P84817 (FIS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 UniProtKB Q9Y3D6
Subunit structure	Interacts with DNM1L/DLP1 through the TPR region. Interacts with MARCH5 By similarity. Interacts with MID51 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 process	Apoptosis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane Peroxisome
Coding sequence diversity	Alternative splicing
Domain	TPR repeat Transmembrane Transmembrane helix
PTM	Acetylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB calcium-mediated signaling using intracellular calcium source Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara elevation of mitochondrial calcium ion concentration Inferred from electronic annotation. Source: Compara mitochondrial fission Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial fragmentation involved in apoptotic process Inferred from electronic annotation. Source: Compara mitochondrion degradation Inferred from electronic annotation. Source: Compara mitochondrion morphogenesis Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of intrinsic apoptotic signaling pathway Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara protein targeting to mitochondrion Inferred from electronic annotation. Source: Compara reduction of endoplasmic reticulum calcium ion concentration Inferred from electronic annotation. Source: Compara regulation of mitochondrion organization Inferred from electronic annotation. Source: Compara release of cytochrome c from mitochondria Inferred from electronic annotation. Source: Compara
Cellular_component	integral to mitochondrial outer membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to peroxisomal membrane Inferred from sequence or structural similarity. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 152	152	Mitochondrial fission 1 protein		PRO_0000233948
Regions
	Topological domain	1 – 122	122	Cytoplasmic Potential
	Transmembrane	123 – 143	21	Helical; Potential
	Topological domain	144 – 152	9	Mitochondrial intermembrane Potential
	Repeat	71 – 104	34	TPR
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity UniProtKB Q9Y3D6
Natural variations
	Alternative sequence	1 – 15	15	MEAVL…VEDLK → MPRDEAAR in isoform 2 and isoform 3.		VSP_039625
	Alternative sequence	121 – 152	32	DGLVG…SKSKS → GDRPHAVCSSSSLRPGPWEH CPHPLHTHSPLSNLPSKGLG SPGAPTLRLYIQVPLFCGGE CGQGRG in isoform 2.		VSP_039626
Experimental info
	Mutagenesis	77	1	L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-84; A-91; A-97 and A-98. Ref.1
	Mutagenesis	84	1	L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-91; A-97 and A-98. Ref.1
	Mutagenesis	91	1	L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-97 and A-98. Ref.1
	Mutagenesis	97	1	L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-91 and A-98. Ref.1
	Mutagenesis	98	1	L → A: Loss of mitochondrial fission-stimulating activity; when associated with A-77; A-84; A-91 and A-97. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: 50068E0C0148B1B0	FASTA	152	16,995
	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
	Isoform 2 [UniParc]. Checksum: 09E996033486C0FA	FASTA	179	20,246
	10 20 30 40 50 60 MPRDEAARNF ERKFQSEQAA GSVSKSTQFE YAWCLVRSKY NDDIRRGIVL LEELLPKGSK 70 80 90 100 110 120 EEQRDYVFYL AVGNYRLKEY EKALKYVRGL LQTEPQNNQA KELERLIDKA MKKGDRPHAV 130 140 150 160 170 CSSSSLRPGP WEHCPHPLHT HSPLSNLPSK GLGSPGAPTL RLYIQVPLFC GGECGQGRG
	Isoform 3 [UniParc]. Checksum: 6D024F4B7CC6C17D	FASTA	145	16,251
	10 20 30 40 50 60 MPRDEAARNF ERKFQSEQAA GSVSKSTQFE YAWCLVRSKY NDDIRRGIVL LEELLPKGSK 70 80 90 100 110 120 EEQRDYVFYL AVGNYRLKEY EKALKYVRGL LQTEPQNNQA KELERLIDKA MKKDGLVGMA 130 140 IVGGMALGVA GLAGLIGLAV SKSKS

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00371036. IPI00896755. IPI00951200.
RefSeq	NP_001099389.1. NM_001105919.1.
UniGene	Rn.1298.
3D structure databases
ProteinModelPortal	P84817.
SMR	P84817. Positions 1-145.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000060173.
Proteomic databases
PaxDb	P84817.
PRIDE	P84817.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000001924; ENSRNOP00000001924; ENSRNOG00000001420. ENSRNOT00000063901; ENSRNOP00000061895; ENSRNOG00000001420.
GeneID	288584.
KEGG	rno:288584.
UCSC	RGD:1306668. rat.
Organism-specific databases
CTD	51024.
RGD	1306668. Fis1.
Phylogenomic databases
eggNOG	NOG235677.
GeneTree	ENSGT00390000000592.
HOGENOM	HOG000165386.
HOVERGEN	HBG081530.
InParanoid	P84817.
OMA	DKALKKD.
Gene expression databases
Genevestigator	P84817.
GermOnline	ENSRNOG00000001420. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.40.10. 1 hit.
InterPro	IPR016543. Tetratricopeptide_rpt_11_Fis1. IPR011990. TPR-like_helical. [Graphical view]
PANTHER	PTHR13247. PTHR13247. 1 hit.
PIRSF	PIRSF008835. TPR_repeat_11_Fis1. 1 hit.
PROSITE	PS50005. TPR. False negative. PS50293. TPR_REGION. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	628350.

Entry information

Entry name

FIS1_RAT

Accession

Primary (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:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program