| Tag |
Content |
LipidDB ID |
LipidDB-10116-00023 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
8.99 |
Molecular Weight |
12096.96 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
CDGSH iron-sulfur domain-containing protein 1 |
Protein Synonyms/Alias |
MitoNEET; |
Gene Name |
Cisd1 |
Gene Synonyms/Alias |
|
Created Date |
25-NOV-2008 |
| Lipid Modification Sites |
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
72 | Canonical | LGDKAVYCRCWRSKK | [1] | S-Palmitoylation |
|
Organism |
Rattus norvegicus (Rat) |
NCBI Taxa ID |
10116 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions. |
Sequence Annotation |
Transmembrane: 13 31 Helical; Signal-anchor for type IIImembrane protein. Topological domain: 32 108 Cytoplasmic. Metal binding site: 72 72 Iron-sulfur (2Fe-2S). Metal binding site: 74 74 Iron-sulfur (2Fe-2S). Metal binding site: 83 83 Iron-sulfur (2Fe-2S). Metal binding site: 87 87 Iron-sulfur (2Fe-2S); via pros nitrogen. Modified residue: 55 55 N6-acetyllysine. Modified residue: 68 68 N6-acetyllysine. Modified residue: 104 104 N6-acetyllysine.
|
Protein Length |
108 AA. |
Protein Sequence (Canonical) |
MGLSSDSPVR VEWIAAVTFA AGTAALGYLA YKKFYAKESR TKAMVNLQIQ KDNPKVVHAF 60
DMEDLGDKAV YCRCWRSKKF PFCDGAHIKH NEETGDNVGP LIIKKKET 108
|
FASTA (Canonical) |
>LipidDB-10116-00023|B0K020
MGLSSDSPVRVEWIAAVTFAAGTAALGYLAYKKFYAKESRTKAMVNLQIQKDNPKVVHAF
DMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET
|
Gene Ontology |
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-KW GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0043457; P:regulation of cellular respiration; IEA:Ensembl |
Interpro |
|
Pfam |
|
SMART |
|
PROSITE |
|
PRINTS |
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