ID MFF_HUMAN Reviewed; 342 AA. AC Q9GZY8; Q567U1; Q658R6; Q9BVZ1; Q9H690; Q9NRG8; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Mitochondrial fission factor; GN Name=MFF; Synonyms=C2orf33; ORFNames=AD030, AD033, GL004; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY. RX PubMed=18353969; DOI=10.1091/mbc.E07-12-1287; RA Gandre-Babbe S., van der Bliek A.M.; RT "The novel tail-anchored membrane protein Mff controls mitochondrial RT and peroxisomal fission in mammalian cells."; RL Mol. Biol. Cell 19:2402-2412(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Liver; RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.; RT "A novel gene expressed in human liver non-tumor tissues."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adrenal gland; RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-342. RC TISSUE=Stomach; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM RP 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115; SER-155; SER-157; RP THR-200; SER-202; SER-229 AND SER-233, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-146 (ISOFORM 5), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(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., RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-157, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(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 RT recruitment and are specific for mitochondrial fission."; RL J. Biol. Chem. 288:27584-27593(2013). RN [16] RP FUNCTION, AND SUBUNIT. RX PubMed=23530241; DOI=10.1073/pnas.1300855110; RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., RA 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 2), AND RP IDENTIFICATION BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., 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 [19] RP VARIANT [LARGE SCALE ANALYSIS] LYS-29. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in mitochondrial and peroxisomal fission. CC Promotes the recruitment and association of the fission mediator CC dynamin-related protein 1 (DNM1L) to the mitochondrial surface. CC May be involved in regulation of synaptic vesicle membrane CC dynamics by recruitment of DNM1L to clathrin-containing vesicles. CC {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23530241}. CC -!- SUBUNIT: Homodimer. Interacts with DNM1L (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass CC type IV membrane protein. Peroxisome. Cytoplasmic vesicle, CC secretory vesicle, synaptic vesicle {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9GZY8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9GZY8-2; Sequence=VSP_025954, VSP_025957; CC Note=Contains a phosphothreonine at position 149. Contains a CC phosphoserine at position 151. Contains a phosphoserine at CC position 146. {ECO:0000244|PubMed:18669648, CC ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:24275569}; CC Name=3; CC IsoId=Q9GZY8-3; Sequence=VSP_025954, VSP_025958; CC Name=4; CC IsoId=Q9GZY8-4; Sequence=VSP_025954, VSP_025955; CC Name=5; CC IsoId=Q9GZY8-5; Sequence=VSP_025954, VSP_025956; CC Note=Contains a phosphoserine at position 146. CC {ECO:0000244|PubMed:20068231}; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney, liver, CC brain, muscle, and stomach. {ECO:0000269|PubMed:18353969}. CC -!- SIMILARITY: Belongs to the Tango11 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; AK026137; BAB15373.1; -; mRNA. DR EMBL; AF246239; AAG44486.1; -; mRNA. DR EMBL; AF226049; AAF86949.1; -; mRNA. DR EMBL; AF258660; AAG44658.1; -; mRNA. DR EMBL; AC097662; AAY24252.1; -; Genomic_DNA. DR EMBL; BC000797; AAH00797.1; -; mRNA. DR EMBL; BC093024; AAH93024.1; -; mRNA. DR EMBL; AL833032; CAH56328.1; -; mRNA. DR CCDS; CCDS2465.1; -. [Q9GZY8-1] DR CCDS; CCDS63139.1; -. [Q9GZY8-3] DR CCDS; CCDS63140.1; -. [Q9GZY8-2] DR CCDS; CCDS63141.1; -. [Q9GZY8-5] DR CCDS; CCDS63142.1; -. [Q9GZY8-4] DR RefSeq; NP_001263990.1; NM_001277061.1. [Q9GZY8-1] DR RefSeq; NP_001263991.1; NM_001277062.1. [Q9GZY8-2] DR RefSeq; NP_001263992.1; NM_001277063.1. [Q9GZY8-3] DR RefSeq; NP_001263993.1; NM_001277064.1. [Q9GZY8-5] DR RefSeq; NP_001263994.1; NM_001277065.1. [Q9GZY8-4] DR RefSeq; NP_001263995.1; NM_001277066.1. [Q9GZY8-4] DR RefSeq; NP_001263996.1; NM_001277067.1. DR RefSeq; NP_001263997.1; NM_001277068.1. DR RefSeq; NP_064579.3; NM_020194.5. [Q9GZY8-1] DR RefSeq; XP_006712701.1; XM_006712638.1. [Q9GZY8-2] DR RefSeq; XP_006712702.1; XM_006712639.2. [Q9GZY8-5] DR RefSeq; XP_011509802.1; XM_011511500.1. [Q9GZY8-1] DR UniGene; Hs.471528; -. DR ProteinModelPortal; Q9GZY8; -. DR BioGrid; 121271; 9. DR STRING; 9606.ENSP00000302037; -. DR PhosphoSite; Q9GZY8; -. DR BioMuta; MFF; -. DR DMDM; 74725008; -. DR MaxQB; Q9GZY8; -. DR PaxDb; Q9GZY8; -. DR PRIDE; Q9GZY8; -. DR DNASU; 56947; -. DR Ensembl; ENST00000304593; ENSP00000304898; ENSG00000168958. [Q9GZY8-2] DR Ensembl; ENST00000337110; ENSP00000338412; ENSG00000168958. [Q9GZY8-3] DR Ensembl; ENST00000349901; ENSP00000304134; ENSG00000168958. [Q9GZY8-5] DR Ensembl; ENST00000353339; ENSP00000302037; ENSG00000168958. [Q9GZY8-1] DR Ensembl; ENST00000354503; ENSP00000346498; ENSG00000168958. [Q9GZY8-4] DR Ensembl; ENST00000409565; ENSP00000386964; ENSG00000168958. [Q9GZY8-4] DR Ensembl; ENST00000409616; ENSP00000386641; ENSG00000168958. [Q9GZY8-5] DR GeneID; 56947; -. DR KEGG; hsa:56947; -. DR UCSC; uc002vos.4; human. [Q9GZY8-1] DR UCSC; uc002vot.4; human. [Q9GZY8-2] DR UCSC; uc002vow.4; human. [Q9GZY8-3] DR UCSC; uc002voz.4; human. [Q9GZY8-4] DR UCSC; uc021vxu.2; human. [Q9GZY8-5] DR CTD; 56947; -. DR GeneCards; MFF; -. DR HGNC; HGNC:24858; MFF. DR HPA; HPA010968; -. DR MIM; 614785; gene. DR neXtProt; NX_Q9GZY8; -. DR PharmGKB; PA162395839; -. DR eggNOG; ENOG410III7; Eukaryota. DR eggNOG; ENOG410XSQR; LUCA. DR GeneTree; ENSGT00390000009776; -. DR HOGENOM; HOG000285976; -. DR HOVERGEN; HBG105704; -. DR InParanoid; Q9GZY8; -. DR OMA; EINRIQY; -. DR PhylomeDB; Q9GZY8; -. DR TreeFam; TF325506; -. DR ChiTaRS; MFF; human. DR GeneWiki; Mitochondrial_fission_factor; -. DR GenomeRNAi; 56947; -. DR NextBio; 62537; -. DR PRO; PR:Q9GZY8; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; Q9GZY8; -. DR CleanEx; HS_MFF; -. DR ExpressionAtlas; Q9GZY8; baseline and differential. DR Genevisible; Q9GZY8; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB. DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:MGI. DR GO; GO:0016559; P:peroxisome fission; 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:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; 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:1900063; P:regulation of peroxisome organization; IMP:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:UniProtKB. DR InterPro; IPR008518; FATE/Miff/Tango-11. DR PANTHER; PTHR16501; PTHR16501; 2. DR Pfam; PF05644; Miff; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Coiled coil; Complete proteome; KW Cytoplasmic vesicle; Membrane; Mitochondrion; KW Mitochondrion outer membrane; Peroxisome; Phosphoprotein; KW Polymorphism; Reference proteome; Synapse; Transmembrane; KW Transmembrane helix. FT CHAIN 1 342 Mitochondrial fission factor. FT /FTId=PRO_0000289184. FT TOPO_DOM 1 322 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 323 340 Helical; Anchor for type IV membrane FT protein. {ECO:0000255}. FT TOPO_DOM 341 342 Mitochondrial intermembrane. FT {ECO:0000255}. FT COILED 291 322 {ECO:0000255}. FT MOD_RES 115 115 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 155 155 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 157 157 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 172 172 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6PCP5}. FT MOD_RES 200 200 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 202 202 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 229 229 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 233 233 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 295 295 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6PCP5}. FT VAR_SEQ 1 26 Missing (in isoform 2, isoform 3, isoform FT 4 and isoform 5). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|Ref.3}. FT /FTId=VSP_025954. FT VAR_SEQ 174 271 Missing (in isoform 4). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_025955. FT VAR_SEQ 174 251 Missing (in isoform 5). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025956. FT VAR_SEQ 174 198 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_025957. FT VAR_SEQ 199 271 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_025958. FT VARIANT 7 7 S -> C (in dbSNP:rs3211097). FT /FTId=VAR_053915. FT VARIANT 7 7 S -> I (in dbSNP:rs3211098). FT /FTId=VAR_053916. FT VARIANT 29 29 E -> K (in a colorectal cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036028. FT CONFLICT 212 212 H -> Y (in Ref. 7; CAH56328). FT {ECO:0000305}. SQ SEQUENCE 342 AA; 38465 MW; 1DBFBBE17DB122A0 CRC64; MSKGTSSDTS LGRVSRAAFP SPTAAEMAEI SRIQYEMEYT EGISQRMRVP EKLKVAPPNA DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DVSFSRPADL DLIQSTPFKP LALKTPPRVL TLSERPLDFL DLERPPTTPQ NEEIRAVGRL KRERSMSENA VRQNGQLVRN DSLWHRSDSA PRNKISRFQA PISAPEYTVT PSPQQARVCP PHMLPEDGAN LSSARGILSL IQSSTRRAYQ QILDVLDENR RPVLRGGSAA ATSNPHHDNV RYGISNIDTT IEGTSDDLTV VDAASLRRQI IKLNRRLQLL EEENKERAKR EMVMYSITVA FWLLNSWLWF RR //