Q9JLJ5

PR
Gene name
Elovl1
Protein name
Elongation of very long chain fatty acids protein 1
Names
3-keto acyl-CoA synthase Elovl1, ELOVL fatty acid elongase 1, ELOVL FA elongase 1, Very long chain 3-ketoacyl-CoA synthase 1, Very long chain 3-oxoacyl-CoA synthase 1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:54325
EC number
2.3.1.199: Transferring groups other than amino-acyl groups
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

227-279 (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 Q9JLJ5

Entry ID Method Resolution Chain Position Source
AF-Q9JLJ5-F1 Predicted AlphaFoldDB

14 variants for Q9JLJ5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3394752545 27 S>P No EVA
rs239353338 40 Y>C No EVA
rs3394734626 53 R>W No EVA
rs3388691761 66 N>K No EVA
rs3388699065 81 L>Q No EVA
rs3394811913 102 P>L No EVA
rs3388702128 110 V>M No EVA
rs3388705862 125 T>I No EVA
rs3388701004 148 L>F No EVA
rs3388704466 165 S>A No EVA
rs3388707284 178 M>K No EVA
rs3388707292 240 G>D No EVA
rs3388707349 276 V>I No EVA
rs3388706233 277 K>N No EVA

No associated diseases with Q9JLJ5

4 regional properties for Q9JLJ5

Type Name Position InterPro Accession
domain RNA recognition motif domain 225 - 302 IPR000504-1
domain RNA recognition motif domain 326 - 406 IPR000504-2
domain RNA recognition motif domain 446 - 521 IPR000504-3
domain ESRP1, RNA recognition motif 1 216 - 308 IPR034427

Functions

Description
EC Number 2.3.1.199 Transferring groups other than amino-acyl groups
Subcellular Localization
  • Endoplasmic reticulum 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 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).
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum 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
3-oxo-cerotoyl-CoA synthase activity Catalysis of the reaction: tetracosanoyl-CoA(4-) + malonyl-CoA(5-) + H+ <=> 3-oxohexacosanoyl-CoA + carbon dioxide + coenzyme A.
3-oxo-lignoceronyl-CoA synthase activity Catalysis of the reaction: behenoyl-CoA(4-) + malonyl-CoA(5-) + H+ <=> 3-oxotetracosanoyl-CoA. + carbon dioxide + coenzyme A.
fatty acid elongase activity Catalysis of the reaction: fatty acid (C-16 or longer) + 2-C = fatty acid (C-16 or longer + 2-C).
very-long-chain 3-ketoacyl-CoA synthase activity Catalysis of the reaction: malonyl-CoA + a very-long-chain 2,3,4-saturated fatty acyl CoA = carbon dioxide + coenzyme A + a very-long-chain oxoacyl-CoA.

9 GO annotations of biological process

Name Definition
ceramide biosynthetic process The chemical reactions and pathways resulting in the formation of ceramides, any N-acylated sphingoid.
establishment of skin barrier Establishment of the epithelial barrier, the functional barrier in the skin that limits its permeability.
fatty acid elongation, monounsaturated fatty acid Elongation of a fatty acid chain into which one C-C double bond has been introduced.
fatty acid elongation, polyunsaturated fatty acid Elongation of a fatty acid chain into which two or more C-C double bonds have been introduced.
fatty acid elongation, saturated fatty acid Elongation of a saturated fatty acid chain.
long-chain fatty-acyl-CoA biosynthetic process The chemical reactions and pathways resulting in the formation of a long-chain fatty-acyl-CoA any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
sphingolipid biosynthetic process The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A1L3X0 ELOVL7 Elongation of very long chain fatty acids protein 7 Homo sapiens (Human) PR
Q9BW60 ELOVL1 Elongation of very long chain fatty acids protein 1 Homo sapiens (Human) PR
Q9D2Y9 Elovl7 Elongation of very long chain fatty acids protein 7 Mus musculus (Mouse) PR
Q3S8M4 ELOVL4 Elongation of very long chain fatty acids protein 4 Macaca mulatta (Rhesus macaque) PR
10 20 30 40 50 60
MEAVVNLYHE LMKHADPRIQ SYPLMGSPLL ITSILLTYVY FILSLGPRIM ANRKPFQLRG
70 80 90 100 110 120
FMIVYNFSLV ILSLYIVYEF LMSGWLSTYT WRCDPIDFSN SPEALRMVRV AWLFMLSKVI
130 140 150 160 170 180
ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW SWWWGIKIAP GGMGSFHAMI NSSVHVVMYL
190 200 210 220 230 240
YYGLSALGPV AQPYLWWKKH MTAIQLIQFV LVSLHISQYY FMPSCNYQYP IIIHLIWMYG
250 260 270
TIFFILFSNF WYHSYTKGKR LPRAVQQNGA PATTKVKAN