FIS1_MOUSE
ID FIS1_MOUSE Reviewed; 152 AA.
AC Q9CQ92;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Mitochondrial fission 1 protein;
DE AltName: Full=FIS1 homolog;
DE AltName: Full=Tetratricopeptide repeat protein 11;
DE Short=TPR repeat protein 11;
GN Name=Fis1; Synonyms=Ttc11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Small intestine, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
RN [3]
RP PROTEIN SEQUENCE OF 20-32; 54-64; 72-83 AND 96-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=23283981; DOI=10.1091/mbc.e12-10-0721;
RA Loson O.C., Song Z., Chen H., Chan D.C.;
RT "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
RT fission.";
RL Mol. Biol. Cell 24:659-667(2013).
RN [6]
RP STRUCTURE BY NMR.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-001, a FIS1p-like and CGI-135 homologous
RT domain from a mouse cDNA.";
RL Submitted (AUG-2002) to the PDB data bank.
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. May be
CC not essential for the assembly of functional fission complexes and the
CC subsequent membrane scission event. Can induce cytochrome c release
CC from the mitochondrion to the cytosol, ultimately leading to apoptosis.
CC Also mediates peroxisomal fission. {ECO:0000269|PubMed:23283981}.
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; Single-pass
CC membrane protein. Peroxisome membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by MARCHF5. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR EMBL; AK004479; BAB23324.1; -; mRNA.
DR EMBL; AK004917; BAB23668.1; -; mRNA.
DR EMBL; AK008078; BAB25445.1; -; mRNA.
DR EMBL; AK008323; BAB25601.1; -; mRNA.
DR EMBL; AK008916; BAB25966.1; -; mRNA.
DR EMBL; BC010783; AAH10783.1; -; mRNA.
DR CCDS; CCDS19757.1; -.
DR RefSeq; NP_001156715.1; NM_001163243.1.
DR RefSeq; NP_079838.1; NM_025562.3.
DR PDB; 1IYG; NMR; -; A=1-120.
DR PDBsum; 1IYG; -.
DR AlphaFoldDB; Q9CQ92; -.
DR SMR; Q9CQ92; -.
DR BioGRID; 211472; 13.
DR IntAct; Q9CQ92; 2.
DR MINT; Q9CQ92; -.
DR STRING; 10090.ENSMUSP00000019198; -.
DR iPTMnet; Q9CQ92; -.
DR PhosphoSitePlus; Q9CQ92; -.
DR SwissPalm; Q9CQ92; -.
DR EPD; Q9CQ92; -.
DR jPOST; Q9CQ92; -.
DR MaxQB; Q9CQ92; -.
DR PaxDb; Q9CQ92; -.
DR PeptideAtlas; Q9CQ92; -.
DR PRIDE; Q9CQ92; -.
DR ProteomicsDB; 267589; -.
DR TopDownProteomics; Q9CQ92; -.
DR DNASU; 66437; -.
DR Ensembl; ENSMUST00000019198; ENSMUSP00000019198; ENSMUSG00000019054.
DR GeneID; 66437; -.
DR KEGG; mmu:66437; -.
DR UCSC; uc009abf.2; mouse.
DR CTD; 51024; -.
DR MGI; MGI:1913687; Fis1.
DR VEuPathDB; HostDB:ENSMUSG00000019054; -.
DR eggNOG; KOG3364; Eukaryota.
DR GeneTree; ENSGT00390000000592; -.
DR HOGENOM; CLU_104368_1_0_1; -.
DR InParanoid; Q9CQ92; -.
DR OMA; VTIQTKF; -.
DR OrthoDB; 1595957at2759; -.
DR PhylomeDB; Q9CQ92; -.
DR TreeFam; TF315180; -.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 66437; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Fis1; mouse.
DR EvolutionaryTrace; Q9CQ92; -.
DR PRO; PR:Q9CQ92; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CQ92; protein.
DR Bgee; ENSMUSG00000019054; Expressed in dorsal pancreas and 245 other tissues.
DR ExpressionAtlas; Q9CQ92; baseline and differential.
DR Genevisible; Q9CQ92; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:MGI.
DR GO; GO:1901653; P:cellular response to peptide; ISO:MGI.
DR GO; GO:1904579; P:cellular response to thapsigargin; ISO:MGI.
DR GO; GO:0000266; P:mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:1903579; P:negative regulation of ATP metabolic process; ISO:MGI.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:MGI.
DR GO; GO:2000192; P:negative regulation of fatty acid transport; ISO:MGI.
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:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:MGI.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
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 3D-structure; Acetylation; Apoptosis; Direct protein sequencing; Membrane;
KW Mitochondrion; 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_0000106394"
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 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 HELIX 2..6
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 11..27
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1IYG"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:1IYG"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:1IYG"
SQ SEQUENCE 152 AA; 17009 MW; B012DF491518A4B1 CRC64;
MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNED IRRGIVLLEE
LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK
DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS
