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Protein

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

Gene

MGAT1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.

Catalytic activityi

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.

Cofactori

Mn2+1 PublicationNote: The cofactor is mostly bound to the substrate.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei117Substrate1
Binding sitei144Substrate1
Binding sitei190Substrate1
Binding sitei212Substrate1
Metal bindingi213Manganese1
Active sitei291Proton acceptorSequence analysis1
Binding sitei322Substrate1

GO - Molecular functioni

GO - Biological processi

  • mannose metabolic process Source: UniProtKB
  • protein N-linked glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.101. 1749.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

Names & Taxonomyi

Protein namesi
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 namesi
Name:MGAT1
Synonyms:GNT1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 447LumenalSequence analysisAdd BLAST418

GO - Cellular componenti

  • Golgi medial cisterna Source: UniProtKB
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001913871 – 447Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferaseAdd BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi115 ↔ 145
Disulfide bondi239 ↔ 305

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP27115.

Expressioni

Tissue specificityi

Appears to be present in all tissues.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi110 – 116Combined sources7
Helixi120 – 130Combined sources11
Turni134 – 136Combined sources3
Beta strandi139 – 143Combined sources5
Helixi148 – 155Combined sources8
Helixi156 – 160Combined sources5
Beta strandi161 – 165Combined sources5
Helixi179 – 181Combined sources3
Helixi182 – 199Combined sources18
Beta strandi205 – 211Combined sources7
Beta strandi214 – 216Combined sources3
Helixi220 – 233Combined sources14
Beta strandi237 – 242Combined sources6
Helixi249 – 251Combined sources3
Beta strandi260 – 265Combined sources6
Beta strandi269 – 274Combined sources6
Helixi275 – 281Combined sources7
Helixi282 – 284Combined sources3
Helixi290 – 294Combined sources5
Helixi297 – 300Combined sources4
Beta strandi304 – 315Combined sources12
Beta strandi318 – 322Combined sources5
Helixi325 – 329Combined sources5
Helixi331 – 333Combined sources3
Helixi343 – 345Combined sources3
Helixi349 – 351Combined sources3
Helixi353 – 366Combined sources14
Helixi372 – 376Combined sources5
Beta strandi384 – 389Combined sources6
Helixi393 – 402Combined sources10
Beta strandi421 – 426Combined sources6
Beta strandi429 – 434Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FO8X-ray1.40A106-447[»]
1FO9X-ray1.50A106-447[»]
1FOAX-ray1.80A106-447[»]
2AM3X-ray1.80A106-447[»]
2AM4X-ray1.70A106-447[»]
2AM5X-ray1.60A106-447[»]
2APCX-ray1.50A106-447[»]
ProteinModelPortaliP27115.
SMRiP27115.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27115.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052466.
InParanoidiP27115.
KOiK00726.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P27115-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPVPSRLPSD NALDDDPASL
60 70 80 90 100
TREVIRLAQD AEVELERQRG LLQQIREHHA LWSQRWKVPT AAPPAQPHVP
110 120 130 140 150
VTPPPAVIPI LVIACDRSTV RRCLDKLLHY RPSAELFPII VSQDCGHEET
160 170 180 190 200
AQVIASYGSA VTHIRQPDLS NIAVQPDHRK FQGYYKIARH YRWALGQIFH
210 220 230 240 250
NFNYPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV SAWNDNGKEQ
260 270 280 290 300
MVDSSKPELL YRTDFFPGLG WLLLAELWAE LEPKWPKAFW DDWMRRPEQR
310 320 330 340 350
KGRACVRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY
360 370 380 390 400
LQQEAYDRDF LARVYGAPQL QVEKVRTNDR KELGEVRVQY TGRDSFKAFA
410 420 430 440
KALGVMDDLK SGVPRAGYRG IVTFLFRGRR VHLAPPQTWD GYDPSWT
Length:447
Mass (Da):51,540
Last modified:August 1, 1992 - v1
Checksum:i18AC90994F0EB435
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57301 mRNA. Translation: AAA31493.1.
PIRiA38561.
RefSeqiNP_001076214.1. NM_001082745.1.
UniGeneiOcu.1975.

Genome annotation databases

GeneIDi100009521.
KEGGiocu:100009521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57301 mRNA. Translation: AAA31493.1.
PIRiA38561.
RefSeqiNP_001076214.1. NM_001082745.1.
UniGeneiOcu.1975.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FO8X-ray1.40A106-447[»]
1FO9X-ray1.50A106-447[»]
1FOAX-ray1.80A106-447[»]
2AM3X-ray1.80A106-447[»]
2AM4X-ray1.70A106-447[»]
2AM5X-ray1.60A106-447[»]
2APCX-ray1.50A106-447[»]
ProteinModelPortaliP27115.
SMRiP27115.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

Proteomic databases

PRIDEiP27115.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009521.
KEGGiocu:100009521.

Organism-specific databases

CTDi4245.

Phylogenomic databases

HOVERGENiHBG052466.
InParanoidiP27115.
KOiK00726.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.101. 1749.

Miscellaneous databases

EvolutionaryTraceiP27115.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMGAT1_RABIT
AccessioniPrimary (citable) accession number: P27115
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.