MID51_PONAB
ID MID51_PONAB Reviewed; 463 AA.
AC Q5RBN0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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.
CC Binds ADP and can also bind GDP, although with lower affinity. Does not
CC bind CDP, UDP, ATP, AMP or GTP. Inhibits DNM1L GTPase activity in the
CC absence of bound ADP. Requires ADP to stimulate DNM1L GTPase activity
CC and the assembly of DNM1L into long, oligomeric tubules with a spiral
CC pattern, as opposed to the ring-like DNM1L oligomers observed in the
CC absence of bound ADP. Does not require ADP for its function in
CC recruiting DNM1L (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L (By similarity).
CC {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; CR858608; CAH90830.1; -; mRNA.
DR RefSeq; NP_001125473.1; NM_001132001.1.
DR AlphaFoldDB; Q5RBN0; -.
DR SMR; Q5RBN0; -.
DR STRING; 9601.ENSPPYP00000024294; -.
DR GeneID; 100172382; -.
DR KEGG; pon:100172382; -.
DR CTD; 54471; -.
DR eggNOG; KOG4542; Eukaryota.
DR InParanoid; Q5RBN0; -.
DR Proteomes; UP000001595; 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:0000266; P:mitochondrial fission; ISS:UniProtKB.
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_0000310450"
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..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..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"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG6"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG6"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGV8"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG6"
SQ SEQUENCE 463 AA; 51199 MW; CAFEBA4D12715D93 CRC64;
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
TRLSHSGKRS WEEPNWMGSP QLLNRDMKTG LSRSLQTLPT DSSAFDTDTF CPPRPKPVAR
KGQVDLKKSR LRMSLQEKLL PYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
LRDVYLSGSL 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
