ID A0A091D216_FUKDA Unreviewed; 98 AA.
AC A0A091D216;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|ARBA:ARBA00021235, ECO:0000256|RuleBase:RU368040};
DE Flags: Fragment;
GN ORFNames=H920_13556 {ECO:0000313|EMBL:KFO25042.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO25042.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO25042.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO25042.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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.
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}.
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DR EMBL; KN123428; KFO25042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D216; -.
DR STRING; 885580.ENSFDAP00000003240; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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 Reference proteome {ECO:0000313|Proteomes:UP000028990};
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 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368040"
FT DOMAIN 7..98
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO25042.1"
SQ SEQUENCE 98 AA; 11449 MW; 7849ADF07F64645C CRC64;
ILDMTEEKLR PSLCGRSPAL TNVHNDNSRH GVSNTAIEGT SQDMTAEDAA VLRRQIMKLN
RRLQLVEGEN KKRPKREMVM YSITVAFWLF TSWLWFRR
//
