Reviewed, UniProtKB/Swiss-Prot Q09324 (GCNT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
    EC=2.4.1.102
Alternative name(s):
    Core 2-branching enzyme
    Core2-GlcNAc-transferase
      Short name=C2GNT

Gene names

Name:

Gcnt1

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	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Forms critical branches in O-glycans. Ref.3
Catalytic activity	UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Expressed in kidney, liver, stomach, spleen, lung and brain. Ref.2
Sequence similarities	Belongs to the glycosyltransferase 14 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 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 – 428

428

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase

PRO_0000191396

Regions

Topological domain

1 – 9

9

Cytoplasmic Potential

Transmembrane

10 – 32

23

Signal-anchor for type II membrane protein Potential

Topological domain

33 – 428

396

Lumenal Potential

Region

33 – 121

89

Stem region

Region

122 – 428

307

Catalytic

Sites

Active site

320

1

Ref.6

Amino acid modifications

Modified residue

236

1

Phosphoserine Ref.5

Modified residue

237

1

Phosphothreonine Ref.5

Modified residue

267

1

Phosphothreonine Ref.5

Glycosylation

58

1

N-linked (GlcNAc...) Ref.6

Glycosylation

95

1

N-linked (GlcNAc...) Ref.6

Disulfide bond

59 ↔ 413

Ref.6 Ref.4

Disulfide bond

100 ↔ 172

Ref.6 Ref.4

Disulfide bond

151 ↔ 199

Ref.6 Ref.4

Disulfide bond

372 ↔ 381

Ref.6 Ref.4

Experimental info

Sequence conflict

191

1

T → S in BAA22999. Ref.2

Sequence conflict

191

1

T → S in BAA22998. Ref.2

Sequence conflict

238

1

G → A in BAA22999. Ref.2

Sequence conflict

238

1

G → A in BAA22998. Ref.2

Sequence conflict

404

1

M → I in BAA22999. Ref.2

Sequence conflict

404

1

M → I in BAA22998. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

428

Helix Strand Turn

Details...

Helix

59 – 63

5

Helix

67 – 78

12

Helix

80 – 83

4

Helix

90 – 96

7

Helix

100 – 107

8

Helix

116 – 119

4

Beta strand

123 – 129

7

Helix

133 – 143

11

Beta strand

148 – 154

7

Helix

160 – 171

12

Beta strand

176 – 178

3

Helix

190 – 206

17

Beta strand

212 – 217

6

Beta strand

221 – 224

4

Helix

226 – 235

10

Turn

236 – 238

3

Beta strand

244 – 246

3

Helix

249 – 251

3

Helix

253 – 256

4

Beta strand

257 – 262

6

Beta strand

265 – 272

8

Beta strand

290 – 292

3

Helix

293 – 301

9

Helix

303 – 312

10

Beta strand

315 – 317

3

Helix

318 – 320

3

Helix

322 – 326

5

Helix

340 – 342

3

Turn

346 – 348

3

Beta strand

349 – 354

6

Turn

357 – 359

3

Helix

363 – 365

3

Beta strand

373 – 377

5

Beta strand

380 – 382

3

Helix

385 – 387

3

Helix

388 – 391

4

Beta strand

397 – 400

4

Turn

404 – 406

3

Helix

408 – 423

16

Sequences

	Sequence		Length	Mass (Da)
	Q09324-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: F3FFD2517B27AAE1	FASTA	428	49,850
	10 20 30 40 50 60 MLRNLFRRRL FSCPTKYYFM LLVLSLITFS VLRIHQKPEF FSVRHLELAG DDPYSNVNCT 70 80 90 100 110 120 KILQGDPEEI QKVKLEILTV QFKKRPRWTP HDYINMTRDC ASFIRTRKYI VEPLTKEEVG 130 140 150 160 170 180 FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDRKAEE SFLAAVQGIA SCFDNVFVAS 190 200 210 220 230 240 QLESVVYASW TRVKADLNCM KDLYRMNANW KYLINLCGMD FPIKTNLEIV RKLKCSTGEN 250 260 270 280 290 300 NLETEKMPPN KEERWKKRYA VVDGKLTNTG IVKAPPPLKT PLFSGSAYFV VTREYVGYVL 310 320 330 340 350 360 ENENIQKLME WAQDTYSPDE FLWATIQRIP EVPGSFPSSN KYDLSDMNAI ARFVKWQYFE 370 380 390 400 410 420 GDVSNGAPYP PCSGVHVRSV CVFGAGDLSW MLRQHHLFAN KFDMDVDPFA IQCLDEHLRR KALENLEH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Warren C.E., Smookler D.S., Dennis J.W. Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: DBA/2.
[2]	"Tissue-specific regulation of mouse core 2 beta-1,6-N-acetylglucosaminyltransferase." Sekine M., Nara K., Suzuki A. J. Biol. Chem. 272:27246-27252(1997) [PubMed: 9341170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Kidney and Submandibular gland.
[3]	"Purification and characterization of UDP-GlcNAc:IV3 beta Gal-Gb4Cer beta-1,6-GlcNAc transferase from mouse kidney." Sekine M., Hashimoto Y., Suzuki M., Inagaki F., Takio K., Suzuki A. J. Biol. Chem. 269:31143-31148(1994) [PubMed: 7983056] [Abstract] Cited for: PROTEIN SEQUENCE OF 62-72; 109-116; 225-232 AND 258-265, FUNCTION. Tissue: Kidney.
[4]	"Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity." Yen T.Y., Macher B.A., Bryson S., Chang X., Tvaroska I., Tse R., Takeshita S., Lew A.M., Datti A. J. Biol. Chem. 278:45864-45881(2003) [PubMed: 12954635] [Abstract] Cited for: DISULFIDE BONDS.
[5]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; THR-237 AND THR-267, MASS SPECTROMETRY. Tissue: Liver.
[6]	"X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism." Pak J.E., Arnoux P., Zhou S., Sivarajah P., Satkunarajah M., Xing X., Rini J.M. J. Biol. Chem. 281:26693-26701(2006) [PubMed: 16829524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 38-428 ALONE AND IN COMPLEX WITH GALBETA1-3GALNAC, DISULFIDE BOND, ACTIVE SITE, GLYCOSYLATION AT ASN-58 AND ASN-95.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

core 2 beta 6 GlcNAc T1

Cross-references

Sequence databases

EMBLGenBankDDBJ

U19265 mRNA. Translation: AAA60948.1.
D87333 mRNA. Translation: BAA22999.1.
D87332 mRNA. Translation: BAA22998.1.

IPI

IPI00311895.

UniGene

Mm.244825

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GAK	X-ray	2.00	A/B	38-428	[»]
2GAM	X-ray	2.70	A/B/C/D	38-428	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT14. Glycosyltransferase Family 14.

PTM databases

PhosphoSite

Q09324.

Proteomic databases

PRIDE

Q09324.

Genome annotation databases

Ensembl

ENSMUSG00000038843. Mus musculus. [Contig view]

Organism-specific databases

MGI

MGI:95676. Gcnt1.

Phylogenomic databases

HOGENOM

Q09324.

HOVERGEN

Q09324.

Enzyme and pathway databases

BRENDA

2.4.1.102. 244.

Gene expression databases

ArrayExpress

Q09324.

Bgee

Q09324.

CleanEx

MM_GCNT1.

GermOnline

ENSMUSG00000038843. Mus musculus.

Family and domain databases

InterPro

IPR003406. Glyco_trans_14.
[Graphical view]

PANTHER

PTHR19297. Glyco_trans_14. 1 hit.

Pfam

PF02485. Branch. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

286198.

SOURCE

Search...

Entry information

Entry name

GCNT1_MOUSE

Accession

Primary (citable) accession number: Q09324
Secondary accession number(s): O35981

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 26, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)