CISD1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0010506Biological processregulation of autophagy
GO_0106034Biological processprotein maturation by [2Fe-2S] cluster transfer
GO_0043457Biological processregulation of cellular respiration
GO_0005741Cellular componentmitochondrial outer membrane
GO_0005739Cellular componentmitochondrion
GO_0042803Molecular functionprotein homodimerization activity
GO_0051537Molecular function2 iron, 2 sulfur cluster binding
GO_0047801Molecular functionL-cysteine transaminase activity
GO_0042802Molecular functionidentical protein binding
GO_0030170Molecular functionpyridoxal phosphate binding
GO_0046872Molecular functionmetal ion binding

IV. Literature review

[source]
Gene nameCISD1
Protein nameCDGSH iron-sulfur domain-containing protein 1 (Cysteine transaminase CISD1) (EC 2.6.1.3) (MitoNEET)
SynonymsMDS029
ZCD1
C10orf70
DescriptionFUNCTION: L-cysteine transaminase that catalyzes the reversible transfer of the amino group from L-cysteine to the alpha-keto acid 2-oxoglutarate to respectively form 2-oxo-3-sulfanylpropanoate and L-glutamate . The catalytic cycle occurs in the presence of pyridoxal 5'-phosphate (PLP) cofactor that facilitates transamination by initially forming an internal aldimine with the epsilon-amino group of active site Lys-55 residue on the enzyme (PLP-enzyme aldimine), subsequently displaced by formation of an external aldimine with the substrate amino group (PLP-L-cysteine aldimine). The external aldimine is further deprotonated to form a carbanion intermediate, which in the presence of 2-oxoglutarate regenerates PLP yielding final products 2-oxo-3-sulfanylpropanoate and L-glutamate. The proton transfer in carbanion intermediate is suggested to be controlled by the active site lysine residue, whereas PLP stabilizes carbanion structure through electron delocalization, also known as the electron sink effect . Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in iron-sulfur cluster shuttling and/or in redox reactions. Can transfer the [2Fe-2S] cluster to an apo-acceptor protein only when in the oxidation state, likely serving as a redox sensor that regulates mitochondrial iron-sulfur cluster assembly and iron trafficking upon oxidative stress . .

AccessionsENST00000333926.6
Q9NZ45