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 Q9CR68

Entry ID Method Resolution Chain Position Source
AF-Q9CR68-F1 Predicted AlphaFoldDB

27 variants for Q9CR68

Variant ID(s) Position Change Description Diseaes Association Provenance
rs13474854 9 G>R No EVA
rs235223292 30 L>V No EVA
rs3389274301 92 R>H No EVA
rs3389274389 99 S>I No EVA
rs3389277189 107 S>I No EVA
rs3389272071 122 T>S No EVA
rs3389234348 128 A>V No EVA
rs3389268365 137 V>I No EVA
rs3389278096 139 S>R No EVA
rs3389272146 152 I>* No EVA
rs3389268314 153 E>G No EVA
rs3389268376 158 D>G No EVA
rs3404015967 161 E>* No EVA
rs3404019052 161 E>A No EVA
rs3389206216 170 R>* No EVA
rs3389272094 175 F>C No EVA
rs3389250857 183 E>D No EVA
rs3389278093 185 D>V No EVA
rs3389275312 189 A>V No EVA
rs3389250868 236 C>S No EVA
rs3389278126 237 P>L No EVA
rs3404328842 239 H>Q No EVA
rs3403577275 242 H>Q No EVA
rs3403312512 242 H>Y No EVA
rs3404193170 243 Y>C No EVA
rs3403312517 246 S>T No EVA
rs3389243547 275 G>R No EVA

No associated diseases with Q9CR68

3 regional properties for Q9CR68

Type Name Position InterPro Accession
domain ABC transporter-like, ATP-binding domain 15 - 256 IPR003439
domain AAA+ ATPase domain 39 - 249 IPR003593
conserved_site ABC transporter-like, conserved site 158 - 172 IPR017871

Functions

Description
EC Number 7.1.1.8 Hydron translocation or charge separation linked to oxidoreductase reactions
Subcellular Localization
  • Mitochondrion inner membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.
mitochondrial respiratory chain complex III A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains about 10 polypeptide subunits including four redox centers: cytochrome b/b6, cytochrome c1 and an 2Fe-2S cluster. Catalyzes the oxidation of ubiquinol by oxidized cytochrome c1.
mitochondrial respiratory chain complex IV A protein complex located in the mitochondrial inner membrane that forms part of the mitochondrial respiratory chain. Contains the 13 polypeptide subunits of cytochrome c oxidase, including cytochrome a and cytochrome a3. Catalyzes the oxidation of reduced cytochrome c by dioxygen (O2).
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
myelin sheath An electrically insulating fatty layer that surrounds the axons of many neurons. It is an outgrowth of glial cells: Schwann cells supply the myelin for peripheral neurons while oligodendrocytes supply it to those of the central nervous system.

5 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
metal ion binding Binding to a metal ion.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
protein-containing complex binding Binding to a macromolecular complex.
ubiquinol-cytochrome-c reductase activity Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: CoQH2 + 2 ferricytochrome c = CoQ + 2 ferrocytochrome c + 2 H+.

6 GO annotations of biological process

Name Definition
cellular respiration The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which either requires oxygen (aerobic respiration) or does not (anaerobic respiration).
mitochondrial electron transport, ubiquinol to cytochrome c The transfer of electrons from ubiquinol to cytochrome c that occurs during oxidative phosphorylation, mediated by the multisubunit enzyme known as complex III.
respiratory electron transport chain A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
response to antibiotic Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms.
response to hormone Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus.
response to xenobiotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLSVAARSGP FAPVLSATSR GVAGALRPLL QGAVPAASEP PVLDVKRPFL CRESLSGQAA
70 80 90 100 110 120
ARPLVATVGL NVPASVRFSH TDVKVPDFSD YRRAEVLDST KSSKESSEAR KGFSYLVTAT
130 140 150 160 170 180
TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT
190 200 210 220 230 240
KKEIDQEAAV EVSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
250 260 270
SHYDASGRIR KGPAPLNLEV PAYEFTSDDV VVVG