ID A0A2U4ADX6_TURTR Unreviewed; 317 AA.
AC A0A2U4ADX6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|ARBA:ARBA00021235, ECO:0000256|RuleBase:RU368040};
GN Name=MFF {ECO:0000313|RefSeq:XP_019779106.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019779106.1};
RN [1] {ECO:0000313|RefSeq:XP_019779106.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019779106.1};
RG RefSeq;
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}.
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DR RefSeq; XP_019779106.1; XM_019923547.1.
DR AlphaFoldDB; A0A2U4ADX6; -.
DR GeneID; 101324194; -.
DR OrthoDB; 5353971at2759; -.
DR Proteomes; UP000245320; Chromosome 7.
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, 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 Reference proteome {ECO:0000313|Proteomes:UP000245320};
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 297..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368040"
FT DOMAIN 27..317
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 268..295
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 35479 MW; 2EF7B758C72E09BF CRC64;
MSKRTSNDTS LGRVSGAAFP SPSAAEMAEI SRIQYEMEYT EGISQRMRVP EKLKVAPPNA
DLEQGFQEGV SNASVIMQVP ERIVVAGNNE DIPFSRPADL DLIQSTPFKP LALKTPPRVL
TLSERPLDFL DLEKPPPTPQ SEEIRAVGRL KRERSMSENA VRQNGQLVRT DSIVTPSPQQ
VRVCPPRMLP EDGANPSSAR GILSLIQSST RRACQQILDV LDESRRPVLR GGSAAATSNP
HHDNARYGIS HIDTTIEGTS DDMTVVDAAS LRRQIIKLNR RLQLLEEENK ERAKREMVMY
SITVAFWLLN SWLWFRR
//
