ID   MID51_DANRE             Reviewed;         468 AA.
AC   A4IG61;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Mitochondrial dynamics protein MID51;
DE   AltName: Full=Mitochondrial dynamics protein of 51 kDa homolog;
DE   AltName: Full=Mitochondrial elongation factor 1;
DE   AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like;
GN   Name=mief1; Synonyms=mid51, smcr7l; ORFNames=zgc:162279;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=WIK; TISSUE=Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mitochondrial outer membrane protein which regulates
CC       mitochondrial fission. Promotes the recruitment and association of the
CC       fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial
CC       surface independently of the mitochondrial fission FIS1 and MFF
CC       proteins. Regulates DNM1L GTPase activity and DNM1L oligomerization (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}.
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DR   EMBL; BC134944; AAI34945.1; -; mRNA.
DR   RefSeq; NP_001077309.1; NM_001083840.1.
DR   AlphaFoldDB; A4IG61; -.
DR   SMR; A4IG61; -.
DR   STRING; 7955.ENSDARP00000083758; -.
DR   PaxDb; A4IG61; -.
DR   PeptideAtlas; A4IG61; -.
DR   PRIDE; A4IG61; -.
DR   GeneID; 564985; -.
DR   KEGG; dre:564985; -.
DR   CTD; 54471; -.
DR   ZFIN; ZDB-GENE-060810-64; mief1.
DR   eggNOG; KOG4542; Eukaryota.
DR   InParanoid; A4IG61; -.
DR   OrthoDB; 515815at2759; -.
DR   PhylomeDB; A4IG61; -.
DR   PRO; PR:A4IG61; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   InterPro; IPR024810; Mab-21_dom.
DR   InterPro; IPR045909; MID49/MID51.
DR   PANTHER; PTHR16451; PTHR16451; 1.
DR   Pfam; PF03281; Mab-21; 1.
DR   SMART; SM01265; Mab-21; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..468
FT                   /note="Mitochondrial dynamics protein MID51"
FT                   /id="PRO_0000310452"
FT   TOPO_DOM        1..29
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          50..196
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          56..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..170
FT                   /note="Important for interaction with DNM1L"
FT                   /evidence="ECO:0000250"
FT   REGION          235..244
FT                   /note="Important for interaction with DNM1L"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        77..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         188
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   468 AA;  52101 MW;  9C057AB4B1B50A0F CRC64;
     MAGVNGDRKG KKDDNGLGTA IDFVLSNAKL VLGVGGAAML GIATLAVKRM YDRALSAPSS
     PTKADPSGRR SWEEPSWLGS SPRTLNHDMK QNVSRSLQTL PTSSSSFKPD SLHRGLARGG
     RPAKAELQRA RLRLSLQEHL WAFFHERVTI PSEEQSVARR AALDICAELR VFLHAKLPDM
     PLREMYLSGS LYDDLQVVTA DHAQLMVPLI LEKNLWSSIP GEDTIMNIPG FSLVRRENLE
     YFPRGSSYWD RCMVGGYLSP KSVLEVFEKL VAGSINWPAI GSVLDYVIRP VVPSETLTLE
     VQYETDRRLY VDFLPLLVME DGVSLIAKPH RLAAERHENL WRQSFRVAET AKLRALDQED
     AGCRSVCLKI LKAVCKLNPA LARLNASQLT NAILLLSEQE GDWTQEALAD RFMQLLRALV
     GHLEAGRMPC TLNLKVNLLC ELTPQEIDEL GYTLYCALSD PESLLRTV