FIS1_HUMAN
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 03-AUG-2022, entry version 191.
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).
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.
CC {ECO:0000269|PubMed:12783892, ECO:0000269|PubMed:12861026,
CC ECO:0000269|PubMed:14996942, ECO:0000269|PubMed:16107562,
CC ECO:0000269|PubMed:16118244, ECO:0000269|PubMed:23283981,
CC ECO:0000269|PubMed:23530241}.
CC -!- SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region. Interacts
CC with MARCHF5. Interacts with MIEF1. Interacts with PEX11A, PEX11B and
CC PEX11G (PubMed:20826455). {ECO:0000269|PubMed:12861026,
CC ECO:0000269|PubMed:16118244, ECO:0000269|PubMed:16874301,
CC ECO:0000269|PubMed:20826455, ECO:0000269|PubMed:21701560}.
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; Single-pass
CC membrane protein. Peroxisome membrane; Single-pass membrane protein.
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:0000269|PubMed:16874301}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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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 PDBsum; 1NZN; -.
DR PDBsum; 1PC2; -.
DR AlphaFoldDB; Q9Y3D6; -.
DR SMR; Q9Y3D6; -.
DR BioGRID; 119230; 217.
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 UCD-2DPAGE; Q9Y3D6; -.
DR EPD; Q9Y3D6; -.
DR jPOST; Q9Y3D6; -.
DR MassIVE; Q9Y3D6; -.
DR MaxQB; Q9Y3D6; -.
DR PaxDb; Q9Y3D6; -.
DR PeptideAtlas; Q9Y3D6; -.
DR PRIDE; Q9Y3D6; -.
DR ProteomicsDB; 86022; -.
DR TopDownProteomics; Q9Y3D6; -.
DR Antibodypedia; 2313; 378 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 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; VTIQTKF; -.
DR OrthoDB; 1595957at2759; -.
DR PhylomeDB; Q9Y3D6; -.
DR TreeFam; TF315180; -.
DR PathwayCommons; Q9Y3D6; -.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; Q9Y3D6; -.
DR BioGRID-ORCS; 51024; 182 hits in 1078 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 198 other tissues.
DR ExpressionAtlas; Q9Y3D6; baseline and differential.
DR Genevisible; Q9Y3D6; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:GOC.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
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: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:0070584; P:mitochondrion morphogenesis; 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; -; 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_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
