ID A0A3Q7TLE6_VULVU Unreviewed; 379 AA.
AC A0A3Q7TLE6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|ARBA:ARBA00021235, ECO:0000256|RuleBase:RU368040};
GN Name=MFF {ECO:0000313|RefSeq:XP_025862107.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025862107.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025862107.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025862107.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025862107.1};
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_025862107.1; XM_026006322.1.
DR AlphaFoldDB; A0A3Q7TLE6; -.
DR KEGG; vvp:112925528; -.
DR OrthoDB; 5353971at2759; -.
DR Proteomes; UP000286640; Unplaced.
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:UP000286640};
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 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368040"
FT DOMAIN 27..379
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..357
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 379 AA; 42920 MW; 143A5F055ADE81A5 CRC64;
MSERTSSDTP LGRVSGAAFP SPTAAEMAEI SRIQYEMEYT EGISQQMRVP EKLKVAPPNA
DLEQGFQEGV PNASVIMQVP ERIVVAGNNE DIPFSRPADL DLIQSTPFKP LALKTPPRVL
TLSERPLDFL DLERPPPTPQ NEEIRAVGRL KRERSMSENA VRQNGQLVRA DSMWHRSDSA
PRNKISRFQA SFSAPEYTGW SLTKEIIPSQ FEKHCSWENS WGKSVTPSPQ QVRVCPPQML
PEDGANLSSA RGILSLIQSS TRRAYQQILD VLDENRSVRR QNEIRCERPV LRGGSAAATS
NPHHDNVRHG ISHIDTTIEG TSDDMTVVDA ASLRRQIIKL NRRLQLLEEE NKERAKREMV
MYSITVAFWL LNSWLWFRR
//
