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Mitochondrial dynamics protein MID51 (Mitochondrial dynamics protein of 51 kDa homolog) (Mitochondrial elongation factor 1) (Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like)

 MID51_MOUSE             Reviewed;         463 AA.
Q8BGV8; Q8C4Y9;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 112.
RecName: Full=Mitochondrial dynamics protein MID51;
AltName: Full=Mitochondrial dynamics protein of 51 kDa homolog;
AltName: Full=Mitochondrial elongation factor 1;
AltName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like;
Name=Mief1; Synonyms=Mid51, Smcr7l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Hypothalamus, Pancreas, Retina, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Brown adipose tissue;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[3]
FUNCTION.
PubMed=23283981; DOI=10.1091/mbc.E12-10-0721;
Loson O.C., Song Z., Chen H., Chan D.C.;
"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial
fission.";
Mol. Biol. Cell 24:659-667(2013).
[4]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 134-463 IN COMPLEX WITH ADP,
NUCLEOTIDE-BINDING, FUNCTION, PARTIAL PROTEIN SEQUENCE, INTERACTION
WITH DNM1L, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-189; HIS-201 AND
LYS-368, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=24508339; DOI=10.1016/j.str.2014.01.001;
Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O.,
Chan D.C.;
"The mitochondrial fission receptor Mid51 requires ADP as a
cofactor.";
Structure 22:367-377(2014).
-!- FUNCTION: Mitochondrial outer membrane protein which regulates
mitochondrial fission. Promotes the recruitment and association of
the fission mediator dynamin-related protein 1 (DNM1L) to the
mitochondrial surface independently of the mitochondrial fission
FIS1 and MFF proteins. Regulates DNM1L GTPase activity and DNM1L
oligomerization. Binds ADP and can also bind GDP, although with
lower affinity. Does not bind CDP, UDP, ATP, AMP or GTP. Inhibits
DNM1L GTPase activity in the absence of bound ADP. Requires ADP to
stimulate DNM1L GTPase activity and the assembly of DNM1L into
long, oligomeric tubules with a spiral pattern, as opposed to the
ring-like DNM1L oligomers observed in the absence of bound ADP.
Does not require ADP for its function in recruiting DNM1L.
{ECO:0000269|PubMed:23283981, ECO:0000269|PubMed:24508339}.
-!- SUBUNIT: Homodimer. Interacts with DNM1L.
{ECO:0000269|PubMed:24508339}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-16092561, EBI-16092561;
Q8K1M6-3:Dnm1l; NbExp=5; IntAct=EBI-16092561, EBI-16092613;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:24508339}; Single-pass membrane protein
{ECO:0000269|PubMed:24508339}.
-!- SIMILARITY: Belongs to the MID49/MID51 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK038466; BAC30010.1; -; mRNA.
EMBL; AK044773; BAC32082.1; -; mRNA.
EMBL; AK050546; BAC34317.1; -; mRNA.
EMBL; AK080375; BAC37896.1; -; mRNA.
CCDS; CCDS27661.1; -.
RefSeq; NP_848834.2; NM_178719.5.
RefSeq; XP_006521009.1; XM_006520946.3.
RefSeq; XP_006521010.1; XM_006520947.3.
UniGene; Mm.307163; -.
PDB; 4OAF; X-ray; 2.20 A; A/B/C/D=134-463.
PDB; 4OAG; X-ray; 2.00 A; A/B=134-463.
PDB; 4OAH; X-ray; 2.00 A; A/B/C/D=134-463.
PDB; 4OAI; X-ray; 2.00 A; Z=134-463.
PDBsum; 4OAF; -.
PDBsum; 4OAG; -.
PDBsum; 4OAH; -.
PDBsum; 4OAI; -.
ProteinModelPortal; Q8BGV8; -.
SMR; Q8BGV8; -.
CORUM; Q8BGV8; -.
DIP; DIP-60660N; -.
IntAct; Q8BGV8; 1.
STRING; 10090.ENSMUSP00000023048; -.
iPTMnet; Q8BGV8; -.
PhosphoSitePlus; Q8BGV8; -.
MaxQB; Q8BGV8; -.
PaxDb; Q8BGV8; -.
PRIDE; Q8BGV8; -.
Ensembl; ENSMUST00000023048; ENSMUSP00000023048; ENSMUSG00000022412.
Ensembl; ENSMUST00000166030; ENSMUSP00000129209; ENSMUSG00000022412.
Ensembl; ENSMUST00000229138; ENSMUSP00000154875; ENSMUSG00000022412.
GeneID; 239555; -.
KEGG; mmu:239555; -.
UCSC; uc007wvh.2; mouse.
CTD; 54471; -.
MGI; MGI:2146020; Mief1.
eggNOG; ENOG410IK9T; Eukaryota.
eggNOG; ENOG41109RH; LUCA.
GeneTree; ENSGT00390000013127; -.
HOGENOM; HOG000038002; -.
HOVERGEN; HBG054078; -.
InParanoid; Q8BGV8; -.
OMA; EDTIMNI; -.
OrthoDB; EOG091G079I; -.
PhylomeDB; Q8BGV8; -.
TreeFam; TF331032; -.
PRO; PR:Q8BGV8; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022412; Expressed in 243 organ(s), highest expression level in cardiac ventricle.
ExpressionAtlas; Q8BGV8; baseline and differential.
Genevisible; Q8BGV8; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0043531; F:ADP binding; ISO:MGI.
GO; GO:0019003; F:GDP binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
InterPro; IPR024810; Mab-21_dom.
Pfam; PF03281; Mab-21; 1.
SMART; SM01265; Mab-21; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 463 Mitochondrial dynamics protein MID51.
/FTId=PRO_0000310449.
TOPO_DOM 1 23 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 24 46 Helical. {ECO:0000255}.
TOPO_DOM 47 463 Cytoplasmic. {ECO:0000255}.
REGION 49 195 Dimerization. {ECO:0000250}.
REGION 160 169 Important for interaction with DNM1L.
{ECO:0000250}.
REGION 234 243 Important for interaction with DNM1L.
{ECO:0000269|PubMed:24508339}.
BINDING 187 187 ADP. {ECO:0000269|PubMed:24508339}.
BINDING 189 189 ADP. {ECO:0000269|PubMed:24508339}.
BINDING 201 201 ADP. {ECO:0000269|PubMed:24508339}.
BINDING 340 340 ADP. {ECO:0000269|PubMed:24508339}.
BINDING 342 342 ADP. {ECO:0000269|PubMed:24508339}.
BINDING 368 368 ADP. {ECO:0000269|PubMed:24508339}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQG6}.
MOD_RES 59 59 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQG6}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQG6}.
MUTAGEN 189 189 S->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24508339}.
MUTAGEN 201 201 H->A: Abolishes ADP binding.
{ECO:0000269|PubMed:24508339}.
MUTAGEN 234 237 RREN->AAEA: Abolishes interaction with
DNM1L.
MUTAGEN 239 243 EYFPR->AAFPA: Impairs interaction with
DNM1L.
MUTAGEN 253 255 VGG->EEE: Impairs interaction with DNM1L.
MUTAGEN 368 368 K->A: Mildly reduces affinity for ADP.
{ECO:0000269|PubMed:24508339}.
CONFLICT 444 444 D -> N (in Ref. 1; BAC37896).
{ECO:0000305}.
HELIX 135 145 {ECO:0000244|PDB:4OAG}.
HELIX 151 173 {ECO:0000244|PDB:4OAG}.
STRAND 179 181 {ECO:0000244|PDB:4OAF}.
STRAND 185 188 {ECO:0000244|PDB:4OAG}.
TURN 189 193 {ECO:0000244|PDB:4OAG}.
STRAND 201 208 {ECO:0000244|PDB:4OAG}.
STRAND 214 219 {ECO:0000244|PDB:4OAG}.
HELIX 220 222 {ECO:0000244|PDB:4OAG}.
STRAND 230 235 {ECO:0000244|PDB:4OAG}.
TURN 238 240 {ECO:0000244|PDB:4OAG}.
HELIX 247 251 {ECO:0000244|PDB:4OAG}.
HELIX 259 269 {ECO:0000244|PDB:4OAG}.
HELIX 271 273 {ECO:0000244|PDB:4OAG}.
HELIX 276 282 {ECO:0000244|PDB:4OAG}.
STRAND 286 289 {ECO:0000244|PDB:4OAG}.
STRAND 292 294 {ECO:0000244|PDB:4OAH}.
STRAND 297 303 {ECO:0000244|PDB:4OAG}.
STRAND 306 318 {ECO:0000244|PDB:4OAG}.
STRAND 321 324 {ECO:0000244|PDB:4OAG}.
HELIX 331 333 {ECO:0000244|PDB:4OAG}.
STRAND 337 339 {ECO:0000244|PDB:4OAG}.
HELIX 342 356 {ECO:0000244|PDB:4OAG}.
HELIX 360 373 {ECO:0000244|PDB:4OAG}.
HELIX 375 377 {ECO:0000244|PDB:4OAG}.
HELIX 382 395 {ECO:0000244|PDB:4OAG}.
HELIX 401 403 {ECO:0000244|PDB:4OAG}.
HELIX 404 421 {ECO:0000244|PDB:4OAG}.
STRAND 427 429 {ECO:0000244|PDB:4OAF}.
TURN 434 437 {ECO:0000244|PDB:4OAG}.
HELIX 440 453 {ECO:0000244|PDB:4OAG}.
HELIX 457 460 {ECO:0000244|PDB:4OAG}.
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


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