ID   MID51_XENTR             Reviewed;         463 AA.
AC   Q52MA5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 49.
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;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) 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; BC090137; AAH90137.1; -; mRNA.
DR   RefSeq; NP_001025525.1; NM_001030354.1.
DR   AlphaFoldDB; Q52MA5; -.
DR   SMR; Q52MA5; -.
DR   GeneID; 594929; -.
DR   CTD; 54471; -.
DR   InParanoid; Q52MA5; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; 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..463
FT                   /note="Mitochondrial dynamics protein MID51"
FT                   /id="PRO_0000310453"
FT   TOPO_DOM        1..23
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..463
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          49..195
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          57..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..169
FT                   /note="Important for interaction with DNM1L"
FT                   /evidence="ECO:0000250"
FT   REGION          234..243
FT                   /note="Important for interaction with DNM1L"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  51293 MW;  0824AD44305C234D CRC64;
     MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
     TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT DSSTFDTDTF CPPRPKPVAR
     KGQVDLKKSR LRMSLQEKLL TYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
     LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY
     FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
     QYERDKHLFI DFLPSVTLGD TVLVAKPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
     SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS PDMLADRFLQ ALRGLISYLE
     AGVLPSALNP KVNLFAELTP EEIDELGYTL YCSLSEPEVL LQT