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 27-MAR-2024, entry version 150. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, RP 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 and RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 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 project: RT 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT 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., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149 AND SER-151 (ISOFORM 2), RP 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 SCALE RP ANALYSIS] AT SER-146 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY RP [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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT 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., 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 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., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT 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 recruitment RT and are specific for mitochondrial fission."; RL J. Biol. Chem. 288:27584-27593(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-233, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] 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., 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-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., 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 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). RN [20] 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., 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 [21] RP INVOLVEMENT IN EMPF2. RX PubMed=26783368; DOI=10.1136/jmedgenet-2015-103500; RA Koch J., Feichtinger R.G., Freisinger P., Pies M., Schroedl F., Iuso A., RA Sperl W., Mayr J.A., Prokisch H., Haack T.B.; RT "Disturbed mitochondrial and peroxisomal dynamics due to loss of MFF causes RT Leigh-like encephalopathy, optic atrophy and peripheral neuropathy."; RL J. Med. Genet. 53:270-278(2016). RN [22] 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., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in mitochondrial and peroxisomal fission CC (PubMed:18353969, PubMed:23530241, PubMed:24196833). Promotes the CC recruitment and association of the fission mediator dynamin-related CC protein 1 (DNM1L) to the mitochondrial surface (PubMed:23530241). May CC be involved in regulation of synaptic vesicle membrane dynamics by CC recruitment of DNM1L to clathrin-containing vesicles (By similarity). CC {ECO:0000250|UniProtKB:Q4KM98, ECO:0000269|PubMed:18353969, CC ECO:0000269|PubMed:23530241, ECO:0000269|PubMed:24196833}. CC -!- SUBUNIT: Homodimer (PubMed:23530241). Interacts with DNM1L CC (PubMed:24196833). Interacts with C11orf65/MFI; the interaction CC inhibits MFF interaction with DNM1L (By similarity). CC {ECO:0000250|UniProtKB:Q6PCP5, ECO:0000269|PubMed:23530241, CC ECO:0000269|PubMed:24196833}. CC -!- INTERACTION: CC Q9GZY8; O00429: DNM1L; NbExp=3; IntAct=EBI-11420856, EBI-724571; CC Q9GZY8; P0DTF1; Xeno; NbExp=3; IntAct=EBI-11420856, EBI-26953451; CC Q9GZY8-5; Q15848: ADIPOQ; NbExp=3; IntAct=EBI-11956541, EBI-10827839; CC Q9GZY8-5; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-11956541, EBI-1754287; CC Q9GZY8-5; Q9NVV5-2: AIG1; NbExp=6; IntAct=EBI-11956541, EBI-11957045; CC Q9GZY8-5; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-11956541, EBI-12109402; CC Q9GZY8-5; P05090: APOD; NbExp=3; IntAct=EBI-11956541, EBI-715495; CC Q9GZY8-5; Q9BQE5: APOL2; NbExp=3; IntAct=EBI-11956541, EBI-4290634; CC Q9GZY8-5; Q92482: AQP3; NbExp=3; IntAct=EBI-11956541, EBI-2808854; CC Q9GZY8-5; Q13520: AQP6; NbExp=3; IntAct=EBI-11956541, EBI-13059134; CC Q9GZY8-5; Q99437: ATP6V0B; NbExp=3; IntAct=EBI-11956541, EBI-3904417; CC Q9GZY8-5; O15155: BET1; NbExp=3; IntAct=EBI-11956541, EBI-749204; CC Q9GZY8-5; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-11956541, EBI-12062109; CC Q9GZY8-5; P11912: CD79A; NbExp=3; IntAct=EBI-11956541, EBI-7797864; CC Q9GZY8-5; O14735: CDIPT; NbExp=3; IntAct=EBI-11956541, EBI-358858; CC Q9GZY8-5; Q8N111: CEND1; NbExp=3; IntAct=EBI-11956541, EBI-946825; CC Q9GZY8-5; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-11956541, EBI-12256978; CC Q9GZY8-5; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-11956541, EBI-11522780; CC Q9GZY8-5; O95406: CNIH1; NbExp=3; IntAct=EBI-11956541, EBI-12172273; CC Q9GZY8-5; P29400-2: COL4A5; NbExp=3; IntAct=EBI-11956541, EBI-12211159; CC Q9GZY8-5; Q4LDR2: CTXN3; NbExp=3; IntAct=EBI-11956541, EBI-12019274; CC Q9GZY8-5; O43169: CYB5B; NbExp=3; IntAct=EBI-11956541, EBI-1058710; CC Q9GZY8-5; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-11956541, EBI-2680384; CC Q9GZY8-5; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-11956541, EBI-781551; CC Q9GZY8-5; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-11956541, EBI-18304435; CC Q9GZY8-5; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-11956541, EBI-18938272; CC Q9GZY8-5; Q92520: FAM3C; NbExp=3; IntAct=EBI-11956541, EBI-2876774; CC Q9GZY8-5; Q969F0: FATE1; NbExp=3; IntAct=EBI-11956541, EBI-743099; CC Q9GZY8-5; Q8NFU4: FDCSP; NbExp=3; IntAct=EBI-11956541, EBI-12210457; CC Q9GZY8-5; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-11956541, EBI-713304; CC Q9GZY8-5; P08034: GJB1; NbExp=3; IntAct=EBI-11956541, EBI-17565645; CC Q9GZY8-5; Q9NS71: GKN1; NbExp=3; IntAct=EBI-11956541, EBI-3933251; CC Q9GZY8-5; O14653: GOSR2; NbExp=3; IntAct=EBI-11956541, EBI-4401517; CC Q9GZY8-5; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-11956541, EBI-13345167; CC Q9GZY8-5; P24593: IGFBP5; NbExp=3; IntAct=EBI-11956541, EBI-720480; CC Q9GZY8-5; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-11956541, EBI-10266796; CC Q9GZY8-5; O43561-2: LAT; NbExp=3; IntAct=EBI-11956541, EBI-8070286; CC Q9GZY8-5; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-11956541, EBI-2820517; CC Q9GZY8-5; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-11956541, EBI-12033434; CC Q9GZY8-5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11956541, EBI-16439278; CC Q9GZY8-5; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-11956541, EBI-11956541; CC Q9GZY8-5; P30301: MIP; NbExp=3; IntAct=EBI-11956541, EBI-8449636; CC Q9GZY8-5; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-11956541, EBI-6163737; CC Q9GZY8-5; O75425: MOSPD3; NbExp=3; IntAct=EBI-11956541, EBI-12179105; CC Q9GZY8-5; O95297: MPZL1; NbExp=3; IntAct=EBI-11956541, EBI-963338; CC Q9GZY8-5; Q6P499: NIPAL3; NbExp=3; IntAct=EBI-11956541, EBI-10252783; CC Q9GZY8-5; Q8N912: NRAC; NbExp=3; IntAct=EBI-11956541, EBI-12051377; CC Q9GZY8-5; Q8IXM6: NRM; NbExp=3; IntAct=EBI-11956541, EBI-10262547; CC Q9GZY8-5; P30990: NTS; NbExp=3; IntAct=EBI-11956541, EBI-6655799; CC Q9GZY8-5; P03999: OPN1SW; NbExp=3; IntAct=EBI-11956541, EBI-13385956; CC Q9GZY8-5; P35372-10: OPRM1; NbExp=3; IntAct=EBI-11956541, EBI-12807478; CC Q9GZY8-5; Q9H4B4: PLK3; NbExp=3; IntAct=EBI-11956541, EBI-751877; CC Q9GZY8-5; Q9Y342: PLLP; NbExp=3; IntAct=EBI-11956541, EBI-3919291; CC Q9GZY8-5; P26678: PLN; NbExp=3; IntAct=EBI-11956541, EBI-692836; CC Q9GZY8-5; P60201-2: PLP1; NbExp=3; IntAct=EBI-11956541, EBI-12188331; CC Q9GZY8-5; Q5VY80: RAET1L; NbExp=3; IntAct=EBI-11956541, EBI-16364752; CC Q9GZY8-5; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-11956541, EBI-10192441; CC Q9GZY8-5; O75783: RHBDL1; NbExp=3; IntAct=EBI-11956541, EBI-12104986; CC Q9GZY8-5; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-11956541, EBI-3917235; CC Q9GZY8-5; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-11956541, EBI-2855401; CC Q9GZY8-5; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11956541, EBI-8652744; CC Q9GZY8-5; O75396: SEC22B; NbExp=3; IntAct=EBI-11956541, EBI-1058865; CC Q9GZY8-5; Q15436: SEC23A; NbExp=3; IntAct=EBI-11956541, EBI-81088; CC Q9GZY8-5; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-11956541, EBI-18037857; CC Q9GZY8-5; Q16572: SLC18A3; NbExp=3; IntAct=EBI-11956541, EBI-17598000; CC Q9GZY8-5; P78383: SLC35B1; NbExp=3; IntAct=EBI-11956541, EBI-12147661; CC Q9GZY8-5; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-11956541, EBI-10290130; CC Q9GZY8-5; P30825: SLC7A1; NbExp=3; IntAct=EBI-11956541, EBI-4289564; CC Q9GZY8-5; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-11956541, EBI-5235586; CC Q9GZY8-5; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-11956541, EBI-13292283; CC Q9GZY8-5; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-11956541, EBI-12188413; CC Q9GZY8-5; P0DN84: STRIT1; NbExp=3; IntAct=EBI-11956541, EBI-12200293; CC Q9GZY8-5; O15400: STX7; NbExp=3; IntAct=EBI-11956541, EBI-3221827; CC Q9GZY8-5; Q9UNK0: STX8; NbExp=3; IntAct=EBI-11956541, EBI-727240; CC Q9GZY8-5; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-11956541, EBI-10329860; CC Q9GZY8-5; P02786: TFRC; NbExp=3; IntAct=EBI-11956541, EBI-355727; CC Q9GZY8-5; Q6P4D7: TM6SF1; NbExp=3; IntAct=EBI-11956541, EBI-12892691; CC Q9GZY8-5; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-11956541, EBI-10694905; CC Q9GZY8-5; Q9NV12: TMEM140; NbExp=3; IntAct=EBI-11956541, EBI-2844246; CC Q9GZY8-5; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-11956541, EBI-2339195; CC Q9GZY8-5; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-11956541, EBI-11994282; CC Q9GZY8-5; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11956541, EBI-10173151; CC Q9GZY8-5; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-11956541, EBI-12195227; CC Q9GZY8-5; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-11956541, EBI-10982110; CC Q9GZY8-5; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-11956541, EBI-11956809; CC Q9GZY8-5; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-11956541, EBI-12038591; CC Q9GZY8-5; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-11956541, EBI-2852148; CC Q9GZY8-5; Q8N661: TMEM86B; NbExp=6; IntAct=EBI-11956541, EBI-2548832; CC Q9GZY8-5; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-11956541, EBI-17198826; CC Q9GZY8-5; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-11956541, EBI-12111910; CC Q9GZY8-5; Q9Y320: TMX2; NbExp=3; IntAct=EBI-11956541, EBI-6447886; CC Q9GZY8-5; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-11956541, EBI-765817; CC Q9GZY8-5; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-11956541, EBI-11996766; CC Q9GZY8-5; O60636: TSPAN2; NbExp=3; IntAct=EBI-11956541, EBI-3914288; CC Q9GZY8-5; Q86UF1: TSPAN33; NbExp=3; IntAct=EBI-11956541, EBI-12045841; CC Q9GZY8-5; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-11956541, EBI-12195249; CC Q9GZY8-5; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-11956541, EBI-10243654; CC Q9GZY8-5; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-11956541, EBI-11988865; CC Q9GZY8-5; Q53HI1: UNC50; NbExp=3; IntAct=EBI-11956541, EBI-7601760; CC Q9GZY8-5; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-11956541, EBI-4401271; CC Q9GZY8-5; O75841: UPK1B; NbExp=3; IntAct=EBI-11956541, EBI-12237619; CC Q9GZY8-5; O75379: VAMP4; NbExp=3; IntAct=EBI-11956541, EBI-744953; CC Q9GZY8-5; O95159: ZFPL1; NbExp=3; IntAct=EBI-11956541, EBI-718439; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23921378}; Single-pass CC type IV membrane protein {ECO:0000255}. Peroxisome CC {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23921378}. Cytoplasmic CC vesicle, secretory vesicle, synaptic vesicle CC {ECO:0000250|UniProtKB:Q4KM98}. 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 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 -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney, liver, brain, CC muscle, and stomach. {ECO:0000269|PubMed:18353969}. CC -!- DISEASE: Encephalopathy due to defective mitochondrial and peroxisomal CC fission 2 (EMPF2) [MIM:617086]: An autosomal recessive disorder CC characterized by delayed psychomotor development, severe hypotonia with CC inability to walk, microcephaly, and abnormal signals in the basal CC ganglia. More variable features include early-onset seizures, optic CC atrophy, and peripheral neuropathy. {ECO:0000269|PubMed:26783368}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. 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. DR RefSeq; XP_006712702.1; XM_006712639.2. DR RefSeq; XP_011509802.1; XM_011511500.1. [Q9GZY8-1] DR RefSeq; XP_016860004.1; XM_017004515.1. DR AlphaFoldDB; Q9GZY8; -. DR SMR; Q9GZY8; -. DR BioGRID; 121271; 181. DR IntAct; Q9GZY8; 116. DR MINT; Q9GZY8; -. DR STRING; 9606.ENSP00000302037; -. DR GlyCosmos; Q9GZY8; 1 site, 1 glycan. DR GlyGen; Q9GZY8; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9GZY8; -. DR PhosphoSitePlus; Q9GZY8; -. DR BioMuta; MFF; -. DR DMDM; 74725008; -. DR EPD; Q9GZY8; -. DR jPOST; Q9GZY8; -. DR MassIVE; Q9GZY8; -. DR MaxQB; Q9GZY8; -. DR PaxDb; 9606-ENSP00000302037; -. DR PeptideAtlas; Q9GZY8; -. DR ProteomicsDB; 80176; -. [Q9GZY8-1] DR ProteomicsDB; 80177; -. [Q9GZY8-2] DR ProteomicsDB; 80178; -. [Q9GZY8-3] DR ProteomicsDB; 80179; -. [Q9GZY8-4] DR ProteomicsDB; 80180; -. [Q9GZY8-5] DR Pumba; Q9GZY8; -. DR TopDownProteomics; Q9GZY8-2; -. [Q9GZY8-2] DR ABCD; Q9GZY8; 2 sequenced antibodies. DR Antibodypedia; 2600; 253 antibodies from 31 providers. DR DNASU; 56947; -. DR Ensembl; ENST00000304593.14; ENSP00000304898.10; ENSG00000168958.21. [Q9GZY8-2] DR Ensembl; ENST00000337110.11; ENSP00000338412.7; ENSG00000168958.21. [Q9GZY8-3] DR Ensembl; ENST00000349901.11; ENSP00000304134.9; ENSG00000168958.21. [Q9GZY8-5] DR Ensembl; ENST00000353339.8; ENSP00000302037.4; ENSG00000168958.21. [Q9GZY8-1] DR Ensembl; ENST00000354503.10; ENSP00000346498.6; ENSG00000168958.21. [Q9GZY8-4] DR Ensembl; ENST00000409565.5; ENSP00000386964.1; ENSG00000168958.21. [Q9GZY8-4] DR GeneID; 56947; -. DR KEGG; hsa:56947; -. DR MANE-Select; ENST00000304593.14; ENSP00000304898.10; NM_001277062.2; NP_001263991.1. [Q9GZY8-2] DR UCSC; uc002vos.5; human. [Q9GZY8-1] DR AGR; HGNC:24858; -. DR CTD; 56947; -. DR DisGeNET; 56947; -. DR GeneCards; MFF; -. DR HGNC; HGNC:24858; MFF. DR HPA; ENSG00000168958; Low tissue specificity. DR MalaCards; MFF; -. DR MIM; 614785; gene. DR MIM; 617086; phenotype. DR neXtProt; NX_Q9GZY8; -. DR OpenTargets; ENSG00000168958; -. DR Orphanet; 485421; MFF-related encephalopathy due to mitochondrial and peroxisomal fission defect. DR PharmGKB; PA162395839; -. DR VEuPathDB; HostDB:ENSG00000168958; -. DR eggNOG; ENOG502R96B; Eukaryota. DR GeneTree; ENSGT00390000009776; -. DR InParanoid; Q9GZY8; -. DR OMA; ERIVVAX; -. DR OrthoDB; 5353971at2759; -. DR PhylomeDB; Q9GZY8; -. DR TreeFam; TF325506; -. DR PathwayCommons; Q9GZY8; -. DR SignaLink; Q9GZY8; -. DR SIGNOR; Q9GZY8; -. DR BioGRID-ORCS; 56947; 15 hits in 1157 CRISPR screens. DR ChiTaRS; MFF; human. DR GeneWiki; Mitochondrial_fission_factor; -. DR GenomeRNAi; 56947; -. DR Pharos; Q9GZY8; Tbio. DR PRO; PR:Q9GZY8; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9GZY8; Protein. DR Bgee; ENSG00000168958; Expressed in sperm and 206 other cell types or tissues. DR ExpressionAtlas; Q9GZY8; baseline and differential. DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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:0007005; P:mitochondrion organization; 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: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; IPR039433; Mff-like_dom. DR InterPro; IPR008518; Mff/Tango-11. DR PANTHER; PTHR16501:SF17; MITOCHONDRIAL FISSION FACTOR; 1. DR PANTHER; PTHR16501; UNCHARACTERIZED; 1. DR Pfam; PF05644; Miff; 1. DR Genevisible; Q9GZY8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasmic vesicle; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Peroxisome; Phosphoprotein; KW Reference proteome; Synapse; Transmembrane; Transmembrane helix. FT CHAIN 1..342 FT /note="Mitochondrial fission factor" FT /id="PRO_0000289184" FT TOPO_DOM 1..322 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 323..340 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 341..342 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT COILED 291..322 FT /evidence="ECO:0000255" FT MOD_RES 115 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 172 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PCP5" FT MOD_RES 200 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 233 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6PCP5" FT VAR_SEQ 1..26 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_025954" FT VAR_SEQ 174..271 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_025955" FT VAR_SEQ 174..251 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025956" FT VAR_SEQ 174..198 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_025957" FT VAR_SEQ 199..271 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_025958" FT VARIANT 7 FT /note="S -> C (in dbSNP:rs3211097)" FT /id="VAR_053915" FT VARIANT 7 FT /note="S -> I (in dbSNP:rs3211098)" FT /id="VAR_053916" FT VARIANT 29 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036028" FT CONFLICT 212 FT /note="H -> Y (in Ref. 7; CAH56328)" FT /evidence="ECO:0000305" FT MOD_RES Q9GZY8-2:146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES Q9GZY8-2:149 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES Q9GZY8-2:151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES Q9GZY8-5:146 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" 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 //