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

5 structures for Q6CUC3

Entry ID Method Resolution Chain Position Source
5H54 X-ray 310 A A 1-239 PDB
5H55 X-ray 350 A A 1-305 PDB
5H5A X-ray 226 A A/B/C/D 1-239 PDB
5H5C X-ray 331 A A 1-239 PDB
AF-Q6CUC3-F1 Predicted AlphaFoldDB

No variants for Q6CUC3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CUC3

No associated diseases with Q6CUC3

No regional properties for Q6CUC3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q6CUC3

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion outer membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions
  • These foci are often found next to mtDNA nucleoids
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
ERMES complex A protein complex that links the endoplasmic reticulum with mitochondria and may have a role in promoting exchange of calcium and phospholipids between the two organelles.

4 GO annotations of molecular function

Name Definition
lipid transfer activity Removes a lipid from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. This results in intermembrane transfer of lipids.
phosphatidylcholine binding Binding to a phosphatidylcholine, a glycophospholipid in which a phosphatidyl group is esterified to the hydroxyl group of choline.
phosphatidylethanolamine binding Binding to a phosphatidylethanolamine, a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine.
phosphatidylglycerol binding Binding to phosphatidylglycerol.

6 GO annotations of biological process

Name Definition
aminophospholipid transport The directed movement of aminophospholipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Aminophospholipids contain phosphoric acid as a mono- or diester and an amino (NH2) group.
mitochondrial genome maintenance The maintenance of the structure and integrity of the mitochondrial genome; includes replication and segregation of the mitochondrial chromosome.
mitochondrial outer membrane translocase complex assembly The aggregation, arrangement and bonding together of a set of components to form a mitochondrial outer membrane translocase complex.
mitochondrion inheritance The distribution of mitochondria, including the mitochondrial genome, into daughter cells after mitosis or meiosis, mediated by interactions between mitochondria and the cytoskeleton.
mitochondrion-endoplasmic reticulum membrane tethering The attachment of a mitochondrion and an endoplasmic reticulum via molecular tethers that physically bridge their respective membranes and attach them to each other. The tethering may facilitate exchange of metabolites between the organelles.
protein insertion into mitochondrial outer membrane The process comprising the insertion of proteins from outside the organelle into the mitochondrial outer membrane, mediated by large outer membrane translocase complexes.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSVEIDWDNI RGDLSVNQGV KDFLNSRLQE FELPSYVNNL KVTNFDLGTM PPNVILKQMD
70 80 90 100 110 120
DPLDEFYSYL LQEGDISKEA AKDKNTDVQL LVELDYKGDM SIELSADLVL NYPSPQFMIL
130 140 150 160 170 180
PVKLRISDIG MHCLCLLAYL KKQLFISFLC DVSDPLLEND KLQVDPSGPN FMGKRALERI
190 200 210 220 230 240
SLIRNIKIHT ELGQLDQGEG SVLRSVGKLE EFLVDLFRNL IRKEAAWPSW IDLDFTPEDP
250 260 270 280 290 300
EDPEEEGREN DLVADSSNDG KDIEMKSGTE ETLGAGIQES VQHVSPAVTS IDQESRVNSN
TSLEE