ID G3NWL3_GASAC Unreviewed; 230 AA.
AC G3NWL3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mitochondrial fission factor {ECO:0000256|RuleBase:RU368040};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000009732.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000009732.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000009732.1}
RP IDENTIFICATION.
RG Ensembl;
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: 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; G3NWL3; -.
DR Ensembl; ENSGACT00000009752.1; ENSGACP00000009732.1; ENSGACG00000007332.1.
DR GeneTree; ENSGT00390000009776; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000007332; Expressed in diencephalon and 13 other cell types or tissues.
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:SF17; MITOCHONDRIAL FISSION FACTOR; 1.
DR PANTHER; PTHR16501; UNCHARACTERIZED; 1.
DR Pfam; PF05644; Miff; 2.
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:UP000007635};
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 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368040"
FT DOMAIN 13..159
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT DOMAIN 161..230
FT /note="Mff-like"
FT /evidence="ECO:0000259|Pfam:PF05644"
FT REGION 117..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..208
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 230 AA; 26408 MW; 0AC22CC52EF68E29 CRC64;
MNGAAFPSPM AEMAEMNRIQ YELDYTEGIS QRMRIPEMLK VAPQGREDPN LGSQEVPRSV
IMQVPERIVI SGDSNDPQYP RPRDLDLIQS TPLESLSLKT PPRVLTLSDR PLDFLEEEQQ
SAPDSEEVSQ PQTRARRERS ASENAAARQN NQLMRNDSAL ALSTYEATLD AGPDDMTVVD
ATTLRRQLIK LNRRLQHLEE ENKERTKREM ILYSVTVAFW LVNTWVWLRR
//
