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 P24457

Entry ID Method Resolution Chain Position Source
AF-P24457-F1 Predicted AlphaFoldDB

70 variants for P24457

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389373535 22 L>R No EVA
rs49125063 27 H>L No EVA
rs579855692 31 H>R No EVA
rs579660523 36 C>Y No EVA
rs32438093 55 G>D No EVA
rs240740403 55 G>S No EVA
rs8236429 66 N>K No EVA
rs8248234 77 G>A No EVA
rs8248233 93 V>M No EVA
rs8248232 106 Q>P No EVA
rs8248232 106 Q>R No EVA
rs8248231 112 Y>H No EVA
rs3389294791 131 W>R No EVA
rs48787765 132 Q>R No EVA
rs50591090 154 D>E No EVA
rs579649743 161 R>K No EVA
rs260017881 161 R>S No EVA
rs3389371252 163 L>H No EVA
rs49925026 174 S>P No EVA
rs48841404 179 T>P No EVA
rs579699258 183 N>K No EVA
rs8279240 184 A>S No EVA
rs8279243 185 V>A No EVA
rs8279242 185 V>M No EVA
rs8279245 198 F>L No EVA
rs3389371286 200 Y>N No EVA
rs8279246 204 Y>F No EVA
rs8279247 211 M>V No EVA
rs8279284 229 E>A No EVA
rs31686715 235 R>C No EVA
rs3389358298 243 V>A No EVA
rs8240901 243 V>F No EVA
rs3389373555 254 L>P No EVA
rs3406367687 267 P>H No EVA
rs3406312537 271 P>A No EVA
rs3389358332 280 A>T No EVA
rs3389340561 284 K>R No EVA
rs8279227 289 P>A No EVA
rs3389371254 292 S>N No EVA
rs8279226 295 D>H No EVA
rs8279224 303 G>R No EVA
rs8279223 303 G>V No EVA
rs222114530 309 G>R No EVA
rs3389384223 319 W>C No EVA
rs3389329326 332 R>G No EVA
rs1135226192 342 I>K No EVA
rs582044438 346 Q>R No EVA
rs579241601 355 R>H No EVA
rs3389340544 363 I>N No EVA
rs236703674 376 P>H No EVA
rs586421219 376 P>T No EVA
rs582340914 378 P>Q No EVA
rs3389376294 378 P>S No EVA
rs3389294819 379 R>H No EVA
rs579127514 379 R>S No EVA
rs212391649 386 E>Q No EVA
rs584624344 390 F>L No EVA
rs236244138 392 V>I No EVA
rs215238607 393 T>P No EVA
rs3389392247 401 N>I No EVA
rs32047531 402 M>L No EVA
rs255062407 405 V>M No EVA
rs47258643 408 D>G No EVA
rs3389373526 416 L>F No EVA
rs8248302 450 A>P No EVA
rs238595679 466 R>H No EVA
rs3389392209 471 V>M No EVA
rs8279238 483 V>A No EVA
rs8279237 500 R>H No EVA
rs8279235 503 G>E No EVA

No associated diseases with P24457

1 regional properties for P24457

Type Name Position InterPro Accession
conserved_site Cytochrome P450, conserved site 439 - 448 IPR017972

Functions

Description
EC Number 1.14.14.1 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
Subcellular Localization
  • Endoplasmic reticulum membrane; Peripheral membrane protein
  • Microsome membrane; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 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.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
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.

10 GO annotations of molecular function

Name Definition
anandamide 11,12 epoxidase activity Catalysis of the reaction: N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced = H(+) + H2O + N-(11,12-epoxy-5Z,8Z,14Z-eicosatrienoyl)-ethanolamine + oxidized
anandamide 14,15 epoxidase activity Catalysis of the reaction: N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced = H(+) + H2O + N-(14,15-epoxy-5Z,8Z,11Z-eicosatrienoyl)-ethanolamine + oxidized
anandamide 8,9 epoxidase activity Catalysis of the reaction: N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine + O2 + reduced = H(+) + H2O + N-(8,9-epoxy-5Z,11Z,14Z-eicosatrienoyl)-ethanolamine + oxidized
aromatase activity Catalysis of the reduction of an aliphatic ring to yield an aromatic ring.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
iron ion binding Binding to an iron (Fe) ion.
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.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor.
steroid hydroxylase activity Catalysis of the formation of a hydroxyl group on a steroid by incorporation of oxygen from O2.

3 GO annotations of biological process

Name Definition
arachidonic acid metabolic process The chemical reactions and pathways involving arachidonic acid, a straight chain fatty acid with 20 carbon atoms and four double bonds per molecule. Arachidonic acid is the all-Z-(5,8,11,14)-isomer.
organic acid metabolic process The chemical reactions and pathways involving organic acids, any acidic compound containing carbon in covalent linkage.
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.

52 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q0IIF9 CYP2U1 Cytochrome P450 2U1 Bos taurus (Bovine) PR
O18963 CYP2E1 Cytochrome P450 2E1 Bos taurus (Bovine) PR
P12394 CYP17A1 Steroid 17-alpha-hydroxylase/17,20 lyase Gallus gallus (Chicken) PR
Q95078 Cyp18a1 Cytochrome P450 18a1 Drosophila melanogaster (Fruit fly) PR
P33260 CYP2C18 Cytochrome P450 2C18 Homo sapiens (Human) PR
Q7Z449 CYP2U1 Cytochrome P450 2U1 Homo sapiens (Human) PR
P05177 CYP1A2 Cytochrome P450 1A2 Homo sapiens (Human) PR
P05093 CYP17A1 Steroid 17-alpha-hydroxylase/17,20 lyase Homo sapiens (Human) PR
P51589 CYP2J2 Cytochrome P450 2J2 Homo sapiens (Human) PR
P10632 CYP2C8 Cytochrome P450 2C8 Homo sapiens (Human) PR
P05181 CYP2E1 Cytochrome P450 2E1 Homo sapiens (Human) PR
P27786 Cyp17a1 Steroid 17-alpha-hydroxylase/17,20 lyase Mus musculus (Mouse) PR
O54749 Cyp2j5 Cytochrome P450 2J5 Mus musculus (Mouse) PR
O54750 Cyp2j6 Cytochrome P450 2J6 Mus musculus (Mouse) PR
P24456 Cyp2d10 Cytochrome P450 2D10 Mus musculus (Mouse) PR
Q9D816 Cyp2c55 Cytochrome P450 2C55 Mus musculus (Mouse) PR
Q9CX98 Cyp2u1 Cytochrome P450 2U1 Mus musculus (Mouse) PR
P79383 CYP2E1 Cytochrome P450 2E1 Sus scrofa (Pig) PR
P33273 Cyp2c55 Cytochrome P450 2C55 Rattus norvegicus (Rat) PR
P05182 Cyp2e1 Cytochrome P450 2E1 Rattus norvegicus (Rat) PR
P24470 Cyp2c23 Cytochrome P450 2C23 Rattus norvegicus (Rat) PR
P11715 Cyp17a1 Steroid 17-alpha-hydroxylase/17,20 lyase Rattus norvegicus (Rat) PR
P05179 Cyp2c7 Cytochrome P450 2C7 Rattus norvegicus (Rat) PR
P12938 Cyp2d3 Cytochrome P450 2D3 Rattus norvegicus (Rat) PR
O35293 Cyp2f2 Cytochrome P450 2F2 Rattus norvegicus (Rat) PR
P20814 Cyp2c13 Cytochrome P450 2C13, male-specific Rattus norvegicus (Rat) PR
P10633 Cyp2d1 Cytochrome P450 2D1 Rattus norvegicus (Rat) PR
P12939 Cyp2d10 Cytochrome P450 2D10 Rattus norvegicus (Rat) PR
Q8HYM9 CYP17A1 Steroid 17-alpha-hydroxylase/17,20 lyase Macaca mulatta (Rhesus macaque) PR
Q6YV88 CYP71Z7 Ent-cassadiene hydroxylase Oryza sativa subsp japonica (Rice) PR
A3A871 CYP71Z6 Ent-isokaurene C2/C3-hydroxylase Oryza sativa subsp japonica (Rice) PR
Q7X7X4 CYP99A2 Cytochrome P450 99A2 Oryza sativa subsp japonica (Rice) PR
O48957 CYP99A1 Cytochrome P450 CYP99A1 Sorghum bicolor (Sorghum) (Sorghum vulgare) PR
Q42797 CYP73A11 Trans-cinnamate 4-monooxygenase Glycine max (Soybean) (Glycine hispida) PR
O48922 CYP98A2 Cytochrome P450 98A2 Glycine max (Soybean) (Glycine hispida) PR
Q9XHC6 CYP93E1 Beta-amyrin 24-hydroxylase Glycine max (Soybean) (Glycine hispida) PR
O81971 CYP71D9 Cytochrome P450 71D9 Glycine max (Soybean) (Glycine hispida) PR
O49340 CYP71A12 Cytochrome P450 71A12 Arabidopsis thaliana (Mouse-ear cress) PR
O64638 CYP76C3 Cytochrome P450 76C3 Arabidopsis thaliana (Mouse-ear cress) PR
P58049 CYP71B11 Cytochrome P450 71B11 Arabidopsis thaliana (Mouse-ear cress) PR
P58050 CYP71B13 Cytochrome P450 71B13 Arabidopsis thaliana (Mouse-ear cress) PR
Q96514 CYP71B7 Cytochrome P450 71B7 Arabidopsis thaliana (Mouse-ear cress) PR
Q9CA61 CYP98A8 Cytochrome P450 98A8 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LTM0 CYP71B23 Cytochrome P450 71B23 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LTM6 CYP71B17 Cytochrome P450 71B17 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LTM7 CYP71B16 Cytochrome P450 71B16 Arabidopsis thaliana (Mouse-ear cress) PR
Q9LVD2 CYP71B10 Cytochrome P450 71B10 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SAE4 CYP71B29 Cytochrome P450 71B29 Arabidopsis thaliana (Mouse-ear cress) PR
Q9SRQ1 CYP89A9 Cytochrome P450 89A9 Arabidopsis thaliana (Mouse-ear cress) PR
Q9ZU07 CYP71B12 Cytochrome P450 71B12 Arabidopsis thaliana (Mouse-ear cress) PR
O64636 CYP76C1 Cytochrome P450 76C1 Arabidopsis thaliana (Mouse-ear cress) PR
Q949U1 CYP79F1 Dihomomethionine N-hydroxylase Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MELLTGAGLW SVAIFTVIFI LLVDLMHRHQ HWTSRCPPGP VPWPVLGNLL QVDLGNMPYS
70 80 90 100 110 120
LYKLQNRYGD VFSLQMGWKP MVVINGLKAM KEVLLTCGED TADRPQVPIF EYLGVKPGSQ
130 140 150 160 170 180
GVVLAPYGPE WQEQRRFSVS TLRNFGLGKK SLEDWVTKEA RHLCDAFTAQ AGQSINPNTM
190 200 210 220 230 240
LNNAVCNVIA SLIFARRFEY EDPYLIRMLK MLKECFTEIS GFIPGVLNEF PIFLRIPGLA
250 260 270 280 290 300
DMVFQGQKSF MAILDNLLTE NRTTWDPDQP PRNLTDAFLA EIEKAKGNPE SSFNDENLRM
310 320 330 340 350 360
VVGDLFTAGM VTTSTTLSWA LLLMILHPDV QRRVQQEIDA VIGQVQHPEM ADQARMPYTN
370 380 390 400 410 420
AVIHEVQRFG DIAPLPLPRI TSRDIEVQDF LVTKGSTLIP NMSSVLKDET VWEKPLRFHP
430 440 450 460 470 480
EHFLDAQGHF VKPEAFMPFS AGHRSCLGEA LARMELFLFF TCLLQRFSIS VPDGQPQPSN
490 500
YRVHAIPVAP FPYQLCAVMR EQGH