ID   MFF_MOUSE               Reviewed;         291 AA.
AC   Q6PCP5; Q3UT87; Q91VG0; Q9D3P5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Mitochondrial fission factor;
GN   Name=Mff;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Xiphoid cartilage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89; SER-146; THR-149; SER-151
RP   AND SER-244, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 (ISOFORM 4),
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
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   [7]
RP   INTERACTION WITH C11ORF65 AND DNM1L, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=30059978; DOI=10.1210/en.2018-00426;
RA   Lee J., Pappalardo Z., Chopra D.G., Hennings T.G., Vaughn I., Lan C.,
RA   Choe J.J., Ang K., Chen S., Arkin M., McManus M.T., German M.S., Ku G.M.;
RT   "A Genetic Interaction Map of Insulin Production Identifies Mfi as an
RT   Inhibitor of Mitochondrial Fission.";
RL   Endocrinology 159:3321-3330(2018).
CC   -!- FUNCTION: Plays a role in mitochondrial and peroxisomal fission
CC       (PubMed:23283981, PubMed:30059978). Promotes the recruitment and
CC       association of the fission mediator dynamin-related protein 1 (DNM1L)
CC       to the mitochondrial surface (PubMed:23283981). May be involved in
CC       regulation of synaptic vesicle membrane dynamics by recruitment of
CC       DNM1L to clathrin-containing vesicles (By similarity).
CC       {ECO:0000250|UniProtKB:Q4KM98, ECO:0000269|PubMed:23283981,
CC       ECO:0000269|PubMed:30059978}.
CC   -!- SUBUNIT: Homodimer (PubMed:30059978). Interacts with DNM1L
CC       (PubMed:30059978). Interacts with C11orf65/MFI; the interaction
CC       inhibits MFF interaction with DNM1L (PubMed:30059978).
CC       {ECO:0000269|PubMed:30059978}.
CC   -!- INTERACTION:
CC       Q6PCP5; Q8K1M6: Dnm1l; NbExp=2; IntAct=EBI-21985996, EBI-2365792;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:30059978}; Single-pass type IV membrane protein
CC       {ECO:0000255}. Peroxisome {ECO:0000250|UniProtKB:Q9GZY8}. Cytoplasmic
CC       vesicle, secretory vesicle, synaptic vesicle
CC       {ECO:0000250|UniProtKB:Q4KM98}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6PCP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PCP5-2; Sequence=VSP_025959, VSP_025961;
CC       Name=3;
CC         IsoId=Q6PCP5-3; Sequence=VSP_025961;
CC       Name=4;
CC         IsoId=Q6PCP5-4; Sequence=VSP_025960;
CC   -!- SIMILARITY: Belongs to the Tango11 family. {ECO:0000305}.
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DR   EMBL; AK017226; BAB30643.1; -; mRNA.
DR   EMBL; AK139649; BAE24093.1; -; mRNA.
DR   EMBL; BC016597; AAH16597.1; -; mRNA.
DR   EMBL; BC059229; AAH59229.1; -; mRNA.
DR   CCDS; CCDS15098.1; -. [Q6PCP5-1]
DR   CCDS; CCDS78630.1; -. [Q6PCP5-2]
DR   CCDS; CCDS78631.1; -. [Q6PCP5-3]
DR   CCDS; CCDS78632.1; -. [Q6PCP5-4]
DR   RefSeq; NP_001297624.1; NM_001310695.1. [Q6PCP5-2]
DR   RefSeq; NP_001297626.1; NM_001310697.1. [Q6PCP5-3]
DR   RefSeq; NP_001297628.1; NM_001310699.1. [Q6PCP5-4]
DR   RefSeq; NP_083685.2; NM_029409.3. [Q6PCP5-1]
DR   AlphaFoldDB; Q6PCP5; -.
DR   SMR; Q6PCP5; -.
DR   BioGRID; 217700; 2.
DR   CORUM; Q6PCP5; -.
DR   IntAct; Q6PCP5; 1.
DR   STRING; 10090.ENSMUSP00000077446; -.
DR   GlyGen; Q6PCP5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6PCP5; -.
DR   PhosphoSitePlus; Q6PCP5; -.
DR   SwissPalm; Q6PCP5; -.
DR   EPD; Q6PCP5; -.
DR   jPOST; Q6PCP5; -.
DR   MaxQB; Q6PCP5; -.
DR   PaxDb; 10090-ENSMUSP00000077446; -.
DR   PeptideAtlas; Q6PCP5; -.
DR   ProteomicsDB; 292304; -. [Q6PCP5-1]
DR   ProteomicsDB; 292305; -. [Q6PCP5-2]
DR   ProteomicsDB; 292306; -. [Q6PCP5-3]
DR   ProteomicsDB; 292307; -. [Q6PCP5-4]
DR   Pumba; Q6PCP5; -.
DR   ABCD; Q6PCP5; 2 sequenced antibodies.
DR   Antibodypedia; 2600; 253 antibodies from 31 providers.
DR   DNASU; 75734; -.
DR   Ensembl; ENSMUST00000073025.12; ENSMUSP00000072784.6; ENSMUSG00000026150.15. [Q6PCP5-2]
DR   Ensembl; ENSMUST00000078332.13; ENSMUSP00000077446.7; ENSMUSG00000026150.15. [Q6PCP5-1]
DR   Ensembl; ENSMUST00000160786.8; ENSMUSP00000125230.2; ENSMUSG00000026150.15. [Q6PCP5-3]
DR   Ensembl; ENSMUST00000160972.8; ENSMUSP00000124200.2; ENSMUSG00000026150.15. [Q6PCP5-4]
DR   GeneID; 75734; -.
DR   KEGG; mmu:75734; -.
DR   UCSC; uc007brx.1; mouse. [Q6PCP5-1]
DR   UCSC; uc007bry.1; mouse. [Q6PCP5-3]
DR   UCSC; uc007brz.1; mouse. [Q6PCP5-2]
DR   UCSC; uc007bsc.1; mouse. [Q6PCP5-4]
DR   AGR; MGI:1922984; -.
DR   CTD; 56947; -.
DR   MGI; MGI:1922984; Mff.
DR   VEuPathDB; HostDB:ENSMUSG00000026150; -.
DR   eggNOG; ENOG502R96B; Eukaryota.
DR   GeneTree; ENSGT00390000009776; -.
DR   HOGENOM; CLU_066026_0_0_1; -.
DR   InParanoid; Q6PCP5; -.
DR   OMA; ERIVVAX; -.
DR   OrthoDB; 5353971at2759; -.
DR   PhylomeDB; Q6PCP5; -.
DR   TreeFam; TF325506; -.
DR   BioGRID-ORCS; 75734; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Mff; mouse.
DR   PRO; PR:Q6PCP5; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q6PCP5; Protein.
DR   Bgee; ENSMUSG00000026150; Expressed in choroid plexus epithelium and 260 other cell types or tissues.
DR   ExpressionAtlas; Q6PCP5; baseline and differential.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
DR   GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR   GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR   GO; GO:0016559; P:peroxisome fission; ISO:MGI.
DR   GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR   GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IDA:UniProtKB.
DR   GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
DR   GO; GO:1900063; P:regulation of peroxisome organization; ISO:MGI.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:MGI.
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; Q6PCP5; MM.
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..291
FT                   /note="Mitochondrial fission factor"
FT                   /id="PRO_0000289185"
FT   TOPO_DOM        1..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..289
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..291
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          106..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..271
FT                   /evidence="ECO:0000255"
FT   MOD_RES         89
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY8"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         149
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY8"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9GZY8"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         117
FT                   /note="E -> EQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025959"
FT   VAR_SEQ         147..220
FT                   /note="IVTPSPPQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDEN
FT                   RRPVLRGGSAAATSNPHHDNVR -> M (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025960"
FT   VAR_SEQ         148..200
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025961"
FT   MOD_RES         Q6PCP5-4:146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   291 AA;  32931 MW;  658884A1EF8EBCFD CRC64;
     MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQEF QDGVPNASVI MQVPERIVVT
     GNNEDISFSR PADLDLIQST PFKPLALKTP PRVLTLSERP LDFLDLERPL PTPQSEESRA
     VGRLKRERSM SENAVRQNGQ LVRNDSIVTP SPPQARVCPP HMLPEDGANL SSARGILSLI
     QSSTRRAYQQ ILDVLDENRR PVLRGGSAAA TSNPHHDNVR YGISNLDAAI EGASDDMTVV
     DAASLRRQII KLNRRLQLLE EENKERAKRE MVMYSITVAF WLLNSWLWFR R
//