MFF_HUMAN
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 03-AUG-2022, entry version 141.
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 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 [20]
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 [21]
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 Promotes the recruitment and association of the fission mediator
CC dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be
CC involved in regulation of synaptic vesicle membrane dynamics by
CC recruitment of DNM1L to clathrin-containing vesicles.
CC {ECO:0000269|PubMed:18353969, ECO:0000269|PubMed:23530241}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L. Interacts with C11orf65/MFI;
CC the interaction inhibits MFF interaction with DNM1L. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q6PCP5}.
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}.
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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 RefSeq; XP_016860004.1; XM_017004515.1. [Q9GZY8-3]
DR AlphaFoldDB; Q9GZY8; -.
DR SMR; Q9GZY8; -.
DR BioGRID; 121271; 172.
DR IntAct; Q9GZY8; 116.
DR MINT; Q9GZY8; -.
DR STRING; 9606.ENSP00000302037; -.
DR GlyGen; Q9GZY8; 1 site, 1 O-linked glycan (1 site).
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; Q9GZY8; -.
DR PeptideAtlas; Q9GZY8; -.
DR PRIDE; 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 TopDownProteomics; Q9GZY8-2; -. [Q9GZY8-2]
DR ABCD; Q9GZY8; 2 sequenced antibodies.
DR Antibodypedia; 2600; 213 antibodies from 31 providers.
DR DNASU; 56947; -.
DR Ensembl; ENST00000304593.14; ENSP00000304898.10; ENSG00000168958.20. [Q9GZY8-2]
DR Ensembl; ENST00000337110.11; ENSP00000338412.7; ENSG00000168958.20. [Q9GZY8-3]
DR Ensembl; ENST00000349901.11; ENSP00000304134.9; ENSG00000168958.20. [Q9GZY8-5]
DR Ensembl; ENST00000353339.7; ENSP00000302037.4; ENSG00000168958.20. [Q9GZY8-1]
DR Ensembl; ENST00000354503.10; ENSP00000346498.6; ENSG00000168958.20. [Q9GZY8-4]
DR Ensembl; ENST00000409565.5; ENSP00000386964.1; ENSG00000168958.20. [Q9GZY8-4]
DR Ensembl; ENST00000409616.5; ENSP00000386641.1; ENSG00000168958.20. [Q9GZY8-5]
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 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 PhylomeDB; Q9GZY8; -.
DR TreeFam; TF325506; -.
DR PathwayCommons; Q9GZY8; -.
DR SignaLink; Q9GZY8; -.
DR SIGNOR; Q9GZY8; -.
DR BioGRID-ORCS; 56947; 14 hits in 1078 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 204 other tissues.
DR ExpressionAtlas; Q9GZY8; baseline and differential.
DR Genevisible; Q9GZY8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
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: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: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; PTHR16501; 1.
DR Pfam; PF05644; Miff; 1.
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
