ID FIS1_HUMAN Reviewed; 152 AA. AC Q9Y3D6; Q9BTP3; DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2003, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Mitochondrial fission 1 protein; DE AltName: Full=FIS1 homolog; DE Short=hFis1; DE AltName: Full=Tetratricopeptide repeat protein 11; DE Short=TPR repeat protein 11; GN Name=FIS1; Synonyms=TTC11; ORFNames=CGI-135; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 [4] RP PROTEIN SEQUENCE OF 1-16, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUN-2005) to UniProtKB. RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12783892; DOI=10.1074/jbc.m303758200; RA James D.I., Parone P.A., Mattenberger Y., Martinou J.-C.; RT "hFis1, a novel component of the mammalian mitochondrial fission RT machinery."; RL J. Biol. Chem. 278:36373-36379(2003). RN [6] RP FUNCTION, AND INTERACTION WITH DNM1L. RX PubMed=12861026; DOI=10.1128/mcb.23.15.5409-5420.2003; RA Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A.; RT "The mitochondrial protein hFis1 regulates mitochondrial fission in RT mammalian cells through an interaction with the dynamin-like protein RT DLP1."; RL Mol. Cell. Biol. 23:5409-5420(2003). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF LYS-149 AND RP LYS-151. RX PubMed=14996942; DOI=10.1242/jcs.01058; RA Stojanovski D., Koutsopoulos O.S., Okamoto K., Ryan M.T.; RT "Levels of human Fis1 at the mitochondrial outer membrane regulate RT mitochondrial morphology."; RL J. Cell Sci. 117:1201-1210(2004). RN [8] RP FUNCTION, INTERACTION WITH DNM1L, AND MUTAGENESIS OF LEU-14; LEU-42; RP LEU-58; LEU-77; LEU-91 AND LEU-110. RX PubMed=16118244; DOI=10.1242/jcs.02537; RA Yu T., Fox R.J., Burwell L.S., Yoon Y.; RT "Regulation of mitochondrial fission and apoptosis by the mitochondrial RT outer membrane protein hFis1."; RL J. Cell Sci. 118:4141-4151(2005). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16107562; DOI=10.1091/mbc.e05-02-0159; RA Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., Schrader M.; RT "A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian RT cells."; RL Mol. Biol. Cell 16:5077-5086(2005). RN [10] RP UBIQUITINATION BY MARCHF5, AND INTERACTION WITH MARCHF5. RX PubMed=16874301; DOI=10.1038/sj.emboj.7601249; RA Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., RA Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S.; RT "A novel mitochondrial ubiquitin ligase plays a critical role in RT mitochondrial dynamics."; RL EMBO J. 25:3618-3626(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP INTERACTION WITH PEX11A; PEX11B AND PEX11G. RX PubMed=20826455; DOI=10.1242/jcs.064907; RA Koch J., Pranjic K., Huber A., Ellinger A., Hartig A., Kragler F., RA Brocard C.; RT "PEX11 family members are membrane elongation factors that coordinate RT peroxisome proliferation and maintenance."; RL J. Cell Sci. 123:3389-3400(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP INTERACTION WITH MIEF1. RX PubMed=21701560; DOI=10.1038/emboj.2011.198; RA Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., RA Shupliakov O., Lendahl U., Nister M.; RT "Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes RT mitochondrial fusion rather than fission."; RL EMBO J. 30:2762-2778(2011). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=23921378; DOI=10.1074/jbc.m113.479873; RA Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., RA Ryan M.T.; RT "MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment RT and are specific for mitochondrial fission."; RL J. Biol. Chem. 288:27584-27593(2013). RN [16] 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 [17] RP FUNCTION. RX PubMed=23530241; DOI=10.1073/pnas.1300855110; RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.; RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for RT membrane scission."; RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-123. RX PubMed=14705031; DOI=10.1002/prot.10524; RA Dohm J.A., Lee S.J., Hardwick J.M., Hill R.B., Gittis A.G.; RT "Cytosolic domain of the human mitochondrial fission protein fis1 adopts a RT TPR fold."; RL Proteins 54:153-156(2004). RN [21] RP STRUCTURE BY NMR, AND SUBCELLULAR LOCATION. RX PubMed=14623186; DOI=10.1016/j.jmb.2003.09.064; RA Suzuki M., Jeong S.-Y., Karbowski M., Youle R.J., Tjandra N.; RT "The solution structure of human mitochondria fission protein Fis1 reveals RT a novel TPR-like helix bundle."; RL J. Mol. Biol. 334:445-458(2003). RN [22] RP FUNCTION, AND INTERACTION WITH DNM1L. RX PubMed=24196833; DOI=10.1091/mbc.e13-09-0525; RA Shen Q., Yamano K., Head B.P., Kawajiri S., Cheung J.T., Wang C., Cho J.H., RA Hattori N., Youle R.J., van der Bliek A.M.; RT "Mutations in Fis1 disrupt orderly disposal of defective mitochondria."; RL Mol. Biol. Cell 25:145-159(2014). CC -!- FUNCTION: Involved in the fragmentation of the mitochondrial network CC and its perinuclear clustering (PubMed:12783892, PubMed:12861026, CC PubMed:14996942, PubMed:23283981). Plays a minor role in the CC recruitment and association of the fission mediator dynamin-related CC protein 1 (DNM1L) to the mitochondrial surface and mitochondrial CC fission (PubMed:12861026, PubMed:16118244, PubMed:23283981, CC PubMed:23530241, PubMed:24196833). May not be essential for the CC assembly of functional fission complexes and the subsequent membrane CC scission event (PubMed:23530241, PubMed:24196833). Also mediates CC peroxisomal fission (PubMed:16107562). May act when the products of CC fission are directed toward mitochondrial homeostasis, mitophagy, or CC apoptosis (PubMed:24196833). Can induce cytochrome c release from the CC mitochondrion to the cytosol, ultimately leading to apoptosis CC (PubMed:12783892). {ECO:0000269|PubMed:12783892, CC ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:14996942, CC ECO:0000269|PubMed:16107562, ECO:0000269|PubMed:16118244, CC ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:23530241, CC ECO:0000269|PubMed:24196833}. CC -!- SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region; may form CC part of a larger protein complex at the endoplasmic reticulum- CC mitochondrial interface during mitochondrial fission (PubMed:12861026, CC PubMed:16118244, PubMed:24196833). Interacts with MARCHF5 CC (PubMed:16874301). Interacts with MIEF1 (PubMed:21701560). Interacts CC with PEX11A, PEX11B and PEX11G (PubMed:20826455). CC {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:16118244, CC ECO:0000269|PubMed:16874301, ECO:0000269|PubMed:20826455, CC ECO:0000269|PubMed:21701560, ECO:0000269|PubMed:24196833}. CC -!- INTERACTION: CC Q9Y3D6; Q9BV23: ABHD6; NbExp=3; IntAct=EBI-3385283, EBI-3916106; CC Q9Y3D6; Q96BI3: APH1A; NbExp=3; IntAct=EBI-3385283, EBI-2606935; CC Q9Y3D6; P51572: BCAP31; NbExp=8; IntAct=EBI-3385283, EBI-77683; CC Q9Y3D6; O00429: DNM1L; NbExp=2; IntAct=EBI-3385283, EBI-724571; CC Q9Y3D6; Q15125: EBP; NbExp=3; IntAct=EBI-3385283, EBI-3915253; CC Q9Y3D6; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3385283, EBI-781551; CC Q9Y3D6; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3385283, EBI-18304435; CC Q9Y3D6; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-3385283, EBI-18938272; CC Q9Y3D6; O15552: FFAR2; NbExp=3; IntAct=EBI-3385283, EBI-2833872; CC Q9Y3D6; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3385283, EBI-10266796; CC Q9Y3D6; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-3385283, EBI-749265; CC Q9Y3D6; P48051: KCNJ6; NbExp=3; IntAct=EBI-3385283, EBI-12017638; CC Q9Y3D6; Q9NQG6: MIEF1; NbExp=4; IntAct=EBI-3385283, EBI-740987; CC Q9Y3D6; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-3385283, EBI-6163737; CC Q9Y3D6; Q9HC29: NOD2; NbExp=2; IntAct=EBI-3385283, EBI-7445625; CC Q9Y3D6; P57054: PIGP; NbExp=3; IntAct=EBI-3385283, EBI-17630288; CC Q9Y3D6; Q6P5S7: RNASEK; NbExp=3; IntAct=EBI-3385283, EBI-18397230; CC Q9Y3D6; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-3385283, EBI-17247926; CC Q9Y3D6; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3385283, EBI-18159983; CC Q9Y3D6; Q13336-2: SLC14A1; NbExp=3; IntAct=EBI-3385283, EBI-19141793; CC Q9Y3D6; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-3385283, EBI-8638294; CC Q9Y3D6; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-3385283, EBI-11724433; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:12783892, ECO:0000269|PubMed:14623186, CC ECO:0000269|PubMed:14996942, ECO:0000269|PubMed:16107562}; Single-pass CC membrane protein {ECO:0000269|PubMed:14996942}. Peroxisome membrane CC {ECO:0000269|PubMed:16107562}; Single-pass membrane protein CC {ECO:0000305|PubMed:16107562}. 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:0000269|PubMed:12861026, ECO:0000269|PubMed:16107562, CC ECO:0000269|PubMed:16118244}. CC -!- PTM: Ubiquitinated by MARCHF5. {ECO:0000269|PubMed:16874301}. CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF151893; AAD34130.1; -; mRNA. DR EMBL; AC006329; AAP22366.1; -; Genomic_DNA. DR EMBL; BC003540; AAH03540.1; -; mRNA. DR EMBL; BC009428; AAH09428.1; -; mRNA. DR CCDS; CCDS43626.1; -. DR RefSeq; NP_057152.2; NM_016068.2. DR PDB; 1NZN; X-ray; 2.00 A; A=1-123. DR PDB; 1PC2; NMR; -; A=1-145. DR PDB; 7YA9; X-ray; 1.70 A; A=1-123. DR PDB; 7YKA; X-ray; 2.30 A; A=2-119, B=2-123. DR PDBsum; 1NZN; -. DR PDBsum; 1PC2; -. DR PDBsum; 7YA9; -. DR PDBsum; 7YKA; -. DR AlphaFoldDB; Q9Y3D6; -. DR SMR; Q9Y3D6; -. DR BioGRID; 119230; 223. DR CORUM; Q9Y3D6; -. DR IntAct; Q9Y3D6; 37. DR MINT; Q9Y3D6; -. DR STRING; 9606.ENSP00000223136; -. DR iPTMnet; Q9Y3D6; -. DR PhosphoSitePlus; Q9Y3D6; -. DR SwissPalm; Q9Y3D6; -. DR BioMuta; FIS1; -. DR DMDM; 33112470; -. DR EPD; Q9Y3D6; -. DR jPOST; Q9Y3D6; -. DR MassIVE; Q9Y3D6; -. DR MaxQB; Q9Y3D6; -. DR PaxDb; 9606-ENSP00000223136; -. DR PeptideAtlas; Q9Y3D6; -. DR ProteomicsDB; 86022; -. DR Pumba; Q9Y3D6; -. DR TopDownProteomics; Q9Y3D6; -. DR Antibodypedia; 2313; 444 antibodies from 38 providers. DR DNASU; 51024; -. DR Ensembl; ENST00000223136.5; ENSP00000223136.4; ENSG00000214253.9. DR GeneID; 51024; -. DR KEGG; hsa:51024; -. DR MANE-Select; ENST00000223136.5; ENSP00000223136.4; NM_016068.3; NP_057152.2. DR UCSC; uc003uyj.5; human. DR AGR; HGNC:21689; -. DR CTD; 51024; -. DR DisGeNET; 51024; -. DR GeneCards; FIS1; -. DR HGNC; HGNC:21689; FIS1. DR HPA; ENSG00000214253; Low tissue specificity. DR MIM; 609003; gene. DR neXtProt; NX_Q9Y3D6; -. DR OpenTargets; ENSG00000214253; -. DR PharmGKB; PA134984211; -. DR VEuPathDB; HostDB:ENSG00000214253; -. DR eggNOG; KOG3364; Eukaryota. DR GeneTree; ENSGT00390000000592; -. DR HOGENOM; CLU_104368_1_0_1; -. DR InParanoid; Q9Y3D6; -. DR OMA; QFNYAWG; -. DR OrthoDB; 2997323at2759; -. DR PhylomeDB; Q9Y3D6; -. DR TreeFam; TF315180; -. DR PathwayCommons; Q9Y3D6; -. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; Q9Y3D6; -. DR SIGNOR; Q9Y3D6; -. DR BioGRID-ORCS; 51024; 185 hits in 1157 CRISPR screens. DR ChiTaRS; FIS1; human. DR EvolutionaryTrace; Q9Y3D6; -. DR GeneWiki; FIS1; -. DR GenomeRNAi; 51024; -. DR Pharos; Q9Y3D6; Tbio. DR PRO; PR:Q9Y3D6; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9Y3D6; Protein. DR Bgee; ENSG00000214253; Expressed in C1 segment of cervical spinal cord and 200 other cell types or tissues. DR ExpressionAtlas; Q9Y3D6; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0008289; F:lipid binding; EXP:DisProt. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0000422; P:autophagy of mitochondrion; IDA:UniProtKB. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB. DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB. DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB. DR GO; GO:1903579; P:negative regulation of ATP metabolic process; IMP:ARUK-UCL. DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IMP:UniProtKB. DR GO; GO:2000192; P:negative regulation of fatty acid transport; IMP:ARUK-UCL. DR GO; GO:0016559; P:peroxisome fission; IDA:UniProtKB. DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IMP:UniProtKB. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB. DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:UniProtKB. DR CDD; cd12212; Fis1; 1. DR DisProt; DP00457; -. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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:SF0; MITOCHONDRIAL FISSION 1 PROTEIN; 1. DR PANTHER; PTHR13247; TETRATRICOPEPTIDE REPEAT PROTEIN 11 TPR REPEAT PROTEIN 11; 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; TPR-like; 1. DR UCD-2DPAGE; Q9Y3D6; -. DR Genevisible; Q9Y3D6; HS. 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_0000106393" 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:0000269|Ref.4, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:25944712" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MUTAGEN 14 FT /note="L->P: Approximately 40% of cells display fragmented FT mitochondria." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 42 FT /note="L->P: Less than 15% of cells display fragmented FT mitochondria." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 58 FT /note="L->P: Less than 15% of cells display fragmented FT mitochondria." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 77 FT /note="L->P: Less than 15% of cells display fragmented FT mitochondria. Shows greatly reduced binding to DNM1L." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 91 FT /note="L->P: Less than 15% of cells display fragmented FT mitochondria. Shows greatly reduced binding to DNM1L." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 110 FT /note="L->P: Approximately 40% of cells display fragmented FT mitochondria. No change in binding to DNM1L." FT /evidence="ECO:0000269|PubMed:16118244" FT MUTAGEN 149 FT /note="K->A: Protein localizes to both mitochondrion and FT endoplasmic reticulum. Protein localizes to endoplasmic FT reticulum only; when associated with A-151." FT /evidence="ECO:0000269|PubMed:14996942" FT MUTAGEN 151 FT /note="K->A: Protein localizes to both mitochondrion and FT endoplasmic reticulum. Protein localizes to endoplasmic FT reticulum only; when associated with A-149." FT /evidence="ECO:0000269|PubMed:14996942" FT CONFLICT 45..46 FT /note="SK -> TR (in Ref. 1; AAD34130)" FT /evidence="ECO:0000305" FT HELIX 1..27 FT /evidence="ECO:0007829|PDB:1NZN" FT HELIX 32..42 FT /evidence="ECO:0007829|PDB:1NZN" FT STRAND 45..47 FT /evidence="ECO:0007829|PDB:1NZN" FT HELIX 48..61 FT /evidence="ECO:0007829|PDB:1NZN" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:1NZN" FT HELIX 67..83 FT /evidence="ECO:0007829|PDB:1NZN" FT HELIX 87..100 FT /evidence="ECO:0007829|PDB:1NZN" FT HELIX 105..120 FT /evidence="ECO:0007829|PDB:1NZN" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:1PC2" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1PC2" SQ SEQUENCE 152 AA; 16938 MW; 6E76EC02B3731A9B CRC64; MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS //