Mitochondria fission 1 protein - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40515 (FIS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mitochondria fission 1 protein

Alternative name(s):
Mitochondrial division protein 2

Gene names

Name:	FIS1
Synonyms:	MDV2
Ordered Locus Names:	YIL065C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.5 Ref.6 Ref.8
Subunit structure	Interacts with DNM1 and MDV1. Ref.6 Ref.9
Subcellular location	Mitochondrion outer membrane; Single-pass membrane protein Ref.1 Ref.7 Ref.11.
Domain	The C-terminus is required for mitochondrial localization, while the N-teminus is necessary for mitochondrial fission By similarity.
Miscellaneous	Present with 2410 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the FIS1 family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW chronological cell aging Inferred from mutant phenotype. Source: SGD mitochondrial fission Inferred from mutant phenotype Ref.5 Ref.1. Source: SGD peroxisome fission Inferred from genetic interaction. Source: SGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from direct assay Ref.1 Ref.12. Source: SGD peroxisome Inferred from direct assay. Source: SGD
Molecular function	binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 155

155

Mitochondria fission 1 protein

PRO_0000202982

Regions

Topological domain

1 – 131

131

Cytoplasmic Potential

Transmembrane

132 – 149

Helical; Potential

Topological domain

150 – 155

Mitochondrial intermembrane Potential

Experimental info

Mutagenesis

L → P in fis1-L80P; no interaction with MDV1; mitochondrial fission is blocked; DNM1 assembly at punctate structures normal as in wild-type. Ref.6

Secondary structure

155

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P40515 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BD62D19524770536
Show »

FASTA

155

17,733

        10         20         30         40         50         60 
MTKVDFWPTL KDAYEPLYPQ QLEILRQQVV SEGGPTATIQ SRFNYAWGLI KSTDVNDERL 

        70         80         90        100        110        120 
GVKILTDIYK EAESRRRECL YYLTIGCYKL GEYSMAKRYV DTLFEHERNN KQVGALKSMV 

       130        140        150 
EDKIQKETLK GVVVAGGVLA GAVAVASFFL RNKRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11038183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed: 9169870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 11038182] [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: 12163467] [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: 12514182] [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: 12679388] [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: 14517324] [Abstract] Cited for: INTERACTION WITH DNM1 AND MDV1.
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[12]	"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: 15809300] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z38060 Genomic DNA. Translation: CAA86158.1.
AY557851 Genomic DNA. Translation: AAS56177.1.
BK006942 Genomic DNA. Translation: DAA08485.1.

PIR

S48414.

RefSeq

NP_012199.1. NM_001179415.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y8M	NMR	-	A	1-138	[»]
2PQN	X-ray	2.15	A	1-129	[»]
2PQR	X-ray	1.88	A/B	1-129	[»]
3O48	X-ray	1.75	A	1-127	[»]

ProteinModelPortal

P40515.

SMR

P40515. Positions 5-127.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1897N.

IntAct

P40515. 6 interactions.

MINT

MINT-398816.

STRING

P40515.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL065C; YIL065C; YIL065C.

GeneID

854745.

KEGG

sce:YIL065C.

NMPDR

fig|4932.3.peg.1730.

Organism-specific databases

CYGD

YIL065c.

SGD

S000001327. FIS1.

Phylogenomic databases

eggNOG

fuNOG11658.

GeneTree

EFGT00050000002203.

HOGENOM

HBG397677.

OrthoDB

EOG48WGBP.

Gene expression databases

ArrayExpress

P40515.

Genevestigator

P40515.

GermOnline

YIL065C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016543. Tetratricopeptide_rpt_11_Fis1.
IPR011990. TPR-like_helical.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 1 hit.

PANTHER

PTHR13247. PTHR13247. 1 hit.

PIRSF

PIRSF008835. TPR_repeat_11_Fis1. 1 hit.

ProtoNet

Search...

Other

NextBio

977467.

Entry information

Entry name

FIS1_YEAST

Accession

Primary (citable) accession number: P40515
Secondary accession number(s): D6VVL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents