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 O62725

Entry ID Method Resolution Chain Position Source
AF-O62725-F1 Predicted AlphaFoldDB

No variants for O62725

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O62725

No associated diseases with O62725

1 regional properties for O62725

Type Name Position InterPro Accession
domain EGF-like domain 17 - 55 IPR000742

Functions

Description
EC Number 1.14.99.1 Miscellaneous
Subcellular Localization
  • Microsome membrane ; Peripheral membrane protein
  • Endoplasmic reticulum membrane ; Peripheral membrane protein
  • Nucleus inner membrane ; Peripheral membrane protein
  • Nucleus outer membrane ; Peripheral membrane protein
  • Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope
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.
nuclear inner membrane The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
nuclear outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the nuclear envelope; continuous with the endoplasmic reticulum of the cell and sometimes studded with ribosomes.

5 GO annotations of molecular function

Name Definition
dioxygenase activity Catalysis of an oxidation-reduction (redox) reaction in which both atoms of oxygen from one molecule of O2 are incorporated into the (reduced) product(s) of the reaction. The two atoms of oxygen may be distributed between two different products. [DOI:10.1016/S0040-4020(03)00944-X, GOC:bf]
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
peroxidase activity Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O.
prostaglandin-endoperoxide synthase activity Catalysis of the reaction: arachidonate + donor-H2 + 2 O2 = prostaglandin H2 + acceptor + H2O.

6 GO annotations of biological process

Name Definition
cyclooxygenase pathway The chemical reactions and pathways by which prostaglandins are formed from arachidonic acid, and in which prostaglandin-endoperoxide synthase (cyclooxygenase) catalyzes the committed step in the conversion of arachidonic acid to the prostaglandin-endoperoxides PGG2 and PGH2.
inflammatory response The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
prostaglandin biosynthetic process The chemical reactions and pathways resulting in the formation of prostaglandins, any of a group of biologically active metabolites which contain a cyclopentane ring.
regulation of blood pressure Any process that modulates the force with which blood travels through the circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
regulation of neuroinflammatory response Any process that modulates the frequency, rate or extent of neuroinflammatory response.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLARAGLLCA SLSPPHAANP CCSNPCQNQG VCMSIGFDQY MCDCSRTGFY GENCSTPEFL
70 80 90 100 110 120
TRVKLLLKPT PNTVHYILTH FKGVWNIVNK IPFLADVIMK YVRTSRSHCI EPPPTYNVHY
130 140 150 160 170 180
AYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGKKELPDS KEIVEKFLLR RKFIPDPQGT
190 200 210 220 230 240
NMMFAFFAQH FTHQFFKTDH KRGPGFTKGL GHGVDLSHVY GETLDRQHKL RLFKDGKMKY
250 260 270 280 290 300
QVIDGEVYPP TVKDTQVEMI YPPHVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
310 320 330 340 350 360
VLKQEQGEWD DERLFRRSRL ILIGETIKIV IEDYVRHLSG YHFSLKFDPE LLFNQQFQYQ
370 380 390 400 410 420
NRIAAEFNTL YHWHPLLPDT LQIDDQEYNF QQFVYNNSIL LEHGLTQFGE SFSRQIAGRV
430 440 450 460 470 480
AGGRNVPAAV QQEQRASIDQ SRQMKYQSLN EYRKRFSVKP YASFEELTGE KEMAGELKAL
490 500 510 520 530 540
YQDIDAMELY PALLVEKPRP DAIFGETMVE IGAPFSLKGL MGNPICSPDY WKPSHFGGEV
550 560 570 580 590 600
GFKIINTASI QSLICNNVKG CPFTAFSVQD PQLTKTVTIN GSSSHSGLDD INPTVLLKER
STEL