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 Q8HZR1

Entry ID Method Resolution Chain Position Source
AF-Q8HZR1-F1 Predicted AlphaFoldDB

4 variants for Q8HZR1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs24619391 17 L>M No EVA
rs853183608 57 R>H No EVA
rs852291113 597 E>Q No EVA
rs850883934 598 R>Q No EVA

No associated diseases with Q8HZR1

1 regional properties for Q8HZR1

Type Name Position InterPro Accession
domain EGF-like domain 35 - 73 IPR000742

Functions

Description
EC Number 1.14.99.1 Miscellaneous
Subcellular Localization
  • Microsome membrane ; Peripheral membrane protein
  • Endoplasmic reticulum membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.

5 GO annotations of molecular function

Name Definition
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.
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.
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.

4 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.
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.
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.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O62664 PTGS1 Prostaglandin G/H synthase 1 Bos taurus (Bovine) PR
P23219 PTGS1 Prostaglandin G/H synthase 1 Homo sapiens (Human) PR
P35354 PTGS2 Prostaglandin G/H synthase 2 Homo sapiens (Human) PR
P22437 Ptgs1 Prostaglandin G/H synthase 1 Mus musculus (Mouse) PR
Q05769 Ptgs2 Prostaglandin G/H synthase 2 Mus musculus (Mouse) PR
Q9C9U3 DOX2 Alpha-dioxygenase 2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSRGSRLHRW PLLLLLLLLL PPPPVLPAEA RTPAPVNPCC YYPCQHQGIC VRFGLDRYQC
70 80 90 100 110 120
DCTRTGYSGP NCTIPELWTW LRNSLRPSPS FLHFLLTHGR WFWEFINATF IRDMLMRLVL
130 140 150 160 170 180
TARSNLIPSP PTYNIAHDYI SWESFSNVSY YTRVLPSVPQ DCPTPMGTKG KKQLPDAQLL
190 200 210 220 230 240
GRRFLLRRKF IPDPQGTNLM FAFFAQHFTH QFFKTSGKMG PGFTKALGHG VDLGHIYGDN
250 260 270 280 290 300
LDRQYQLRLF KDGKLKYQVL DGEMYPPSVE EAPVLMHYPR GILPQSQMAV GQEVFGLLPG
310 320 330 340 350 360
LMLYATLWLR EHNRVCDLLK AEHPTWGDEQ LFQTARLILI GETIKIVIEE YVQQLSGYFL
370 380 390 400 410 420
QLKFDPELLF SAQFQYRNRI AMEFNQLYHW HPLMPDSFWV GSQEYSYEQF LFNTSMLTHY
430 440 450 460 470 480
GIEALVDAFS RQSAGRIGGG RNIDHHVLHV AVETIKESRE LRLQPFNEYR KRFGMRPYMS
490 500 510 520 530 540
FQELTGEKEM AAELEELYGD IDALEFYPGL LLEKCHPNSI FGESMIEIGA PFSLKGLLGN
550 560 570 580 590 600
PICSPEYWKP STFGGEMGFN MVKTATLKKL VCLNTKTCPY VSFRVPDPHQ DGGPGVERPS
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