471

4

Beta strand

476 – 478

3

Beta strand

481 – 484

4

Beta strand

493 – 496

4

Helix

502 – 504

3

Beta strand

506 – 509

4

Turn

510 – 513

4

Beta strand

514 – 520

7

Beta strand

522 – 526

5

Beta strand

529 – 531

3

Beta strand

536 – 539

4

Helix

544 – 546

3

Beta strand

548 – 550

3

Sequences

	Sequence		Length	Mass (Da)
	O08912-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: AC5AB655D91F83E4	FASTA	559	64,255
	10 20 30 40 50 60 MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKQER GLPAGDVLEL VQKPHEGPGE 70 80 90 100 110 120 MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV 130 140 150 160 170 180 VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV 190 200 210 220 230 240 IRMEQRSGLI RARLKGAAVS RGQVITFLDA HCECTAGWLE 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 VDYGDISSRL GLRRKLQCKP 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase." Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A. J. Biol. Chem. 272:13843-13848(1997) [PubMed: 9153242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain and Embryo.
[3]	"Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold." Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A. J. Biol. Chem. 274:6797-6803(1999) [PubMed: 10037781] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF HIS-125; GLU-127; GLU-150; ASP-155; ASP-156; ASP-209; HIS-211; GLU-213; ASP-310; GLU-319; ASN-320; GLU-322; HIS-341; ASP-375; GLU-376; ASP-444; GLY-455; PHE-457; HIS-460; GLY-464; ASN-465 AND GLN-466.
[4]	"Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family." Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A. Glycobiology 13:549-557(2003) [PubMed: 12651884] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1." Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A. Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(2004) [PubMed: 15486088] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559, GLYCOSYLATION AT ASN-552, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases

EMBLGenBankDDBJ

U73820 mRNA. Translation: AAB58477.1.
BC056215 mRNA. Translation: AAH56215.1.
BC090962 mRNA. Translation: AAH90962.1.

IPI

IPI00117174.

RefSeq

NP_038842.2.

UniGene

Mm.30249

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XHB	X-ray	2.50	A	88-559	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PRIDE

O08912.

Genome annotation databases

Ensembl

ENSMUSG00000000420. Mus musculus. [Contig view]

GeneID

14423.

KEGG

mmu:14423.

Organism-specific databases

MGI

MGI:894693. Galnt1.

Phylogenomic databases

HOGENOM

O08912.

HOVERGEN

O08912.

OMA

O08912. RIKHDRK.

Enzyme and pathway databases

BRENDA

2.4.1.41. 244.

Gene expression databases

ArrayExpress

O08912.

Bgee

O08912.

GermOnline

ENSMUSG00000000420. Mus musculus.

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]

PROSITE

PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

286021.

SOURCE

Search...

Entry information

Entry name

GALT1_MOUSE

Accession

Primary (citable) accession number: O08912
Secondary accession number(s): Q5BKS3, Q7TND1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)