Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q5A4E3

Entry ID Method Resolution Chain Position Source
AF-Q5A4E3-F1 Predicted AlphaFoldDB

No variants for Q5A4E3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5A4E3

No associated diseases with Q5A4E3

1 regional properties for Q5A4E3

Type Name Position InterPro Accession
conserved_site Glycosyltransferase, DXD sugar-binding motif 117 - 206 IPR007577

Functions

Description
EC Number 2.4.1.232 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type II membrane protein
  • Golgi apparatus membrane ; Single-pass type II membrane protein
  • Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
mannan polymerase complex A protein complex with alpha-(1->6)-mannosyltransferase activity, located in the cis Golgi membrane; adds mannan to N-linked glycans on proteins.

2 GO annotations of molecular function

Name Definition
alpha-1,6-mannosyltransferase activity Catalysis of the transfer of a mannose residue to an oligosaccharide, forming an alpha-(1->6) linkage.
glycolipid 1,6-alpha-mannosyltransferase activity Catalysis of the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-mannose linkage.

6 GO annotations of biological process

Name Definition
cellular response to heat Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
cellular response to starvation Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of nourishment.
filamentous growth The process in which a multicellular organism, a unicellular organism or a group of unicellular organisms grow in a threadlike, filamentous shape.
filamentous growth of a population of unicellular organisms in response to starvation The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to deprivation of nourishment.
N-glycan processing The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLQLREPQMV HKHLKLAVLG IVVIFTTYFI ISSLSSPTST HKTEYNSPKL QLAKELELNS
70 80 90 100 110 120
NWKELGLNFQ PNKKYSLPDE STLRQQLSYQ FPYDESKPFP KNIWQTWKVG IDEKSFPKRY
130 140 150 160 170 180
LKYQQTWEDK NPDYKHYVVP DKQCDLLIEQ LYSQVPDVAK AYRIMPKSIL KADFFRYLIL
190 200 210 220 230 240
FARGGVYTDI DTVGLKPVDE WISNSEMILE KKNRSGLVVG IEADPDRPDW ADWYARRIQF
250 260 270 280 290 300
CQWTIQSKRG HPMLRELIAK ITDITLTRHK KGQLKKVLGK NEGGDIMNWT GPGIFTDTVF
310 320 330 340 350 360
EYMNNILQSP EVFKNKKKWA TIIDWKLFTG MEQPIAIDDV LVLPITSFSP DVNQMGAKDS
370 380
HDPMAYAKHM FSGSWKDDGM PEMEQ