MFF_PONAB
ID MFF_PONAB Reviewed; 218 AA.
AC Q5R795;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Mitochondrial fission factor;
GN Name=MFF;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860223; CAH92365.1; -; mRNA.
DR RefSeq; NP_001126391.1; NM_001132919.1.
DR RefSeq; XP_009236459.1; XM_009238184.1.
DR AlphaFoldDB; Q5R795; -.
DR Ensembl; ENSPPYT00000034534; ENSPPYP00000036398; ENSPPYG00000013238.
DR GeneID; 100173373; -.
DR KEGG; pon:100173373; -.
DR CTD; 56947; -.
DR eggNOG; ENOG502R96B; Eukaryota.
DR GeneTree; ENSGT00390000009776; -.
DR InParanoid; Q5R795; -.
DR OrthoDB; 1383657at2759; -.
DR Proteomes; UP000001595; Chromosome 2B.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS: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_0000289186"
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; 25031 MW; 0123960DD8969EFA CRC64;
MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQGF QEGVPNASVI MQVPERIVVA
GNNEDVSFSR PADLDLIQST PFKSLALKTP PRVLTLSERP LDFLDLERPP TTPQNEEIRA
VGRVKRERSM SENAVRQNGQ LVRNDSLYGI SNIDTTTEGT SDDLTVVDAA SLRRQIIKLN
RRLQLLEEEN KERAKREMVM YSITVAFWLL NSWLWFRR