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 F4JLZ6

Entry ID Method Resolution Chain Position Source
AF-F4JLZ6-F1 Predicted AlphaFoldDB

19 variants for F4JLZ6

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH06754876 19 T>S No 1000Genomes
tmp_4_11953547_G_C 21 F>L No 1000Genomes
tmp_4_11953501_C_T 37 V>I No 1000Genomes
ENSVATH00531692 62 T>S No 1000Genomes
tmp_4_11953414_C_T 66 D>N No 1000Genomes
tmp_4_11953381_A_G 77 S>P No 1000Genomes
tmp_4_11953302_G_A 103 S>F No 1000Genomes
tmp_4_11953001_T_G 109 M>L No 1000Genomes
ENSVATH06754868 138 T>A No 1000Genomes
ENSVATH12154647 176 A>G No 1000Genomes
tmp_4_11952788_T_C 180 I>V No 1000Genomes
ENSVATH02910532 197 M>I No 1000Genomes
ENSVATH00531690 208 F>I No 1000Genomes
ENSVATH06754863 233 P>A No 1000Genomes
ENSVATH12154645 248 S>T No 1000Genomes
ENSVATH06754855 276 H>Q No 1000Genomes
ENSVATH12154613 282 A>T No 1000Genomes
ENSVATH06754854 286 R>G No 1000Genomes
ENSVATH06754853 290 H>Q No 1000Genomes

No associated diseases with F4JLZ6

1 regional properties for F4JLZ6

Type Name Position InterPro Accession
domain Fatty acid hydroxylase 128 - 263 IPR006694

Functions

Description
EC Number 1.14.18.9 With another compound as one donor, and incorporation of one atom of oxygen
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 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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

3 GO annotations of molecular function

Name Definition
C-4 methylsterol oxidase activity Catalysis of the reaction: 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + 6 Fe(II)- + 5 H+ + 3 O2 = 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholesta-8,24-dien-3-beta-ol + 6 Fe(III)-
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.

1 GO annotations of biological process

Name Definition
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.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZLL6 MSMO1 Methylsterol monooxygenase 1 Gallus gallus (Chicken) PR
10 20 30 40 50 60
MIPYPTVEDA SVALGRNLTW FETVWFDYSA TKSNFHVYCH TILVLFLVFS LAPFPLVIVE
70 80 90 100 110 120
WTGWFDQFKI QKKVKYSLSD MFQCYKEVMK LFLLVVGTLQ IVSYPSIQMV GIRSGLPLPS
130 140 150 160 170 180
LMEIVAQLVV YFLIEDYTNY WIHRWMHCKW GYEKIHRIHH EYTSPIGYAS PYAHWAEILI
190 200 210 220 230 240
LGIPTFLGPA IAPGHIMTFW LWISLRQFEA IETHSGYDFP WSVTKLIPFY GGPEYHDYHH
250 260 270 280 290
YVGGQSQSNF ASVFTYCDYI YGTDKGYRIH KKLLHHQIKE EAEEKRVRKH D