MID51_MOUSE
ID MID51_MOUSE Reviewed; 463 AA.
AC Q8BGV8; Q8C4Y9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, Pancreas, Retina, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION.
RX PubMed=23283981; DOI=10.1091/mbc.e12-10-0721;
RA Loson O.C., Song Z., Chen H., Chan D.C.;
RT "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
RT fission.";
RL Mol. Biol. Cell 24:659-667(2013).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 134-463 IN COMPLEX WITH ADP,
RP NUCLEOTIDE-BINDING, FUNCTION, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-189; HIS-201 AND LYS-368,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=24508339; DOI=10.1016/j.str.2014.01.001;
RA Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O., Chan D.C.;
RT "The mitochondrial fission receptor Mid51 requires ADP as a cofactor.";
RL Structure 22:367-377(2014).
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. {ECO:0000269|PubMed:23283981,
CC ECO:0000269|PubMed:24508339}.
CC -!- SUBUNIT: Homodimer. Interacts with DNM1L.
CC {ECO:0000269|PubMed:24508339}.
CC -!- INTERACTION:
CC Q8BGV8; Q8K1M6: Dnm1l; NbExp=2; IntAct=EBI-16092561, EBI-2365792;
CC Q8BGV8; Q8K1M6-3: Dnm1l; NbExp=5; IntAct=EBI-16092561, EBI-16092613;
CC Q8BGV8; Q8BGV8: Mief1; NbExp=2; IntAct=EBI-16092561, EBI-16092561;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24508339}; Single-pass membrane protein
CC {ECO:0000269|PubMed:24508339}.
CC -!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}.
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DR EMBL; AK038466; BAC30010.1; -; mRNA.
DR EMBL; AK044773; BAC32082.1; -; mRNA.
DR EMBL; AK050546; BAC34317.1; -; mRNA.
DR EMBL; AK080375; BAC37896.1; -; mRNA.
DR CCDS; CCDS27661.1; -.
DR RefSeq; NP_848834.2; NM_178719.5.
DR RefSeq; XP_006521009.1; XM_006520946.3.
DR RefSeq; XP_006521010.1; XM_006520947.3.
DR PDB; 4OAF; X-ray; 2.20 A; A/B/C/D=134-463.
DR PDB; 4OAG; X-ray; 2.00 A; A/B=134-463.
DR PDB; 4OAH; X-ray; 2.00 A; A/B/C/D=134-463.
DR PDB; 4OAI; X-ray; 2.00 A; Z=134-463.
DR PDBsum; 4OAF; -.
DR PDBsum; 4OAG; -.
DR PDBsum; 4OAH; -.
DR PDBsum; 4OAI; -.
DR AlphaFoldDB; Q8BGV8; -.
DR SMR; Q8BGV8; -.
DR CORUM; Q8BGV8; -.
DR DIP; DIP-60660N; -.
DR IntAct; Q8BGV8; 1.
DR STRING; 10090.ENSMUSP00000023048; -.
DR iPTMnet; Q8BGV8; -.
DR PhosphoSitePlus; Q8BGV8; -.
DR jPOST; Q8BGV8; -.
DR MaxQB; Q8BGV8; -.
DR PaxDb; Q8BGV8; -.
DR PRIDE; Q8BGV8; -.
DR ProteomicsDB; 292325; -.
DR Antibodypedia; 26626; 158 antibodies from 25 providers.
DR DNASU; 239555; -.
DR Ensembl; ENSMUST00000023048; ENSMUSP00000023048; ENSMUSG00000022412.
DR Ensembl; ENSMUST00000166030; ENSMUSP00000129209; ENSMUSG00000022412.
DR Ensembl; ENSMUST00000229138; ENSMUSP00000154875; ENSMUSG00000022412.
DR GeneID; 239555; -.
DR KEGG; mmu:239555; -.
DR UCSC; uc007wvh.2; mouse.
DR CTD; 54471; -.
DR MGI; MGI:2146020; Mief1.
DR VEuPathDB; HostDB:ENSMUSG00000022412; -.
DR eggNOG; KOG4542; Eukaryota.
DR GeneTree; ENSGT00390000013127; -.
DR HOGENOM; CLU_046803_0_0_1; -.
DR InParanoid; Q8BGV8; -.
DR OMA; CEKEGDW; -.
DR OrthoDB; 515815at2759; -.
DR PhylomeDB; Q8BGV8; -.
DR TreeFam; TF331032; -.
DR BioGRID-ORCS; 239555; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Mief1; mouse.
DR PRO; PR:Q8BGV8; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BGV8; protein.
DR Bgee; ENSMUSG00000022412; Expressed in animal zygote and 230 other tissues.
DR ExpressionAtlas; Q8BGV8; baseline and differential.
DR Genevisible; Q8BGV8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISO:MGI.
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 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..463
FT /note="Mitochondrial dynamics protein MID51"
FT /id="PRO_0000310449"
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:0000269|PubMed:24508339"
FT BINDING 187
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
FT BINDING 189
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
FT BINDING 201
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
FT BINDING 340
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
FT BINDING 342
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
FT BINDING 368
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:24508339"
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:0007744|PubMed:21183079"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQG6"
FT MUTAGEN 189
FT /note="S->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24508339"
FT MUTAGEN 201
FT /note="H->A: Abolishes ADP binding."
FT /evidence="ECO:0000269|PubMed:24508339"
FT MUTAGEN 234..237
FT /note="RREN->AAEA: Abolishes interaction with DNM1L."
FT MUTAGEN 239..243
FT /note="EYFPR->AAFPA: Impairs interaction with DNM1L."
FT MUTAGEN 253..255
FT /note="VGG->EEE: Impairs interaction with DNM1L."
FT MUTAGEN 368
FT /note="K->A: Mildly reduces affinity for ADP."
FT /evidence="ECO:0000269|PubMed:24508339"
FT CONFLICT 444
FT /note="D -> N (in Ref. 1; BAC37896)"
FT /evidence="ECO:0000305"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 151..173
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4OAF"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4OAG"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:4OAG"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:4OAH"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 306..318
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 342..356
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 382..395
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 404..421
FT /evidence="ECO:0007829|PDB:4OAG"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:4OAF"
FT TURN 434..437
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 440..453
FT /evidence="ECO:0007829|PDB:4OAG"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:4OAG"
SQ SEQUENCE 463 AA; 51184 MW; 69C8869807974024 CRC64;
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
TRLSHSGKRS WEEPNWMGSP RLLNKDMKAG LSRSLQTLPT DSSAFDTDTF CPPRPKPLAR
RGQVDLKKSR LRMSLQEKLL SYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY
FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
QYEKDKHLVI DFLPSVTLGD TVLVARPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS PDMLADRFLQ ALRGLISYLE
AGVLPSALNP KVNLFAELTP QEIDELGYTL YCSLSEPEVL LQT
