MFF_MOUSE
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 03-AUG-2022, entry version 117.
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 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:23283981, ECO:0000269|PubMed:30059978}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L (PubMed:30059978). Interacts
CC with C11orf65/MFI; the interaction inhibits MFF interaction with DNM1L
CC (PubMed:30059978). {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 iPTMnet; Q6PCP5; -.
DR PhosphoSitePlus; Q6PCP5; -.
DR SwissPalm; Q6PCP5; -.
DR EPD; Q6PCP5; -.
DR jPOST; Q6PCP5; -.
DR MaxQB; Q6PCP5; -.
DR PaxDb; Q6PCP5; -.
DR PeptideAtlas; Q6PCP5; -.
DR PRIDE; Q6PCP5; -.
DR ProteomicsDB; 292304; -. [Q6PCP5-1]
DR ProteomicsDB; 292305; -. [Q6PCP5-2]
DR ProteomicsDB; 292306; -. [Q6PCP5-3]
DR ProteomicsDB; 292307; -. [Q6PCP5-4]
DR ABCD; Q6PCP5; 2 sequenced antibodies.
DR Antibodypedia; 2600; 213 antibodies from 31 providers.
DR DNASU; 75734; -.
DR Ensembl; ENSMUST00000073025; ENSMUSP00000072784; ENSMUSG00000026150. [Q6PCP5-2]
DR Ensembl; ENSMUST00000078332; ENSMUSP00000077446; ENSMUSG00000026150. [Q6PCP5-1]
DR Ensembl; ENSMUST00000160786; ENSMUSP00000125230; ENSMUSG00000026150. [Q6PCP5-3]
DR Ensembl; ENSMUST00000160972; ENSMUSP00000124200; ENSMUSG00000026150. [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 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; 1383657at2759; -.
DR PhylomeDB; Q6PCP5; -.
DR TreeFam; TF325506; -.
DR BioGRID-ORCS; 75734; 2 hits in 72 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 256 other tissues.
DR ExpressionAtlas; Q6PCP5; baseline and differential.
DR Genevisible; Q6PCP5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:MGI.
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: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; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:0016559; P:peroxisome fission; 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: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; PTHR16501; 2.
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..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
