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 O88822

Entry ID Method Resolution Chain Position Source
AF-O88822-F1 Predicted AlphaFoldDB

20 variants for O88822

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389040086 15 P>L No EVA
rs3389030500 35 L>Q No EVA
rs3389025630 70 K>M No EVA
rs3389035333 85 P>T No EVA
rs3389030504 99 L>R No EVA
rs3389035044 105 L>H No EVA
rs3389040098 108 D>V No EVA
rs3389017123 116 W>L No EVA
rs3389037231 122 S>N No EVA
rs3389042784 127 L>P No EVA
rs3389040046 128 F>L No EVA
rs3389017098 155 H>N No EVA
rs3389025648 167 A>V No EVA
rs3389037234 169 H>Q No EVA
rs3388986008 172 D>E No EVA
rs227883817 217 Q>R No EVA
rs3389035079 219 L>I No EVA
rs3389031145 241 G>R No EVA
rs3389030532 269 V>M No EVA
rs36310583 291 G>S No EVA

No associated diseases with O88822

1 regional properties for O88822

Type Name Position InterPro Accession
domain Fatty acid hydroxylase 124 - 252 IPR006694

Functions

Description
EC Number 1.14.19.20 With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
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.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

4 GO annotations of molecular function

Name Definition
C-5 sterol desaturase activity Catalysis of the reaction: 5,7,24(28)-ergostatrienol + O2 + NADPH = 5,7,22,24(28)-ergostatetraenol + 2 H2O + NADP+.
delta7-sterol 5(6)-desaturase activity Catalysis of the reaction: a delta(7)-sterol + 2 ferrocytochrome b5 + O2 + 2 H+ -> a delta(5,7)-sterol + 2 ferricytochrome b5 + 2 H2O.
iron ion binding Binding to an iron (Fe) ion.
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.

2 GO annotations of biological process

Name Definition
cholesterol biosynthetic process via lathosterol The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, via the intermediate lathosterol.
sterol biosynthetic process The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
O75845 SC5D Lathosterol oxidase Homo sapiens (Human) PR
Q9EQS5 Sc5d Lathosterol oxidase Rattus norvegicus (Rat) PR
O17554 agmo-1 Alkylglycerol monooxygenase Caenorhabditis elegans PR
Q5M8F9 agmo Alkylglycerol monooxygenase Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q6NYE4 agmo Alkylglycerol monooxygenase Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MDLVLSAADY YFFTPYVYPA TWPEDNIIRQ TISLLIVTNL GAYILYFFCA TLSYYFVYDH
70 80 90 100 110 120
SLMKHPQFLK NQVSREIVFT VKSLPWISIP TVSLFLLELR GYSKLYDDIG DFPNGWIHLM
130 140 150 160 170 180
VSVVSFLFFT DMLIYWIHRG LHHRLVYKRI HKPHHIWKIP TPFASHAFHP VDGFLQSLPY
190 200 210 220 230 240
HIYPFVFPLH KVVYLGLYVL VNVWTISIHD GDFRVPQILR PFINGSAHHT DHHMFFDYNY
250 260 270 280 290
GQYFTLWDRI GGSFKHPSSF EGKGPHSYVK NMTEKESNSF AENGCKGKKV GNGEFTKNK