ID A0A3Q0KPF4_SCHMA Unreviewed; 205 AA.
AC A0A3Q0KPF4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JUN-2023, entry version 20.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|RuleBase:RU368040};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_148140.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_148140.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_148140.1};
RG WormBaseParasite;
RL Submitted (DEC-2018) 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: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC Mitochondrion outer membrane {ECO:0000256|RuleBase:RU368040}; Single-
CC pass type IV membrane protein {ECO:0000256|RuleBase:RU368040}.
CC Peroxisome {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 AlphaFoldDB; A0A3Q0KPF4; -.
DR EnsemblMetazoa; Smp_148140.1; Smp_148140.1; Smp_148140.
DR WBParaSite; Smp_148140.1; Smp_148140.1; Smp_148140.
DR InParanoid; A0A3Q0KPF4; -.
DR Proteomes; UP000008854; 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: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:SF6; TRANSPORT AND GOLGI ORGANIZATION PROTEIN 11; 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};
KW Mitochondrion {ECO:0000256|RuleBase:RU368040};
KW Mitochondrion outer membrane {ECO:0000256|RuleBase:RU368040};
KW Peroxisome {ECO:0000256|RuleBase:RU368040};
KW Reference proteome {ECO:0000313|Proteomes:UP000008854};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..90
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 156..183
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 23102 MW; 1532078A5CC72A21 CRC64;
MRVPDRISLD PSSLSQMNLS LNSSENDNMK VPERIVMSGA QNQSSPLMAF NRRGDDLIDN
LDPVPLQHAL EPLPTSLVLN EVHYPDLERL TIEKREIETT ISTPLTIESQ NHVPTEPQSS
PLPLSNVSNV MNHSSTSTST SSSSLLTNQT SNAQSIVVDT RRIRLLENRI NEIELELTRR
QLMDKVLYIT FGGYFVLKFL RLLFS
//