Q9Z122

PR
Gene name
Fads2 (Fadsd6)
Protein name
Acyl-CoA 6-desaturase
Names
Delta(6) fatty acid desaturase, D6D, Delta(6) desaturase, Delta-6 desaturase, Fatty acid desaturase 2
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:83512
EC number
1.14.19.3: With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

71-144 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9Z122

Entry ID Method Resolution Chain Position Source
AF-Q9Z122-F1 Predicted AlphaFoldDB

1 variants for Q9Z122

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3319186578 246 P>A No EVA

No associated diseases with Q9Z122

2 regional properties for Q9Z122

Type Name Position InterPro Accession
domain Cytochrome b5-like heme/steroid binding domain 18 - 95 IPR001199
domain Fatty acid desaturase domain 157 - 417 IPR005804

Functions

Description
EC Number 1.14.19.3 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
  • Microsome membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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.

4 GO annotations of molecular function

Name Definition
linoleoyl-CoA desaturase activity Catalysis of the reaction: linoleoyl-CoA + reduced acceptor + O2 = gamma-linolenoyl-CoA + acceptor + 2 H2O.
omega-6 fatty acid desaturase activity Catalysis of the introduction of an omega-6 double bond into the fatty acid hydrocarbon chain.
oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced to two molecules of water.
stearoyl-CoA 9-desaturase activity Catalysis of the reaction: stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.

3 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.
unsaturated fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of an unsaturated fatty acid, any fatty acid containing one or more double bonds between carbon atoms.
very long-chain fatty acid biosynthetic process The chemical reactions and pathways resulting in the formation of a fatty acid which has a chain length greater than C22.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9ZRP7 SLD1 Delta(8)-fatty-acid desaturase 1 Arabidopsis thaliana (Mouse-ear cress) PR
Q9DEX7 fads2 Acyl-CoA 6-desaturase Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MGKGGNQGEG STELQAPMPT FRWEEIQKHN LRTDRWLVID RKVYNVTKWS QRHPGGHRVI
70 80 90 100 110 120
GHYSGEDATD AFRAFHLDLD FVGKFLKPLL IGELAPEEPS LDRGKSSQIT EDFRALKKTA
130 140 150 160 170 180
EDMNLFKTNH LFFFLLLSHI IVMESIAWFI LSYFGNGWIP TVITAFVLAT SQAQAGWLQH
190 200 210 220 230 240
DYGHLSVYKK SIWNHIVHKF VIGHLKGASA NWWNHRHFQH HAKPNIFHKD PDIKSLHVFV
250 260 270 280 290 300
LGEWQPLEYG KKKLKYLPYN HQHEYFFLIG PPLLIPMYFQ YQIIMTMIRR RDWVDLAWAI
310 320 330 340 350 360
SYYARFFYTY IPFYGILGAL VFLNFIRFLE SHWFVWVTQM NHIVMEIDLD HYRDWFSSQL
370 380 390 400 410 420
AATCNVEQSF FNDWFSGHLN FQIEHHLFPT MPRHNLHKIA PLVKSLCAKH GIEYQEKPLL
430 440
RALLDIVSSL KKSGELWLDA YLHK