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 O08807

Entry ID Method Resolution Chain Position Source
3VWU X-ray 330 A A/B/C/D/E/F/G/H/I/J 41-274 PDB
3VWV X-ray 180 A A/B 87-274 PDB
3W8J X-ray 210 A C/D 244-263 PDB
3WGX X-ray 092 A C/D 244-263 PDB
AF-O08807-F1 Predicted AlphaFoldDB

13 variants for O08807

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389548639 72 V>D No EVA
rs3410981140 135 G>I No EVA
rs3389584482 166 P>L No EVA
rs3389588208 171 G>V No EVA
rs3389574122 184 N>S No EVA
rs13470613 211 K>N No EVA
rs3412526769 213 V>G No EVA
rs3389548560 215 R>K No EVA
rs3411985170 220 N>T No EVA
rs3412406506 224 V>D No EVA
rs3389584532 235 V>I No EVA
rs3389592925 246 E>D No EVA
rs3412526790 246 E>G No EVA

No associated diseases with O08807

3 regional properties for O08807

Type Name Position InterPro Accession
domain Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant 84 - 216 IPR000866
domain Thioredoxin domain 82 - 240 IPR013766
domain Peroxiredoxin, C-terminal 237 - 264 IPR019479

Functions

Description
EC Number 1.11.1.24 Peroxidases
Subcellular Localization
  • Cytoplasm
  • Endoplasmic reticulum
  • Not secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
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.
smooth endoplasmic reticulum The smooth endoplasmic reticulum (smooth ER or SER) has no ribosomes attached to it. The smooth ER is the recipient of the proteins synthesized in the rough ER. Those proteins to be exported are passed to the Golgi complex, the resident proteins are returned to the rough ER and the lysosomal proteins after phosphorylation of their mannose residues are passed to the lysosomes. Glycosylation of the glycoproteins also continues. The smooth ER is the site of synthesis of lipids, including the phospholipids. The membranes of the smooth ER also contain enzymes that catalyze a series of reactions to detoxify both lipid-soluble drugs and harmful products of metabolism. Large quantities of certain compounds such as phenobarbital cause an increase in the amount of the smooth ER.

3 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
molecular sequestering activity Binding to a specific molecule to prevent it from interacting with other partners or to inhibit its localization to the area of the cell or complex where it is active.
thioredoxin-dependent peroxiredoxin activity Catalysis of the reaction:

9 GO annotations of biological process

Name Definition
cell redox homeostasis Any process that maintains the redox environment of a cell or compartment within a cell.
extracellular matrix organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
male gonad development The process whose specific outcome is the progression of the male gonad over time, from its formation to the mature structure.
negative regulation of male germ cell proliferation Any process that stops, prevents or reduces the frequency, rate or extent of male germ cell proliferation.
peptidyl-proline hydroxylation to 4-hydroxy-L-proline The modification of peptidyl-proline to form 4-hydroxy-L-proline; catalyzed by procollagen-proline,2-oxoglutarate-4-dioxygenase.
protein maturation by protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that results in the attainment of the full functional capacity of a protein.
reactive oxygen species metabolic process The chemical reactions and pathways involving a reactive oxygen species, any molecules or ions formed by the incomplete one-electron reduction of oxygen. They contribute to the microbicidal activity of phagocytes, regulation of signal transduction and gene expression, and the oxidative damage to biopolymers.
response to oxidative stress 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
spermatogenesis The developmental process by which male germ line stem cells self renew or give rise to successive cell types resulting in the development of a spermatozoa.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR ENECHFYAGG
70 80 90 100 110 120
QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP
130 140 150 160 170 180
LDFTFVCPTE IIAFGDRIEE FKSINTEVVA CSVDSQFTHL AWINTPRRQG GLGPIRIPLL
190 200 210 220 230 240
SDLNHQISKD YGVYLEDSGH TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY
250 260 270
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN