P27115

PR
Gene name
MGAT1 (GNT1)
Protein name
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Names
CD62 antigen-like family member E, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I, GNT-I, GlcNAc-T I
Species
Oryctolagus cuniculus (Rabbit)
KEGG Pathway
ocu:100009521
EC number
2.4.1.101: Hexosyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

7-136 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

8 structures for P27115

Entry ID Method Resolution Chain Position Source
1FO8 X-ray 140 A A 106-447 PDB
1FO9 X-ray 150 A A 106-447 PDB
1FOA X-ray 180 A A 106-447 PDB
2AM3 X-ray 180 A A 106-447 PDB
2AM4 X-ray 170 A A 106-447 PDB
2AM5 X-ray 160 A A 106-447 PDB
2APC X-ray 150 A A 106-447 PDB
AF-P27115-F1 Predicted AlphaFoldDB

No variants for P27115

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P27115

No associated diseases with P27115

2 regional properties for P27115

Type Name Position InterPro Accession
domain Mannitol dehydrogenase, C-terminal 162 - 375 IPR013118
domain Mannitol dehydrogenase, N-terminal 11 - 132 IPR013131

Functions

Description
EC Number 2.4.1.101 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
  • Cytoplasm, perinuclear region
  • Co-localizes with BRI3 at the perinuclear region
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
Golgi medial cisterna The middle Golgi cisterna (or cisternae).
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

3 GO annotations of molecular function

Name Definition
alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2--alpha-D-mannosyl)-beta-D-mannosyl-R + H(+) + UDP.
manganese ion binding Binding to a manganese ion (Mn).
protein N-acetylglucosaminyltransferase activity Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + protein = UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein.

5 GO annotations of biological process

Name Definition
in utero embryonic development The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
mannose metabolic process The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. The D-(+)-form is widely distributed in mannans and hemicelluloses and is of major importance in the core oligosaccharide of N-linked oligosaccharides of glycoproteins.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
protein N-linked glycosylation via asparagine The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
UDP-N-acetylglucosamine catabolic process The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
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