CISD1
entrez
55847
canonical
uniprot
Q9NZ45
canonical
ensembl
ENSG00000122873
resolver
ensp
ENSP00000363041
resolver
enst
ENST00000333926
resolver
genesymbol
CISD1
resolver
genesymbol_syn
C10orf70
resolver
genesymbol_syn
ZCD1
resolver
hgnc
HGNC:30880
resolver
uniprot
Q1X902
resolver
uniprot_entry
CISD1_HUMAN
resolver
uniprot_sec
Q1X902
resolver
amino_acid_sequence
MSLTSSSSVRVEWIAAVTIAAGTAAIGYLAYKRFYVKDHRNKAMINLHIQKDNPKIVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHTKHNEETGDNVGPLIIKKKET
uniprot
proteins
ec_number
2.6.1.3
uniprot
proteins
function
FUNCTION: 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 (PubMed:36194135). 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 (PubMed:36194135). 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 (PubMed:17584744, PubMed:21788481, PubMed:23758282). {ECO:0000250, ECO:0000250|UniProtKB:Q91WS0, ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:17766440, ECO:0000269|PubMed:21788481, ECO:0000269|PubMed:23758282, ECO:0000269|PubMed:36194135}.
uniprot
proteins
mass_dalton
12199
uniprot
proteins
mutagenesis
MUTAGEN 55; /note="K->E: Slighly reduces the transfer rate of the [2Fe-2S] cluster."; /evidence="ECO:0000269|PubMed:21788481"; MUTAGEN 55; /note="K->I: Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster; when associated with Cys-87."; /evidence="ECO:0000269|PubMed:23758282"; MUTAGEN 72; /note="C->S: Abolishes absorption in the 300-500 nm range."; /evidence="ECO:0000269|PubMed:17584744"; MUTAGEN 74; /note="C->S: Abolishes absorption in the 300-500 nm range."; /evidence="ECO:0000269|PubMed:17584744"; MUTAGEN 77; /note="S->A: Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster."; /evidence="ECO:0000269|PubMed:23758282"; MUTAGEN 83; /note="C->S: Abolishes absorption in the 300-500 nm range."; /evidence="ECO:0000269|PubMed:17584744"; MUTAGEN 84; /note="D->N: Fully incorporates the [2Fe-2S] cluster upon in vitro reconstitution. Does not affect absorption in the 300-500 nm range. Slightly affects neutral pH dependence of the midpoint redox potential of the [2Fe-2S] cluster."; /evidence="ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:23758282"; MUTAGEN 87; /note="H->C: Fully incorporates and stabilizes the [2Fe-2S] cluster upon in vitro reconstitution. Abolishes alkaline pH dependence of the midpoint redox potential of the [2Fe-2S] cluster; when associated with Ile-55. Markedly decreases the transfer rate of the [2Fe-2S] cluster. Abolishes iron transfer to the mitochondrial matrix."; /evidence="ECO:0000269|PubMed:17584744, ECO:0000269|PubMed:21788481, ECO:0000269|PubMed:23758282"; MUTAGEN 87; /note="H->Q: Abolishes absorption in the 300-500 nm range."; /evidence="ECO:0000269|PubMed:17584744
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000269|PubMed:25621951}.
uniprot
proteins
protein_family
CISD protein family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17376863
uniprot
proteins
pubmed
17584744
uniprot
proteins
pubmed
17766439
uniprot
proteins
pubmed
17766440
uniprot
proteins
pubmed
17905743
uniprot
proteins
pubmed
18047834
uniprot
proteins
pubmed
19580816
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21788481
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23758282
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25621951
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
36194135
uniprot
proteins
sequence_length
108
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}; Single-pass type III membrane protein {ECO:0000269|PubMed:17376863, ECO:0000269|PubMed:17766439, ECO:0000269|PubMed:17905743, ECO:0000269|PubMed:18047834}.
uniprot
proteins
transmembrane_region
TRANSMEM 14..31; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255
uniprot
proteins