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Protein

Mitochondria fission 1 protein

Gene

FIS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a role in mitochondrial fission. Has a role in outer membrane fission but not matrix separation. Required for targeting MDV1 to the mitochondria. Regulates the assembly of DNM1 into punctate structures, in the mitochondrial tubules, promoting mitochondrial membrane constriction and/or division.5 Publications

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • chronological cell aging Source: SGD
  • mitochondrial fission Source: SGD
  • peroxisome fission Source: SGD
  • peroxisome organization Source: SGD
  • positive regulation of mitochondrial fission Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciYEAST:G3O-31333-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondria fission 1 protein
Alternative name(s):
Mitochondrial division protein 2
Gene namesi
Name:FIS1
Synonyms:MDV2
Ordered Locus Names:YIL065C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL065C.
SGDiS000001327. FIS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 131131CytoplasmicSequence analysisAdd
BLAST
Transmembranei132 – 14918HelicalSequence analysisAdd
BLAST
Topological domaini150 – 1556Mitochondrial intermembraneSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: SGD
  • peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi80 – 801L → P in fis1-L80P; no interaction with MDV1; mitochondrial fission is blocked; DNM1 assembly at punctate structures normal as in wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 155155Mitochondria fission 1 proteinPRO_0000202982Add
BLAST

Proteomic databases

MaxQBiP40515.

PTM databases

iPTMnetiP40515.

Interactioni

Subunit structurei

Interacts with DNM1 and MDV1.2 Publications

Protein-protein interaction databases

BioGridi34927. 103 interactions.
DIPiDIP-1897N.
IntActiP40515. 6 interactions.
MINTiMINT-398816.

Structurei

Secondary structure

1
155
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143Combined sources
Helixi19 – 3113Combined sources
Helixi34 – 363Combined sources
Helixi39 – 5113Combined sources
Beta strandi52 – 543Combined sources
Helixi55 – 7117Combined sources
Helixi73 – 753Combined sources
Helixi76 – 9015Combined sources
Helixi93 – 10412Combined sources
Helixi111 – 12717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8MNMR-A1-138[»]
2PQNX-ray2.15A1-129[»]
2PQRX-ray1.88A/B1-129[»]
3O48X-ray1.75A1-127[»]
3UUXX-ray3.90A/C1-129[»]
ProteinModelPortaliP40515.
SMRiP40515. Positions 5-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40515.

Family & Domainsi

Domaini

The C-terminus is required for mitochondrial localization, while the N-terminus is necessary for mitochondrial fission.By similarity

Sequence similaritiesi

Belongs to the FIS1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000000592.
HOGENOMiHOG000165386.
InParanoidiP40515.
KOiK17969.
OMAiYYLTIGC.
OrthoDBiEOG7N0CHT.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR016543. Fis1.
IPR028061. Fis1_TPR_C.
IPR028058. Fis1_TPR_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13247. PTHR13247. 1 hit.
PfamiPF14853. Fis1_TPR_C. 1 hit.
PF14852. Fis1_TPR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF008835. TPR_repeat_11_Fis1. 1 hit.
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

P40515-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKVDFWPTL KDAYEPLYPQ QLEILRQQVV SEGGPTATIQ SRFNYAWGLI
60 70 80 90 100
KSTDVNDERL GVKILTDIYK EAESRRRECL YYLTIGCYKL GEYSMAKRYV
110 120 130 140 150
DTLFEHERNN KQVGALKSMV EDKIQKETLK GVVVAGGVLA GAVAVASFFL

RNKRR
Length:155
Mass (Da):17,733
Last modified:February 1, 1995 - v1
Checksum:iBD62D19524770536
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38060 Genomic DNA. Translation: CAA86158.1.
AY557851 Genomic DNA. Translation: AAS56177.1.
BK006942 Genomic DNA. Translation: DAA08485.1.
PIRiS48414.
RefSeqiNP_012199.3. NM_001179415.3.

Genome annotation databases

EnsemblFungiiYIL065C; YIL065C; YIL065C.
GeneIDi854745.
KEGGisce:YIL065C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38060 Genomic DNA. Translation: CAA86158.1.
AY557851 Genomic DNA. Translation: AAS56177.1.
BK006942 Genomic DNA. Translation: DAA08485.1.
PIRiS48414.
RefSeqiNP_012199.3. NM_001179415.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8MNMR-A1-138[»]
2PQNX-ray2.15A1-129[»]
2PQRX-ray1.88A/B1-129[»]
3O48X-ray1.75A1-127[»]
3UUXX-ray3.90A/C1-129[»]
ProteinModelPortaliP40515.
SMRiP40515. Positions 5-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34927. 103 interactions.
DIPiDIP-1897N.
IntActiP40515. 6 interactions.
MINTiMINT-398816.

PTM databases

iPTMnetiP40515.

Proteomic databases

MaxQBiP40515.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL065C; YIL065C; YIL065C.
GeneIDi854745.
KEGGisce:YIL065C.

Organism-specific databases

EuPathDBiFungiDB:YIL065C.
SGDiS000001327. FIS1.

Phylogenomic databases

GeneTreeiENSGT00390000000592.
HOGENOMiHOG000165386.
InParanoidiP40515.
KOiK17969.
OMAiYYLTIGC.
OrthoDBiEOG7N0CHT.

Enzyme and pathway databases

BioCyciYEAST:G3O-31333-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP40515.
PROiP40515.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR016543. Fis1.
IPR028061. Fis1_TPR_C.
IPR028058. Fis1_TPR_N.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13247. PTHR13247. 1 hit.
PfamiPF14853. Fis1_TPR_C. 1 hit.
PF14852. Fis1_TPR_N. 1 hit.
[Graphical view]
PIRSFiPIRSF008835. TPR_repeat_11_Fis1. 1 hit.
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p."
    Mozdy A.D., McCaffery J.M., Shaw J.M.
    J. Cell Biol. 151:367-380(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division."
    Tieu Q., Nunnari J.
    J. Cell Biol. 151:353-366(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission."
    Tieu Q., Okreglak V., Naylor K., Nunnari J.
    J. Cell Biol. 158:445-452(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDV1, MUTAGENESIS OF LEU-80.
  7. "Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae."
    Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.
    J. Biol. Chem. 278:8219-8223(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p."
    Jakobs S., Martini N., Schauss A.C., Egner A., Westermann B., Hell S.W.
    J. Cell Sci. 116:2005-2014(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria."
    Cerveny K.L., Jensen R.E.
    Mol. Biol. Cell 14:4126-4139(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNM1 AND MDV1.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  12. "Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
    Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
    Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission."
    Suzuki M., Neutzner A., Tjandra N., Youle R.J.
    J. Biol. Chem. 280:21444-21452(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiFIS1_YEAST
AccessioniPrimary (citable) accession number: P40515
Secondary accession number(s): D6VVL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2410 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.