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P27115

- MGAT1_RABIT

UniProt

P27115 - MGAT1_RABIT

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Protein

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

Gene

MGAT1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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

Manganese. The cofactor is mostly bound to the substrate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei117 – 1171Substrate
Binding sitei144 – 1441Substrate
Binding sitei190 – 1901Substrate
Binding sitei212 – 2121Substrate
Metal bindingi213 – 2131Manganese
Active sitei291 – 2911Proton acceptorSequence Analysis
Binding sitei322 – 3221Substrate

GO - Molecular functioni

  1. alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. protein N-acetylglucosaminyltransferase activity Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

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
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000191387Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 145
Disulfide bondi239 ↔ 305

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Appears to be present in all tissues.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi110 – 1167
Helixi120 – 13011
Turni134 – 1363
Beta strandi139 – 1435
Helixi148 – 1558
Helixi156 – 1605
Beta strandi161 – 1655
Helixi179 – 1813
Helixi182 – 19918
Beta strandi205 – 2117
Beta strandi214 – 2163
Helixi220 – 23314
Beta strandi237 – 2426
Helixi249 – 2513
Beta strandi260 – 2656
Beta strandi269 – 2746
Helixi275 – 2817
Helixi282 – 2843
Helixi290 – 2945
Helixi297 – 3004
Beta strandi304 – 31512
Beta strandi318 – 3225
Helixi325 – 3295
Helixi331 – 3333
Helixi343 – 3453
Helixi349 – 3513
Helixi353 – 36614
Helixi372 – 3765
Beta strandi384 – 3896
Helixi393 – 40210
Beta strandi421 – 4266
Beta strandi429 – 4346

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 106-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27115.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini30 – 447418LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG052466.
InParanoidiP27115.

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:
EMBL
GenBank
DDBJ
Links Updated
M57301 mRNA. Translation: AAA31493.1.
PIRiA38561.
RefSeqiNP_001076214.1. NM_001082745.1.
UniGeneiOcu.1975.

Genome annotation databases

GeneIDi100009521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57301 mRNA. Translation: AAA31493.1 .
PIRi A38561.
RefSeqi NP_001076214.1. NM_001082745.1.
UniGenei Ocu.1975.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P27115.
SMRi P27115. Positions 106-447.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT13. Glycosyltransferase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009521.

Organism-specific databases

CTDi 4245.

Phylogenomic databases

HOVERGENi HBG052466.
InParanoidi P27115.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

EvolutionaryTracei P27115.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10468. PTHR10468. 1 hit.
Pfami PF03071. GNT-I. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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: October 29, 2014
This is version 100 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

External Data

Dasty 3