MFF_RAT
ID MFF_RAT Reviewed; 218 AA.
AC Q4KM98;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Mitochondrial fission factor;
GN Name=Mff;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH DNM1L, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23792689; DOI=10.1038/ncb2791;
RA Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
RA Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
RA Morrison R.S., Jonas E.A.;
RT "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during
RT endocytosis.";
RL Nat. Cell Biol. 15:773-785(2013).
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:23792689}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L (PubMed:23792689). Interacts
CC with C11orf65/MFI; the interaction inhibits MFF interaction with DNM1L
CC (By similarity). {ECO:0000250|UniProtKB:Q6PCP5,
CC ECO:0000269|PubMed:23792689}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q6PCP5}; Single-pass type IV membrane protein
CC {ECO:0000255}. Peroxisome {ECO:0000250}. Cytoplasmic vesicle, secretory
CC vesicle, synaptic vesicle {ECO:0000269|PubMed:23792689}.
CC -!- SIMILARITY: Belongs to the Tango11 family. {ECO:0000305}.
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DR EMBL; BC098682; AAH98682.1; -; mRNA.
DR RefSeq; NP_001034104.1; NM_001039015.2.
DR RefSeq; NP_001258213.1; NM_001271284.1.
DR RefSeq; NP_001263330.1; NM_001276401.1.
DR RefSeq; XP_006245273.2; XM_006245211.2.
DR RefSeq; XP_008765547.1; XM_008767325.1.
DR RefSeq; XP_017459407.1; XM_017603918.1.
DR AlphaFoldDB; Q4KM98; -.
DR BioGRID; 257006; 1.
DR CORUM; Q4KM98; -.
DR DIP; DIP-60704N; -.
DR IntAct; Q4KM98; 3.
DR STRING; 10116.ENSRNOP00000020705; -.
DR iPTMnet; Q4KM98; -.
DR jPOST; Q4KM98; -.
DR PaxDb; Q4KM98; -.
DR PRIDE; Q4KM98; -.
DR ABCD; Q4KM98; 2 sequenced antibodies.
DR GeneID; 301563; -.
DR KEGG; rno:301563; -.
DR UCSC; RGD:1310230; rat.
DR CTD; 56947; -.
DR RGD; 1310230; Mff.
DR eggNOG; ENOG502R96B; Eukaryota.
DR InParanoid; Q4KM98; -.
DR OrthoDB; 1383657at2759; -.
DR PRO; PR:Q4KM98; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q4KM98; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISO:RGD.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:RGD.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:0016559; P:peroxisome fission; ISO:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:RGD.
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:RGD.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:CAFA.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
DR GO; GO:1900063; P:regulation of peroxisome organization; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR InterPro; IPR039433; Mff-like_dom.
DR InterPro; IPR008518; Mff/Tango-11.
DR PANTHER; PTHR16501; PTHR16501; 2.
DR Pfam; PF05644; Miff; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Peroxisome; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="Mitochondrial fission factor"
FT /id="PRO_0000289187"
FT TOPO_DOM 1..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..216
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..218
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT COILED 167..198
FT /evidence="ECO:0000255"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZY8"
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:22673903"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCP5"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCP5"
SQ SEQUENCE 218 AA; 24971 MW; 4CAF8F7309D707CC CRC64;
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QDGVPNASVI MQVPERIVVT
GNNEDISFSR PADLDLIQST PFKPLALKTP PRVLTLSERP LDFLDLERPP PTPQSEEIRA
VGRLKRERSM SENAVRQNGQ LVRNDSMYGI SSLDAAVEGA SEDMSVVDAA SLRRQIIKLN
RRLQLLEEEN KERAKREMVM YSITVAFWLL NSWLWFRR
