| General information | | DisProt: | DP00457 | | Name: | Mitochondrial fission 1 protein | | Synonym(s): | FIS1_HUMAN
FIS1 homolog
hFis1
Tetratricopeptide repeat protein 11
TPR repeat protein 11
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q9Y3D6 | | UniGene: | Hs.423968 | | SwissProt: | FIS1_HUMAN | | TrEMBL: | | | NCBI (GI): | 151108473 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 152 | | Percent disordered: | 30% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE - 60
LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK - 120
DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS
|
| Functional narrative |
Promotes the fragmentation of the mitochondrial network and its perinuclear clustering. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 10 | | Length: | 10 | | Region sequence: |
MEAVLNELVS | | Modification type: | Engineered
Mutant
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (305 K; )
| References:
- Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. "The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle." J Mol Biol. 2003; 334(3): 445-58. PubMed: 14623186
| Comments:
|
| Region 2 | | Type: | Disordered | | Name: | | | Location: | 28 - 31 | | Length: | 4 | | Region sequence: |
GSVS | | Modification type: | Engineered
Mutant
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (305 K; )
| References:
- Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. "The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle." J Mol Biol. 2003; 334(3): 445-58. PubMed: 14623186
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 121 - 152 | | Length: | 32 | | Region sequence: |
DGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS | | Modification type: | Engineered
Mutant
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Unknown
| Detection methods:
- Nuclear magnetic resonance (NMR) (305 K; )
| References:
- Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. "The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle." J Mol Biol. 2003; 334(3): 445-58. PubMed: 14623186
| Comments:The length of the recombinant protein is the same as that of the wild-type protein but the last seven amino acids are EHHHHHH instead of AVSKSKS.
|
| Comments |
According to the paper, Fis1 may function as a molecular adaptor at the mitochondrial outer membrane because it has a binding domain and a transmembrane segment.
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
