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 Q5RBK3

Entry ID Method Resolution Chain Position Source
AF-Q5RBK3-F1 Predicted AlphaFoldDB

No variants for Q5RBK3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RBK3

No associated diseases with Q5RBK3

No regional properties for Q5RBK3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q5RBK3

Functions

Description
EC Number 4.2.1.134 Hydro-lyases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.

6 GO annotations of molecular function

Name Definition
3-hydroxy-arachidoyl-CoA dehydratase activity Catalysis of the reaction: (R)-3-hydroxyicosanoyl-CoA <=> trans-2-icosenoyl-CoA + H2O.
3-hydroxy-behenoyl-CoA dehydratase activity Catalysis of the reaction: (R)-3-hydroxybehenoyl-CoA <=> trans-2-docosenoyl-CoA + H2O.
3-hydroxy-lignoceroyl-CoA dehydratase activity Catalysis of the reaction: (R)-3-hydroxylignoceroyl-CoA(4-) <=> trans-2-tetracosenoyl-CoA + H2O.
3-hydroxyacyl-CoA dehydratase activity Catalysis of the reaction: alkene-CoA + H2O = alcohol-CoA. Substrates are crotonoyl-CoA (producing 3-hydroxyacyl-CoA) and 2,3-didehydro-pimeloyl-CoA (producing 3-hydroxypimeloyl-CoA).
enzyme binding Binding to an enzyme, a protein with catalytic activity.
very-long-chain 3-hydroxyacyl-CoA dehydratase activity Catalysis of the reaction: a very-long-chain (3R)-3-hydroxyacyl-CoA = H2O + a very-long-chain trans-2,3-dehydroacyl-CoA.

3 GO annotations of biological process

Name Definition
fatty acid elongation The elongation of a fatty acid chain by the sequential addition of two-carbon units.
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).
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAAAAAATAA AKGNGGGGGR AGAGDASGTR KKKGPGPLAT AYLVIYNVVM TAGWLVIAVG
70 80 90 100 110 120
LVRAYLAKGS YHSLYYSIEK PLKFFQTGAL LEILHCAIGI VPSSVVLTSF QVMSRVFLIW
130 140 150 160 170 180
AVTHSVKEVQ SEDSVLLFVI AWTITEIIRY SFYTFSLLNH LPYLIKWARY TLFIVLYPMG
190 200 210 220 230 240
VSGELLTIYA ALPFVRQAGL YSISLPNKYN FSFDYYAFLI LIMISYIPIF PQLYFHMIHQ
250
RRKILSHTEE HKKFE