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 P97872

Entry ID Method Resolution Chain Position Source
AF-P97872-F1 Predicted AlphaFoldDB

22 variants for P97872

Variant ID(s) Position Change Description Diseaes Association Provenance
rs37557226 47 A>T No EVA
rs232178366 82 Y>F No EVA
rs3388651186 90 E>* No EVA
rs3388638395 98 E>D No EVA
rs3388654944 109 T>I No EVA
rs3388643934 130 T>I No EVA
rs1134264990 155 H>L No EVA
rs3388654075 170 K>E No EVA
rs3388647614 178 K>M No EVA
rs36298704 181 V>M No EVA
rs214803069 209 K>M No EVA
rs3388649493 231 P>L No EVA
rs237794467 234 L>M No EVA
rs3388654996 255 N>S No EVA
rs36785610 313 V>I No EVA
rs3388654119 326 V>I No EVA
rs3388644014 354 K>Q No EVA
rs3388651213 394 K>Q No EVA
rs3388649504 414 E>K No EVA
rs242145991 458 R>K No EVA
rs3388647671 469 T>A No EVA
rs3388654973 532 Y>C No EVA

No associated diseases with P97872

No regional properties for P97872

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P97872

Functions

Description
EC Number 1.6.3.1 With oxygen as acceptor
Subcellular Localization
  • Microsome membrane
  • Endoplasmic reticulum membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
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).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

6 GO annotations of molecular function

Name Definition
aldehyde oxidase activity Catalysis of the reaction: an aldehyde + H2O + O2 = a carboxylic acid + hydrogen peroxide.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
N,N-dimethylaniline monooxygenase activity Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
NADP binding Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
NADPH oxidase H202-forming activity Catalysis of the reaction: NADPH + H+ + O2 = NADP + hydrogen peroxide (H2O2).

4 GO annotations of biological process

Name Definition
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
NADPH oxidation A metabolic process that results in the oxidation of reduced nicotinamide adenine dinucleotide, NADPH, to the oxidized form, NADP.
regulation of cholesterol metabolic process Any process that modulates the rate, frequency, or extent of cholesterol metabolism, the chemical reactions and pathways involving cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
xenobiotic metabolic process The chemical reactions and pathways involving a xenobiotic compound, 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.

12 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P31512 FMO4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Homo sapiens (Human) PR
P49326 FMO5 Flavin-containing monooxygenase 5 Homo sapiens (Human) PR
P97501 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Mus musculus (Mouse) PR
Q8K2I3 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Mus musculus (Mouse) PR
Q8VHG0 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Mus musculus (Mouse) PR
Q8K4B7 Fmo4 Dimethylaniline monooxygenase [N-oxide-forming] 4 Rattus norvegicus (Rat) PR
Q6IRI9 Fmo2 Dimethylaniline monooxygenase [N-oxide-forming] 2 Rattus norvegicus (Rat) PR
Q9EQ76 Fmo3 Dimethylaniline monooxygenase [N-oxide-forming] 3 Rattus norvegicus (Rat) PR
Q8K4C0 Fmo5 Flavin-containing monooxygenase 5 Rattus norvegicus (Rat) PR
Q9SVU0 YUC8 Probable indole-3-pyruvate monooxygenase YUCCA8 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SXD9 At1g62580 Flavin-containing monooxygenase FMO GS-OX-like 7 Arabidopsis thaliana (Mouse-ear cress) PR
Q9C8T8 At1g63340 Putative flavin-containing monooxygenase FMO GS-OX-like 10 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAKKRIAVIG AGASGLTCIK CCLEEGLEPV CFERSGDIGG LWRFQEAPEE GRASIYQSVV
70 80 90 100 110 120
INTSKEMMCF SDYPIPDHYP NYMHNSQVLE YFRMYAKEFD LLKYIQFKTT VCSVKKQPDF
130 140 150 160 170 180
STSGQWQVVT ECEGKQQVDV FDGVLVCTGH HTDAHLPLES FPGIEKFKGK YFHSRDYKNP
190 200 210 220 230 240
VEFTGKRVIV IGIGNSGGDL AVEISHTAKQ VFLSTRRGAW ILNRVGKHGY PIDLLLSSRI
250 260 270 280 290 300
MYYLSRICGP SLKNNYMEKQ MNQRFDHEMF GLKPKHRALS QHPTVNDDLP NRIIAGLVKV
310 320 330 340 350 360
KGNVKEFTET AAVFEDGSRE DGIDVVIFAT GYSFAFPFLE DSVKVVKNKV SLYKKVFPPN
370 380 390 400 410 420
LEKPTLAIIG LIQPLGAIMP ISELQGRWAT QVFKGLKKLP SQSEMMAEIN KAREEMAKRY
430 440 450 460 470 480
VDSQRHTIQG DYIDTMEEIA DLVGVRPNIL PLVFTDPRLA LRLLLGPCTP VQYRLQGPGK
490 500 510 520 530
WAGARKTILT TEDRVRKPLM TRVVERDSSG GSLVTVRVLM LAVAFFAVIL AYF