ID   MFF_BOVIN               Reviewed;         218 AA.
AC   Q3ZCD8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Mitochondrial fission factor;
GN   Name=MFF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q6PCP5, ECO:0000250|UniProtKB:Q9GZY8}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q6PCP5}; 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   -!- SIMILARITY: Belongs to the Tango11 family. {ECO:0000305}.
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DR   EMBL; BC102501; AAI02502.1; -; mRNA.
DR   RefSeq; NP_001029439.1; NM_001034267.2.
DR   AlphaFoldDB; Q3ZCD8; -.
DR   SMR; Q3ZCD8; -.
DR   PaxDb; Q3ZCD8; -.
DR   Ensembl; ENSBTAT00000028425; ENSBTAP00000028425; ENSBTAG00000021319.
DR   GeneID; 506291; -.
DR   KEGG; bta:506291; -.
DR   CTD; 56947; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021319; -.
DR   eggNOG; ENOG502R96B; Eukaryota.
DR   GeneTree; ENSGT00390000009776; -.
DR   HOGENOM; CLU_066026_0_0_1; -.
DR   InParanoid; Q3ZCD8; -.
DR   OrthoDB; 1383657at2759; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000021319; Expressed in spermatocyte and 109 other tissues.
DR   ExpressionAtlas; Q3ZCD8; baseline and differential.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
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:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR   InterPro; IPR039433; Mff-like_dom.
DR   InterPro; IPR008518; Mff/Tango-11.
DR   PANTHER; PTHR16501; PTHR16501; 2.
DR   Pfam; PF05644; Miff; 2.
PE   2: Evidence at transcript 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_0000289183"
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:0000250|UniProtKB:Q9GZY8"
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;  25060 MW;  B53223CF14EA46E7 CRC64;
     MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVSNASVI MQVPERIVVA
     GNNEDIPFSR PADLDLIQST PFKPLALKTP PRVLTLSERP LDFLDLERPA PTPQNEEIRA
     VGRLKRERSM SENAVRQNGQ LVKTDSMYGI SNIDAMIEGT SEDMTVVDAA SLRRQIIKLN
     RRLQLLEEEN KERAKREMVM YSITVAFWLL NSWLWFRR