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P84817 (FIS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Short name=rFis1
Tetratricopeptide repeat protein 11
Short name=TPR repeat protein 11
Gene names
Name:Fis1
Synonyms:Ttc11
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis. Also mediates peroxisomal fission By similarity. Ref.1

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 Ref.1.

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. Ref.1 UniProtKB Q9Y3D6

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
   Coding sequence diversityAlternative splicing
   DomainTPR repeat
Transmembrane
Transmembrane helix
   PTMAcetylation
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling using intracellular calcium source

Inferred from electronic annotation. Source: Ensembl

mitochondrial fission

Inferred from sequence or structural similarity. 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 electronic annotation. Source: Ensembl

negative regulation of endoplasmic reticulum calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

peroxisome fission

Inferred from sequence or structural similarity. 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

peroxisome

Inferred from direct assay PubMed 14561759. Source: HGNC

protein complex

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P84817-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P84817-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MEAVLNELVSVEDLK → MPRDEAAR
     121-152: DGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS → GDRPHAVCSS...CGGECGQGRG
Isoform 3 (identifier: P84817-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MEAVLNELVSVEDLK → MPRDEAAR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Mitochondrial fission 1 protein
PRO_0000233948

Regions

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity UniProtKB Q9Y3D6

Natural variations

Alternative sequence1 – 1515MEAVL…VEDLK → MPRDEAAR in isoform 2 and isoform 3.
VSP_039625
Alternative sequence121 – 15232DGLVG…SKSKS → GDRPHAVCSSSSLRPGPWEH CPHPLHTHSPLSNLPSKGLG SPGAPTLRLYIQVPLFCGGE CGQGRG in isoform 2.
VSP_039626

Experimental info

Mutagenesis771L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-84; A-91; A-97 and A-98. Ref.1
Mutagenesis841L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-91; A-97 and A-98. Ref.1
Mutagenesis911L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-97 and A-98. Ref.1
Mutagenesis971L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-91 and A-98. Ref.1
Mutagenesis981L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-91 and A-97. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 50068E0C0148B1B0

FASTA15216,995
        10         20         30         40         50         60 
MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNDD IRRGIVLLEE 

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

       130        140        150 
DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS 

« Hide

Isoform 2 [UniParc].

Checksum: 09E996033486C0FA
Show »

FASTA17920,246
Isoform 3 [UniParc].

Checksum: 6D024F4B7CC6C17D
Show »

FASTA14516,251

References

« Hide 'large scale' references
[1]"Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein."
Jofuku A., Ishihara N., Mihara K.
Biochem. Biophys. Res. Commun. 333:650-659(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-77; LEU-84; LEU-91; LEU-97 AND LEU-98.
Tissue: Liver.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 2).
Tissue: Spleen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC111745 Genomic DNA. No translation available.
CH473973 Genomic DNA. Translation: EDM13301.1.
BC167057 mRNA. Translation: AAI67057.1.
RefSeqNP_001099389.1. NM_001105919.1. [P84817-3]
XP_006249184.1. XM_006249122.1. [P84817-2]
XP_006249185.1. XM_006249123.1. [P84817-1]
UniGeneRn.1298.

3D structure databases

ProteinModelPortalP84817.
SMRP84817. Positions 1-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid252608. 1 interaction.
MINTMINT-4581071.
STRING10116.ENSRNOP00000060173.

Proteomic databases

PaxDbP84817.
PRIDEP84817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001924; ENSRNOP00000001924; ENSRNOG00000001420. [P84817-1]
ENSRNOT00000063901; ENSRNOP00000061895; ENSRNOG00000001420. [P84817-2]
GeneID288584.
KEGGrno:288584.
UCSCRGD:1306668. rat. [P84817-1]

Organism-specific databases

CTD51024.
RGD1306668. Fis1.

Phylogenomic databases

eggNOGNOG235677.
GeneTreeENSGT00390000000592.
HOGENOMHOG000165386.
HOVERGENHBG081530.
InParanoidP84817.
KOK17969.
OMAEIFRTSP.
OrthoDBEOG73V6NH.
PhylomeDBP84817.
TreeFamTF315180.

Gene expression databases

GenevestigatorP84817.

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

NextBio628350.
PROP84817.

Entry information

Entry nameFIS1_RAT
AccessionPrimary (citable) accession number: P84817
Secondary accession number(s): B2RZ80, D4A5K3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: May 14, 2014
This is version 70 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