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 Q3S8M4

Entry ID Method Resolution Chain Position Source
AF-Q3S8M4-F1 Predicted AlphaFoldDB

No variants for Q3S8M4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3S8M4

No associated diseases with Q3S8M4

1 regional properties for Q3S8M4

Type Name Position InterPro Accession
conserved_site ELO family, conserved site 154 - 162 IPR030457

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.

2 GO annotations of molecular function

Name Definition
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.

7 GO annotations of biological process

Name Definition
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
Q9JLJ5 Elovl1 Elongation of very long chain fatty acids protein 1 Mus musculus (Mouse) PR
Q9D2Y9 Elovl7 Elongation of very long chain fatty acids protein 7 Mus musculus (Mouse) PR
10 20 30 40 50 60
MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL SISTLYLLFV
70 80 90 100 110 120
WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN FFIFRELFMG SYNAGYSYIC QSVDYSNNVN
130 140 150 160 170 180
EVRIAAALWW YFVSKGVEYL DTVFFILRKK NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ
190 200 210 220 230 240
AFFGAQMNSF IHVIMYSYYG LAAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD
250 260 270 280 290 300
CPFPKWMHWA LIAYAISFIF LFLNFYIRTY KEPKKPKTGK TAMNGISANG VSKSEKQLVI
310
ENGKKQKNGK AKGD