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 Q9YI25

Entry ID Method Resolution Chain Position Source
AF-Q9YI25-F1 Predicted AlphaFoldDB

No variants for Q9YI25

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9YI25

No associated diseases with Q9YI25

1 regional properties for Q9YI25

Type Name Position InterPro Accession
domain Ribosome control protein 1 734 - 986 IPR009771

Functions

Description
EC Number 3.1.1.64 Carboxylic ester hydrolases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Lipid-anchor
  • Microsome membrane
  • Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

8 GO annotations of molecular function

Name Definition
all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity Catalysis of the reaction: H(2)O + all-trans-retinyl ester = 11-cis-retinol + fatty acid.
all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity Catalysis of the reaction: H(2)O + all-trans-retinyl palmitate = 11-cis-retinol + H(+) + palmitate.
cardiolipin binding Binding to cardiolipin.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from one donor, and two oxygen atoms is incorporated into a donor.
phosphatidylcholine binding Binding to a phosphatidylcholine, a glycophospholipid in which a phosphatidyl group is esterified to the hydroxyl group of choline.
phosphatidylserine binding Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.

4 GO annotations of biological process

Name Definition
response to 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. The process begins with detection of the stimulus and ends with a change in state or activity or the cell or organism.
retinoid metabolic process The chemical reactions and pathways involving retinoids, any member of a class of isoprenoids that contain or are derived from four prenyl groups linked head-to-tail. Retinoids include retinol and retinal and structurally similar natural derivatives or synthetic compounds, but need not have vitamin A activity.
visual perception The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
zeaxanthin biosynthetic process The chemical reactions and pathways resulting in the formation of zeaxanthin.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTNRVDHPAG GYKKLFESTE ELVAPVTAQV TGRIPVWLSG SLLRCGPGLF EVGSEQFYHL
70 80 90 100 110 120
FDGQALLHKF EFKGGHVIYH RRFIRTDTYV RAMTEKRIVI TEFGTFAFPD PCKNIFSRFL
130 140 150 160 170 180
SYFQGLEVTD NALVNVYPVG EDYYACTETN YITKINPETL ETVKKVDLCN YVSINGVTAH
190 200 210 220 230 240
PHIEHDGTVY NIGNCFGKHF AFAYNIVKIP PLQADKEDPI NKAKVVVQFP CSERFKPSYV
250 260 270 280 290 300
HSFGLTPNYI VFVEQPVKIN LFKFLSSWSI WGANYMDCFE SHETMGVWMH VAEKHTGEYL
310 320 330 340 350 360
NIKYRTSAFN LFHHINTYED HGFLIVDLCC WKGFEFVYNY LYLANLRENW EEVKRSAEKP
370 380 390 400 410 420
PQPEVRRYVL PLDIHKVDTG KNLVNLPYTT ATAVLRSDET IWLEPEVLFS GPRQAFEFPQ
430 440 450 460 470 480
INYKKHGGKD YTYAYGVGLN HFVPDRLSKL NVKTKETWVW QEPDTYPSEP IFVSQPDAIE
490 500 510 520 530
EDDGVVLSVV ISPGEGQKPA FLLILNAKDM SEIARAEVDS NIPVTFHGMF KKA