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Protein

Mitochondrial dynamics protein MID51

Gene

Mief1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871ADP1 Publication
Binding sitei189 – 1891ADP1 Publication
Binding sitei201 – 2011ADP1 Publication
Binding sitei340 – 3401ADP1 Publication
Binding sitei342 – 3421ADP1 Publication
Binding sitei368 – 3681ADP1 Publication

GO - Molecular functioni

GO - Biological processi

  • mitochondrial fission Source: UniProtKB
  • positive regulation of mitochondrial fission Source: UniProtKB
  • positive regulation of protein targeting to membrane Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial dynamics protein MID51
Alternative name(s):
Mitochondrial dynamics protein of 51 kDa homolog
Mitochondrial elongation factor 1
Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like
Gene namesi
Name:Mief1
Synonyms:Mid51, Smcr7l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2146020. Mief1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei24 – 4623HelicalSequence analysisAdd
BLAST
Topological domaini47 – 463417CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891S → A: Abolishes ADP binding. 1 Publication
Mutagenesisi201 – 2011H → A: Abolishes ADP binding. 1 Publication
Mutagenesisi234 – 2374RREN → AAEA: Abolishes interaction with DNM1L.
Mutagenesisi239 – 2435EYFPR → AAFPA: Impairs interaction with DNM1L.
Mutagenesisi253 – 2553VGG → EEE: Impairs interaction with DNM1L.
Mutagenesisi368 – 3681K → A: Mildly reduces affinity for ADP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463Mitochondrial dynamics protein MID51PRO_0000310449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551PhosphoserineBy similarity
Modified residuei59 – 591PhosphoserineBy similarity
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei94 – 941PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BGV8.
MaxQBiQ8BGV8.
PaxDbiQ8BGV8.
PRIDEiQ8BGV8.

PTM databases

iPTMnetiQ8BGV8.
PhosphoSiteiQ8BGV8.

Expressioni

Gene expression databases

BgeeiQ8BGV8.
ExpressionAtlasiQ8BGV8. baseline and differential.
GenevisibleiQ8BGV8. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with DNM1L.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60660N.
STRINGi10090.ENSMUSP00000023048.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi135 – 14511Combined sources
Helixi151 – 17323Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi185 – 1884Combined sources
Turni189 – 1935Combined sources
Beta strandi201 – 2088Combined sources
Beta strandi214 – 2196Combined sources
Helixi220 – 2223Combined sources
Beta strandi230 – 2356Combined sources
Turni238 – 2403Combined sources
Helixi247 – 2515Combined sources
Helixi259 – 26911Combined sources
Helixi271 – 2733Combined sources
Helixi276 – 2827Combined sources
Beta strandi286 – 2894Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi297 – 3037Combined sources
Beta strandi306 – 31813Combined sources
Beta strandi321 – 3244Combined sources
Helixi331 – 3333Combined sources
Beta strandi337 – 3393Combined sources
Helixi342 – 35615Combined sources
Helixi360 – 37314Combined sources
Helixi375 – 3773Combined sources
Helixi382 – 39514Combined sources
Helixi401 – 4033Combined sources
Helixi404 – 42118Combined sources
Beta strandi427 – 4293Combined sources
Turni434 – 4374Combined sources
Helixi440 – 45314Combined sources
Helixi457 – 4604Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OAFX-ray2.20A/B/C/D134-463[»]
4OAGX-ray2.00A/B134-463[»]
4OAHX-ray2.00A/B/C/D134-463[»]
4OAIX-ray2.00Z134-463[»]
ProteinModelPortaliQ8BGV8.
SMRiQ8BGV8. Positions 134-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 195147DimerizationBy similarityAdd
BLAST
Regioni160 – 16910Important for interaction with DNM1LBy similarity
Regioni234 – 24310Important for interaction with DNM1L

Sequence similaritiesi

Belongs to the MID49/MID51 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IK9T. Eukaryota.
ENOG41109RH. LUCA.
GeneTreeiENSGT00390000013127.
HOGENOMiHOG000038002.
HOVERGENiHBG054078.
InParanoidiQ8BGV8.
OMAiSTHNDAV.
OrthoDBiEOG7K9K2S.
PhylomeDBiQ8BGV8.
TreeFamiTF331032.

Family and domain databases

InterProiIPR024810. Mab-21_dom.
[Graphical view]
PfamiPF03281. Mab-21. 1 hit.
[Graphical view]
SMARTiSM01265. Mab-21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY
60 70 80 90 100
DRAISAPTSP TRLSHSGKRS WEEPNWMGSP RLLNKDMKAG LSRSLQTLPT
110 120 130 140 150
DSSAFDTDTF CPPRPKPLAR RGQVDLKKSR LRMSLQEKLL SYYRNRAAIP
160 170 180 190 200
AGEQARAKQA AVDICAELRS FLRAKLPDMP LRDMYLSGSL YDDLQVVTAD
210 220 230 240 250
HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY FPRGSSYWDR
260 270 280 290 300
CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
310 320 330 340 350
QYEKDKHLVI DFLPSVTLGD TVLVARPHRL AQYDNLWRLS LRPAETARLR
360 370 380 390 400
ALDQADSGCR SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS
410 420 430 440 450
PDMLADRFLQ ALRGLISYLE AGVLPSALNP KVNLFAELTP QEIDELGYTL
460
YCSLSEPEVL LQT
Length:463
Mass (Da):51,184
Last modified:March 1, 2003 - v1
Checksum:i69C8869807974024
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti444 – 4441D → N in BAC37896 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038466 mRNA. Translation: BAC30010.1.
AK044773 mRNA. Translation: BAC32082.1.
AK050546 mRNA. Translation: BAC34317.1.
AK080375 mRNA. Translation: BAC37896.1.
CCDSiCCDS27661.1.
RefSeqiNP_848834.2. NM_178719.5.
XP_006521009.1. XM_006520946.2.
XP_006521010.1. XM_006520947.2.
UniGeneiMm.307163.

Genome annotation databases

EnsembliENSMUST00000023048; ENSMUSP00000023048; ENSMUSG00000022412.
ENSMUST00000166030; ENSMUSP00000129209; ENSMUSG00000022412.
GeneIDi239555.
KEGGimmu:239555.
UCSCiuc007wvh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK038466 mRNA. Translation: BAC30010.1.
AK044773 mRNA. Translation: BAC32082.1.
AK050546 mRNA. Translation: BAC34317.1.
AK080375 mRNA. Translation: BAC37896.1.
CCDSiCCDS27661.1.
RefSeqiNP_848834.2. NM_178719.5.
XP_006521009.1. XM_006520946.2.
XP_006521010.1. XM_006520947.2.
UniGeneiMm.307163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OAFX-ray2.20A/B/C/D134-463[»]
4OAGX-ray2.00A/B134-463[»]
4OAHX-ray2.00A/B/C/D134-463[»]
4OAIX-ray2.00Z134-463[»]
ProteinModelPortaliQ8BGV8.
SMRiQ8BGV8. Positions 134-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60660N.
STRINGi10090.ENSMUSP00000023048.

PTM databases

iPTMnetiQ8BGV8.
PhosphoSiteiQ8BGV8.

Proteomic databases

EPDiQ8BGV8.
MaxQBiQ8BGV8.
PaxDbiQ8BGV8.
PRIDEiQ8BGV8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023048; ENSMUSP00000023048; ENSMUSG00000022412.
ENSMUST00000166030; ENSMUSP00000129209; ENSMUSG00000022412.
GeneIDi239555.
KEGGimmu:239555.
UCSCiuc007wvh.2. mouse.

Organism-specific databases

CTDi54471.
MGIiMGI:2146020. Mief1.

Phylogenomic databases

eggNOGiENOG410IK9T. Eukaryota.
ENOG41109RH. LUCA.
GeneTreeiENSGT00390000013127.
HOGENOMiHOG000038002.
HOVERGENiHBG054078.
InParanoidiQ8BGV8.
OMAiSTHNDAV.
OrthoDBiEOG7K9K2S.
PhylomeDBiQ8BGV8.
TreeFamiTF331032.

Miscellaneous databases

NextBioi384173.
PROiQ8BGV8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGV8.
ExpressionAtlasiQ8BGV8. baseline and differential.
GenevisibleiQ8BGV8. MM.

Family and domain databases

InterProiIPR024810. Mab-21_dom.
[Graphical view]
PfamiPF03281. Mab-21. 1 hit.
[Graphical view]
SMARTiSM01265. Mab-21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hypothalamus, Pancreas, Retina and Thymus.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Brown adipose tissue.
  3. "Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
    Loson O.C., Song Z., Chen H., Chan D.C.
    Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "The mitochondrial fission receptor Mid51 requires ADP as a cofactor."
    Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O., Chan D.C.
    Structure 22:367-377(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiMID51_MOUSE
AccessioniPrimary (citable) accession number: Q8BGV8
Secondary accession number(s): Q8C4Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.