Q09324 (GCNT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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 › Mus

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms critical branches in O-glycans. Ref.4
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 Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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

Helical; 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.7

Amino acid modifications

Modified residue

236

1

Phosphoserine Ref.6

Modified residue

237

1

Phosphothreonine Ref.6

Modified residue

267

1

Phosphothreonine Ref.6

Glycosylation

58

1

N-linked (GlcNAc...) Ref.7

Glycosylation

95

1

N-linked (GlcNAc...) Ref.7

Disulfide bond

59 ↔ 413

Ref.5 Ref.7

Disulfide bond

100 ↔ 172

Ref.5 Ref.7

Disulfide bond

151 ↔ 199

Ref.5 Ref.7

Disulfide bond

372 ↔ 381

Ref.5 Ref.7

Experimental info

Sequence conflict

88

1

R → W in AAA60948. Ref.1

Sequence conflict

88

1

R → W in BAA22998. Ref.2

Sequence conflict

88

1

R → W in BAA22999. Ref.2

Sequence conflict

191

1

S → T in AAA60948. Ref.1

Sequence conflict

238

1

G → A in BAA22998. Ref.2

Sequence conflict

238

1

G → A in BAA22999. Ref.2

Sequence conflict

260

1

T → A in AAA60948. Ref.1

Sequence conflict

260

1

T → A in BAA22998. Ref.2

Sequence conflict

260

1

T → A in BAA22999. Ref.2

Sequence conflict

362

1

H → D in AAA60948. Ref.1

Sequence conflict

362

1

H → D in BAA22998. Ref.2

Sequence conflict

362

1

H → D in BAA22999. Ref.2

Sequence conflict

404

1

M → I in BAA22998. Ref.2

Sequence conflict

404

1

M → I in BAA22999. Ref.2

Sequence conflict

420

1

H → R in AAA60948. Ref.1

Sequence conflict

420

1

H → R in BAA22998. Ref.2

Sequence conflict

420

1

H → R in BAA22999. Ref.2

Secondary structure

1

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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 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 57E54F07AFFE640B	FASTA	428	49,839
	10 20 30 40 50 60 MLRNLFRRRL FSCPTKYYFM LLVLSLITFS VLRIHQKPEF FSVRHLELAG DDPYSNVNCT 70 80 90 100 110 120 KILQGDPEEI QKVKLEILTV QFKKRPRRTP HDYINMTRDC ASFIRTRKYI VEPLTKEEVG 130 140 150 160 170 180 FPIAYSIVVH HKIEMLDRLL RAIYMPQNFY CIHVDRKAEE SFLAAVQGIA SCFDNVFVAS 190 200 210 220 230 240 QLESVVYASW SRVKADLNCM KDLYRMNANW KYLINLCGMD FPIKTNLEIV RKLKCSTGEN 250 260 270 280 290 300 NLETEKMPPN KEERWKKRYT VVDGKLTNTG IVKAPPPLKT PLFSGSAYFV VTREYVGYVL 310 320 330 340 350 360 ENENIQKLME WAQDTYSPDE FLWATIQRIP EVPGSFPSSN KYDLSDMNAI ARFVKWQYFE 370 380 390 400 410 420 GHVSNGAPYP PCSGVHVRSV CVFGAGDLSW MLRQHHLFAN KFDMDVDPFA IQCLDEHLRH 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]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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

EMBL
GenBank
DDBJ

U19265 mRNA. Translation: AAA60948.1.
D87332 mRNA. Translation: BAA22998.1.
D87333 mRNA. Translation: BAA22999.1.
AK045216 mRNA. Translation: BAC32265.1.

IPI

IPI00311895.

RefSeq

NP_001129956.1. NM_001136484.1.
NP_034395.2. NM_010265.3.
NP_775618.1. NM_173442.3.

UniGene

Mm.244825.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3OTK	X-ray	2.30	A/B/C/D	38-428	[»]

ProteinModelPortal

Q09324.

SMR

Q09324. Positions 56-424.

ModBase

Search...

Protein-protein interaction databases

STRING

Q09324.

Protein family/group databases

CAZy

GT14. Glycosyltransferase Family 14.

PTM databases

PhosphoSite

Q09324.

Proteomic databases

PRIDE

Q09324.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000067276; ENSMUSP00000069023; ENSMUSG00000038843.
ENSMUST00000168606; ENSMUSP00000129033; ENSMUSG00000038843.
ENSMUST00000169897; ENSMUSP00000127835; ENSMUSG00000038843.

GeneID

14537.

KEGG

mmu:14537.

Organism-specific databases

CTD

2650.

MGI

MGI:95676. Gcnt1.

Phylogenomic databases

eggNOG

maNOG06661.

GeneTree

ENSGT00550000074330.

HOGENOM

HBG446687.

HOVERGEN

HBG051711.

InParanoid

Q09324.

OrthoDB

EOG4W0XDC.

Gene expression databases

ArrayExpress

Q09324.

Bgee

Q09324.

CleanEx

MM_GCNT1.

Genevestigator

Q09324.

GermOnline

ENSMUSG00000038843. Mus musculus.

Family and domain databases

InterPro

IPR003406. Glyco_trans_14.
[Graphical view]

KO

K00727.

Pfam

PF02485. Branch. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

286198.

SOURCE

Search...

Entry information

Entry name

GCNT1_MOUSE

Accession

Primary (citable) accession number: Q09324
Secondary accession number(s): O35981, Q8BRB2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program