FIS1_RAT
ID FIS1_RAT Reviewed; 152 AA.
AC P84817; B2RZ80; D4A5K3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Mitochondrial fission 1 protein;
DE AltName: Full=FIS1 homolog;
DE Short=rFis1;
DE AltName: Full=Tetratricopeptide repeat protein 11;
DE Short=TPR repeat protein 11;
GN Name=Fis1 {ECO:0000250|UniProtKB:Q9Y3D6};
GN Synonyms=Ttc11 {ECO:0000312|RGD:1306668};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-77; LEU-84; LEU-91; LEU-97 AND LEU-98.
RC TISSUE=Liver {ECO:0000269|PubMed:15979461};
RX PubMed=15979461; DOI=10.1016/j.bbrc.2005.05.154;
RA Jofuku A., Ishihara N., Mihara K.;
RT "Analysis of functional domains of rat mitochondrial Fis1, the
RT mitochondrial fission-stimulating protein.";
RL Biochem. Biophys. Res. Commun. 333:650-659(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Involved in the fragmentation of the mitochondrial network
CC and its perinuclear clustering. Plays a minor role in the recruitment
CC and association of the fission mediator dynamin-related protein 1
CC (DNM1L) to the mitochondrial surface and mitochondrial fission. Can
CC induce cytochrome c release from the mitochondrion to the cytosol,
CC ultimately leading to apoptosis. Also mediates peroxisomal fission (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:15979461}.
CC -!- SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region. Interacts
CC with MARCHF5. Interacts with MIEF1. Interacts with PEX11A, PEX11B and
CC PEX11G. {ECO:0000250|UniProtKB:Q9Y3D6}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:15979461}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15979461}. Peroxisome membrane
CC {ECO:0000269|PubMed:15979461}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15979461}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P84817-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P84817-2; Sequence=VSP_039625, VSP_039626;
CC Name=3;
CC IsoId=P84817-3; Sequence=VSP_039625;
CC -!- DOMAIN: The C-terminus is required for mitochondrial or peroxisomal
CC localization, while the N-terminus is necessary for mitochondrial or
CC peroxisomal fission, localization and regulation of the interaction
CC with DNM1L.
CC -!- PTM: Ubiquitinated by MARCHF5. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR EMBL; AC111745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473973; EDM13301.1; -; Genomic_DNA.
DR EMBL; BC167057; AAI67057.1; -; mRNA.
DR RefSeq; NP_001099389.1; NM_001105919.1. [P84817-3]
DR RefSeq; XP_006249184.1; XM_006249122.3. [P84817-2]
DR RefSeq; XP_006249185.1; XM_006249123.3. [P84817-1]
DR AlphaFoldDB; P84817; -.
DR SMR; P84817; -.
DR BioGRID; 252608; 1.
DR STRING; 10116.ENSRNOP00000061895; -.
DR iPTMnet; P84817; -.
DR PhosphoSitePlus; P84817; -.
DR SwissPalm; P84817; -.
DR jPOST; P84817; -.
DR PaxDb; P84817; -.
DR PRIDE; P84817; -.
DR Ensembl; ENSRNOT00000001924; ENSRNOP00000001924; ENSRNOG00000001420. [P84817-1]
DR Ensembl; ENSRNOT00000063901; ENSRNOP00000061895; ENSRNOG00000001420. [P84817-2]
DR GeneID; 288584; -.
DR KEGG; rno:288584; -.
DR UCSC; RGD:1306668; rat. [P84817-1]
DR CTD; 51024; -.
DR RGD; 1306668; Fis1.
DR eggNOG; KOG3364; Eukaryota.
DR GeneTree; ENSGT00390000000592; -.
DR HOGENOM; CLU_1503028_0_0_1; -.
DR InParanoid; P84817; -.
DR OMA; VTIQTKF; -.
DR OrthoDB; 1595957at2759; -.
DR PhylomeDB; P84817; -.
DR TreeFam; TF315180; -.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:P84817; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Proteomes; UP000234681; Chromosome 12.
DR Bgee; ENSRNOG00000001420; Expressed in duodenum and 19 other tissues.
DR Genevisible; P84817; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IDA:RGD.
DR GO; GO:1904579; P:cellular response to thapsigargin; IMP:RGD.
DR GO; GO:0097237; P:cellular response to toxic substance; IEP:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:1903579; P:negative regulation of ATP metabolic process; ISO:RGD.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:RGD.
DR GO; GO:2000192; P:negative regulation of fatty acid transport; ISO:RGD.
DR GO; GO:0016559; P:peroxisome fission; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:RGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:1905395; P:response to flavonoid; IEP:RGD.
DR GO; GO:1902617; P:response to fluoride; IEP:RGD.
DR GO; GO:1990910; P:response to hypobaric hypoxia; IEP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR CDD; cd12212; Fis1; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR016543; Fis1.
DR InterPro; IPR033745; Fis1_cytosol.
DR InterPro; IPR028061; Fis1_TPR_C.
DR InterPro; IPR028058; Fis1_TPR_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13247; PTHR13247; 1.
DR Pfam; PF14853; Fis1_TPR_C; 1.
DR Pfam; PF14852; Fis1_TPR_N; 1.
DR PIRSF; PIRSF008835; TPR_repeat_11_Fis1; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; TPR repeat; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..152
FT /note="Mitochondrial fission 1 protein"
FT /id="PRO_0000233948"
FT TOPO_DOM 1..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..152
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 71..104
FT /note="TPR"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3D6"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3D6"
FT VAR_SEQ 1..15
FT /note="MEAVLNELVSVEDLK -> MPRDEAAR (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039625"
FT VAR_SEQ 121..152
FT /note="DGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS -> GDRPHAVCSSSSLRPG
FT PWEHCPHPLHTHSPLSNLPSKGLGSPGAPTLRLYIQVPLFCGGECGQGRG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039626"
FT MUTAGEN 77
FT /note="L->A: Loss of mitochondrial fission-stimulating
FT activity; when associated with A-84; A-91; A-97 and A-98."
FT /evidence="ECO:0000269|PubMed:15979461"
FT MUTAGEN 84
FT /note="L->A: Loss of mitochondrial fission-stimulating
FT activity; when associated with A-77; A-91; A-97 and A-98."
FT /evidence="ECO:0000269|PubMed:15979461"
FT MUTAGEN 91
FT /note="L->A: Loss of mitochondrial fission-stimulating
FT activity; when associated with A-77; A-84; A-97 and A-98."
FT /evidence="ECO:0000269|PubMed:15979461"
FT MUTAGEN 97
FT /note="L->A: Loss of mitochondrial fission-stimulating
FT activity; when associated with A-77; A-84; A-91 and A-98."
FT /evidence="ECO:0000269|PubMed:15979461"
FT MUTAGEN 98
FT /note="L->A: Loss of mitochondrial fission-stimulating
FT activity; when associated with A-77; A-84; A-91 and A-97."
FT /evidence="ECO:0000269|PubMed:15979461"
SQ SEQUENCE 152 AA; 16995 MW; 50068E0C0148B1B0 CRC64;
MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNDD IRRGIVLLEE
LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK
DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS
