ID A0A0A0MS29_HUMAN Unreviewed; 221 AA.
AC A0A0A0MS29;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|ARBA:ARBA00021235, ECO:0000256|RuleBase:RU368040};
GN Name=MFF {ECO:0000313|Ensembl:ENSP00000375912.2};
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 {ECO:0000313|Ensembl:ENSP00000375912.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000375912.2, ECO:0000313|Proteomes:UP000005640}
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 [2] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0007829|PubMed:18220336}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [4] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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 [8] {ECO:0007829|PubMed:21406692}
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 [9] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
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 [10] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [11] {ECO:0007829|PubMed:25944712}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712;
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 [12] {ECO:0000313|Ensembl:ENSP00000375912.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU368040}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle {ECO:0000256|ARBA:ARBA00004234}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}. Mitochondrion outer membrane
CC {ECO:0000256|RuleBase:RU368040}; Single-pass type IV membrane protein
CC {ECO:0000256|RuleBase:RU368040}. Peroxisome
CC {ECO:0000256|RuleBase:RU368040}.
CC -!- SIMILARITY: Belongs to the Tango11 family.
CC {ECO:0000256|ARBA:ARBA00009806, ECO:0000256|RuleBase:RU368040}.
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; AC097662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001263996.1; NM_001277067.1.
DR AlphaFoldDB; A0A0A0MS29; -.
DR SMR; A0A0A0MS29; -.
DR MassIVE; A0A0A0MS29; -.
DR PeptideAtlas; A0A0A0MS29; -.
DR Antibodypedia; 2600; 253 antibodies from 31 providers.
DR DNASU; 56947; -.
DR Ensembl; ENST00000392059.6; ENSP00000375912.2; ENSG00000168958.21.
DR GeneID; 56947; -.
DR UCSC; uc031rrq.1; human.
DR CTD; 56947; -.
DR HGNC; HGNC:24858; MFF.
DR VEuPathDB; HostDB:ENSG00000168958; -.
DR GeneTree; ENSGT00390000009776; -.
DR HOGENOM; CLU_066026_0_0_1; -.
DR OrthoDB; 5353971at2759; -.
DR BioGRID-ORCS; 56947; 15 hits in 1157 CRISPR screens.
DR ChiTaRS; MFF; human.
DR GenomeRNAi; 56947; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000168958; Expressed in sperm and 206 other cell types or tissues.
DR ExpressionAtlas; A0A0A0MS29; baseline and differential.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0000266; P:mitochondrial fission; IEA:UniProtKB-UniRule.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:UniProtKB-UniRule.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:UniProtKB-UniRule.
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.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368040};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368040};
KW Mitochondrion outer membrane {ECO:0000256|RuleBase:RU368040};
KW Peroxisome {ECO:0000256|RuleBase:RU368040};
KW Proteomics identification {ECO:0007829|EPD:A0A0A0MS29,
KW ECO:0007829|MaxQB:A0A0A0MS29};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368040};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368040}.
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368040"
FT DOMAIN 1..221
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 79..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 172..199
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 221 AA; 25302 MW; 9B80D8383D558701 CRC64;
MQVPERIVVA GNNEDVSFSR PADLDLIQST PFKPLALKTP PRVLTLSERP LDFLDLERPP
TTPQNEEIRA VGRLKRERSM SENAVRQNGQ LVRNDSLVTP SPQQARVCPP HMLPEDGANL
SSARGILSLI QSSTRRAYQQ ILDVLDENRR YGISNIDTTI EGTSDDLTVV DAASLRRQII
KLNRRLQLLE EENKERAKRE MVMYSITVAF WLLNSWLWFR R
//