P27115 (MGAT1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
EC=2.4.1.101

Alternative name(s):
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
Short name=GNT-I
Short name=GlcNAc-T I

Gene names

Name:	MGAT1
Synonyms:	GNT1

Organism

Oryctolagus cuniculus (Rabbit) [Reference proteome]

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Catalytic activity	UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.
Cofactor	Manganese. The cofactor is mostly bound to the substrate. Ref.3
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein.
Tissue specificity	Appears to be present in all tissues.
Sequence similarities	Belongs to the glycosyltransferase 13 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mannose metabolic process Inferred from direct assay PubMed 1447191. Source: UniProtKB protein N-linked glycosylation Inferred from direct assay PubMed 1447191. Source: UniProtKB
Cellular_component	Golgi medial cisterna Inferred from direct assay PubMed 1447191. Source: UniProtKB Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein N-acetylglucosaminyltransferase activity Inferred from direct assay PubMed 1447191. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 447

447

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

PRO_0000191387

Regions

Topological domain

1 – 6

6

Cytoplasmic Potential

Transmembrane

7 – 29

23

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

Topological domain

30 – 447

418

Lumenal Potential

Sites

Active site

291

1

Proton acceptor Potential

Metal binding

213

1

Manganese

Binding site

117

1

Substrate

Binding site

144

1

Substrate

Binding site

190

1

Substrate

Binding site

212

1

Substrate

Binding site

322

1

Substrate

Amino acid modifications

Disulfide bond

115 ↔ 145

Ref.2 Ref.3

Disulfide bond

239 ↔ 305

Ref.2 Ref.3

Secondary structure

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447

Helix Strand Turn

Details...

Beta strand

110 – 116

7

Helix

120 – 130

11

Turn

134 – 136

3

Beta strand

139 – 143

5

Helix

148 – 155

8

Helix

156 – 160

5

Beta strand

161 – 165

5

Helix

179 – 181

3

Helix

182 – 199

18

Beta strand

205 – 211

7

Beta strand

214 – 216

3

Helix

220 – 233

14

Beta strand

237 – 242

6

Helix

249 – 251

3

Beta strand

260 – 265

6

Beta strand

269 – 274

6

Helix

275 – 281

7

Helix

282 – 284

3

Helix

290 – 294

5

Helix

297 – 300

4

Beta strand

304 – 315

12

Beta strand

318 – 322

5

Helix

325 – 329

5

Helix

331 – 333

3

Helix

343 – 345

3

Helix

349 – 351

3

Helix

353 – 366

14

Helix

372 – 376

5

Beta strand

384 – 389

6

Helix

393 – 402

10

Beta strand

421 – 426

6

Beta strand

429 – 434

6

Sequences

	Sequence		Length	Mass (Da)
	P27115 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 18AC90994F0EB435	FASTA	447	51,540
	10 20 30 40 50 60 MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPVPSRLPSD NALDDDPASL TREVIRLAQD 70 80 90 100 110 120 AEVELERQRG LLQQIREHHA LWSQRWKVPT AAPPAQPHVP VTPPPAVIPI LVIACDRSTV 130 140 150 160 170 180 RRCLDKLLHY RPSAELFPII VSQDCGHEET AQVIASYGSA VTHIRQPDLS NIAVQPDHRK 190 200 210 220 230 240 FQGYYKIARH YRWALGQIFH NFNYPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV 250 260 270 280 290 300 SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLAELWAE LEPKWPKAFW DDWMRRPEQR 310 320 330 340 350 360 KGRACVRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQQEAYDRDF 370 380 390 400 410 420 LARVYGAPQL QVEKVRTNDR KELGEVRVQY TGRDSFKAFA KALGVMDDLK SGVPRAGYRG 430 440 IVTFLFRGRR VHLAPPQTWD GYDPSWT

References

[1]	"Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans: UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I." Sarkar M., Hull E., Nishikawa Y., Simpson R.J., Moritz R.L., Dunn R., Schachter H. Proc. Natl. Acad. Sci. U.S.A. 88:234-238(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT I) in complex with donor substrate analogues." Gordon R.D., Sivarajah P., Satkunarajah M., Ma D., Tarling C.A., Vizitiu D., Withers S.G., Rini J.M. J. Mol. Biol. 360:67-79(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 106-447 IN COMPLEX WITH SUBSTRATE ANALOGS, MANGANESE-BINDING SITE, DISULFIDE BONDS.
[3]	"X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily." Unligil U.M., Zhou S., Yuwaraj S., Sarkar M., Schachter H., Rini J.M. EMBO J. 19:5269-5280(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 106-447 ALONE AND IN COMPLEX WITH UDP-GLCNAC, ACTIVE SITE, COFACTOR, MANGANESE-BINDING SITE, SUBSTRATE-BINDING SITES, DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57301 mRNA. Translation: AAA31493.1.

PIR

A38561.

RefSeq

NP_001076214.1. NM_001082745.1.

UniGene

Ocu.1975.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FO8	X-ray	1.40	A	106-447	[»]
1FO9	X-ray	1.50	A	106-447	[»]
1FOA	X-ray	1.80	A	106-447	[»]
2AM3	X-ray	1.80	A	106-447	[»]
2AM4	X-ray	1.70	A	106-447	[»]
2AM5	X-ray	1.60	A	106-447	[»]
2APC	X-ray	1.50	A	106-447	[»]

ProteinModelPortal

P27115.

SMR

P27115. Positions 106-447.

ModBase

Search...

Protein family/group databases

CAZy

GT13. Glycosyltransferase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

100009521.

Organism-specific databases

CTD

100009521.

Phylogenomic databases

HOVERGEN

HBG052466.

Enzyme and pathway databases

UniPathway

UPA00378.

Family and domain databases

InterPro

IPR004139. Glyco_trans_13.
[Graphical view]

PANTHER

PTHR10468. PTHR10468. 1 hit.

Pfam

PF03071. GNT-I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27115.

Entry information

Entry name

MGAT1_RABIT

Accession

Primary (citable) accession number: P27115

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program