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Q9CQ92 (FIS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial fission 1 protein
Alternative name(s):
FIS1 homolog
Tetratricopeptide repeat protein 11
Short name=TPR repeat protein 11
Gene names
Name:Fis1
Synonyms:Ttc11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the fragmentation of the mitochondrial network and its perinuclear clustering. Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission. May be not essential for the assembly of functional fission complexes and the subsequent membrane scission event. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission. Ref.4

Subunit structure

Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5 By similarity. Interacts with MIEF1 By similarity.

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein. Peroxisome membrane; Single-pass membrane protein By similarity.

Domain

The C-terminus is required for mitochondrial or peroxisomal localization, while the N-terminus is necessary for mitochondrial or peroxisomal fission, localization and regulation of the interaction with DNM1L By similarity.

Post-translational modification

Ubiquitinated by MARCH5 By similarity.

Sequence similarities

Belongs to the FIS1 family.

Contains 1 TPR repeat.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
Peroxisome
   DomainTPR repeat
Transmembrane
Transmembrane helix
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling using intracellular calcium source

Inferred from electronic annotation. Source: Ensembl

mitochondrial fission

Inferred from mutant phenotype Ref.4. Source: UniProtKB

mitochondrial fragmentation involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial fusion

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion degradation

Inferred from electronic annotation. Source: Ensembl

mitochondrion morphogenesis

Inferred from sequence orthology PubMed 21149567. Source: MGI

negative regulation of endoplasmic reticulum calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

peroxisome fission

Inferred from sequence or structural similarity PubMed 17408615. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial fission

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein targeting to mitochondrion

Inferred from electronic annotation. Source: Ensembl

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of peroxisomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853PubMed 17035996PubMed 18614015. Source: MGI

peroxisome

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Mitochondrial fission 1 protein
PRO_0000106394

Regions

Topological domain1 – 122122Cytoplasmic Potential
Transmembrane123 – 14321Helical; Potential
Topological domain144 – 1529Mitochondrial intermembrane Potential
Repeat71 – 10434TPR

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Secondary structure

............... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CQ92 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B012DF491518A4B1

FASTA15217,009
        10         20         30         40         50         60 
MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNED IRRGIVLLEE 

        70         80         90        100        110        120 
LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK 

       130        140        150 
DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Liver, Small intestine and Stomach.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 20-32; 54-64; 72-83 AND 96-108, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
Loson O.C., Song Z., Chen H., Chan D.C.
Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Solution structure of RSGI RUH-001, a FIS1p-like and CGI-135 homologous domain from a mouse cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2002) to the PDB data bank
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK004479 mRNA. Translation: BAB23324.1.
AK004917 mRNA. Translation: BAB23668.1.
AK008078 mRNA. Translation: BAB25445.1.
AK008323 mRNA. Translation: BAB25601.1.
AK008916 mRNA. Translation: BAB25966.1.
BC010783 mRNA. Translation: AAH10783.1.
CCDSCCDS19757.1.
RefSeqNP_001156715.1. NM_001163243.1.
NP_079838.1. NM_025562.3.
UniGeneMm.25849.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYGNMR-A1-120[»]
ProteinModelPortalQ9CQ92.
SMRQ9CQ92. Positions 1-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211472. 1 interaction.
IntActQ9CQ92. 1 interaction.
MINTMINT-1859640.
STRING10090.ENSMUSP00000019198.

PTM databases

PhosphoSiteQ9CQ92.

Proteomic databases

MaxQBQ9CQ92.
PaxDbQ9CQ92.
PRIDEQ9CQ92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019198; ENSMUSP00000019198; ENSMUSG00000019054.
GeneID66437.
KEGGmmu:66437.
UCSCuc009abf.2. mouse.

Organism-specific databases

CTD51024.
MGIMGI:1913687. Fis1.

Phylogenomic databases

eggNOGNOG235677.
GeneTreeENSGT00390000000592.
HOGENOMHOG000165386.
HOVERGENHBG081530.
InParanoidQ9CQ92.
KOK17969.
OMAEIFRTSP.
PhylomeDBQ9CQ92.
TreeFamTF315180.

Gene expression databases

BgeeQ9CQ92.
GenevestigatorQ9CQ92.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR016543. Fis1.
IPR028061. Fis1_TPR_C.
IPR028058. Fis1_TPR_N.
IPR011990. TPR-like_helical.
[Graphical view]
PANTHERPTHR13247. PTHR13247. 1 hit.
PfamPF14853. Fis1_TPR_C. 1 hit.
PF14852. Fis1_TPR_N. 1 hit.
[Graphical view]
PIRSFPIRSF008835. TPR_repeat_11_Fis1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSFIS1. mouse.
EvolutionaryTraceQ9CQ92.
NextBio321685.
PROQ9CQ92.
SOURCESearch...

Entry information

Entry nameFIS1_MOUSE
AccessionPrimary (citable) accession number: Q9CQ92
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot