MID51_RAT
ID MID51_RAT Reviewed; 463 AA.
AC Q5XIS8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC083593; AAH83593.1; -; mRNA.
DR RefSeq; NP_001007710.1; NM_001007709.1.
DR RefSeq; XP_006242143.1; XM_006242081.2.
DR RefSeq; XP_006242145.1; XM_006242083.3.
DR RefSeq; XP_008763940.1; XM_008765718.2.
DR AlphaFoldDB; Q5XIS8; -.
DR SMR; Q5XIS8; -.
DR STRING; 10116.ENSRNOP00000023843; -.
DR iPTMnet; Q5XIS8; -.
DR PhosphoSitePlus; Q5XIS8; -.
DR PaxDb; Q5XIS8; -.
DR PRIDE; Q5XIS8; -.
DR Ensembl; ENSRNOT00000092569; ENSRNOP00000075752; ENSRNOG00000017553.
DR GeneID; 315141; -.
DR KEGG; rno:315141; -.
DR UCSC; RGD:1359173; rat.
DR CTD; 54471; -.
DR RGD; 1359173; Mief1.
DR VEuPathDB; HostDB:ENSRNOG00000067422; -.
DR eggNOG; KOG4542; Eukaryota.
DR GeneTree; ENSGT00390000013127; -.
DR HOGENOM; CLU_046803_0_0_1; -.
DR InParanoid; Q5XIS8; -.
DR OMA; CEKEGDW; -.
DR OrthoDB; 515815at2759; -.
DR PhylomeDB; Q5XIS8; -.
DR TreeFam; TF331032; -.
DR PRO; PR:Q5XIS8; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000017553; Expressed in skeletal muscle tissue and 18 other tissues.
DR ExpressionAtlas; Q5XIS8; baseline and differential.
DR Genevisible; Q5XIS8; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISO:RGD.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISO:RGD.
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 1: Evidence at protein 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_0000310451"
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 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:0007744|PubMed:22673903"
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; 51309 MW; 1A079546AE474513 CRC64;
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
TRLSHSGKRS WEEPNWMGSP RLLNRDMKTG LSRSLQTLPT DSSAFDTDTF CPPRPKPLAR
RGQVDLKKSR LRMSLQEKLL SYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNIPGF FLVRRENPEY
FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
QYERDKHLVI DFLPSVTLGD TVLVARPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
SLCLKILKAI CKSTPALGHL TASQLTNVIL HLSQEEADWS PDMLADRFLQ ALRGLISYLE
AGVLPSALNP KVNLFAELTP HEIDELGYTL YCSLSEPEVL LQT
