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P58281 (OPA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynamin-like 120 kDa protein, mitochondrial

EC=3.6.5.5
Alternative name(s):
Large GTP-binding protein
Short name=LargeG
Optic atrophy protein 1 homolog

Cleaved into the following chain:

  1. Dynamin-like 120 kDa protein, form S1
Gene names
Name:Opa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length960 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dynamin-related GTPase required for mitochondrial fusion and regulation of apoptosis. May form a diffusion barrier for proteins stored in mitochondrial cristae. Proteolytic processing in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space. Ref.4 Ref.5 Ref.6 Ref.8

Dynamin-like 120 kDa protein, form S1: Inactive form produced by cleavage at S1 position by OMA1 following stress conditions that induce loss of mitochondrial membrane potential, leading to negative regulation of mitochondrial fusion. Ref.4 Ref.5 Ref.6 Ref.8

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

Oligomeric complex consisting of membrane-bound and soluble forms of OPA1. Interacts with CHCHD3 and IMMT; these interactions occur preferentially with soluble OPA1 forms. Binds PARL. Interacts with PRELID1. Ref.4 Ref.5 Ref.7

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion intermembrane space Ref.4.

Post-translational modification

PARL-dependent proteolytic processing releases an antiapoptotic soluble form not required for mitochondrial fusion. Cleaved by OMA1 at position S1 following stress conditions.

Disruption phenotype

Embryonic fibroblasts show a defect in apoptosis in response to intrinsic signals. This defect can be complemented by a soluble form of Opa1 targeted to the mitochondrial intermembrane space. Ref.4

Sequence similarities

Belongs to the dynamin family.

Sequence caution

The sequence AAH25160.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
Sensory transduction
Vision
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transit peptide
Transmembrane
Transmembrane helix
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement Ref.1. Source: GOC

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

inner mitochondrial membrane organization

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial fusion

Inferred from direct assay Ref.6. Source: MGI

mitochondrion organization

Non-traceable author statement Ref.1. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.4. Source: UniProtKB

negative regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype Ref.4. Source: UniProtKB

neural tube closure

Inferred from mutant phenotype PubMed 15755804. Source: MGI

response to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

visual perception

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentdendrite

Inferred from direct assay Ref.1. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial crista

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from mutant phenotype Ref.4. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrial outer membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.1PubMed 14651853PubMed 17035996PubMed 18614015. Source: MGI

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P58281-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P58281-2)

The sequence of this isoform differs from the canonical sequence as follows:
     208-208: K → KGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8787Mitochondrion By similarity
Chain88 – 960873Dynamin-like 120 kDa protein, mitochondrial
PRO_0000007398
Chain195 – 960766Dynamin-like 120 kDa protein, form S1 By similarity
PRO_0000253480

Regions

Topological domain88 – 969Mitochondrial matrix Potential
Transmembrane97 – 11317Helical; Potential
Topological domain114 – 960847Mitochondrial intermembrane Potential
Nucleotide binding295 – 3028GTP Potential
Nucleotide binding398 – 4025GTP Potential
Nucleotide binding467 – 4704GTP Potential
Coiled coil210 – 25445 Potential
Coiled coil895 – 96066 Potential

Amino acid modifications

Modified residue2281N6-acetyllysine By similarity

Natural variations

Alternative sequence2081K → KGLLGELILLQQQIQEHEEE ARRAAGQYSTSYAQQKRK in isoform 2.
VSP_021037

Experimental info

Sequence conflict2361L → P in BAC30002. Ref.2
Sequence conflict330 – 3312TL → NN in BAC32021. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 26, 2001. Version 1.
Checksum: 0F103FB1FD570F49

FASTA960111,339
        10         20         30         40         50         60 
MWRAGRAAVA CEVCQSLVKH SSGIQRNVPL QKLHLVSRSI YRSHHPALKL QRPQLRTPFQ 

        70         80         90        100        110        120 
QFSSLTHLSL HKLKLSPIKY GYQPRRNFWP ARLAARLLKL RYIILGSAVG GGYTAKKTFD 

       130        140        150        160        170        180 
EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE KIRKALPSSE DLASLAPDLD KITESLSLLK 

       190        200        210        220        230        240 
DFFTAGSPGE TAFRATDHGS ESDKHYRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN 

       250        260        270        280        290        300 
KELRKLVLQK DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG 

       310        320        330        340        350        360 
KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL TKEEDLAALR 

       370        380        390        400        410        420 
HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP GVINTVTSGM APDTKETIFS 

       430        440        450        460        470        480 
ISKAYMQNPN AIILCIQDGS VDAERSIVTD LVSQMDPHGR RTIFVLTKVD LAEKNVASPS 

       490        500        510        520        530        540 
RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT 

       550        560        570        580        590        600 
TRNLSLAVSD CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE 

       610        620        630        640        650        660 
ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW 

       670        680        690        700        710        720 
TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED 

       730        740        750        760        770        780 
SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQGRLKDTE NAIENMIGPD WKKRWMYWKN 

       790        800        810        820        830        840 
RTQEQCVHNE TKNELEKMLK VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV 

       850        860        870        880        890        900 
YRRHFLKTAL NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN 

       910        920        930        940        950        960 
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK 

« Hide

Isoform 2 [UniParc].

Checksum: FADCB1430E585522
Show »

FASTA997115,593

References

« Hide 'large scale' references
[1]"Primary structure of a dynamin-related mouse mitochondrial GTPase and its distribution in brain, subcellular localization, and effect on mitochondrial morphology."
Misaka T., Miyashita T., Kubo Y.
J. Biol. Chem. 277:15834-15842(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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. expand/collapse author list , 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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-365 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Blastocyst, Hypothalamus, Liver, Retina and Skin.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Czech II.
Tissue: Brain and Mammary gland.
[4]"Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling."
Cipolat S., Rudka T., Hartmann D., Costa V., Serneels L., Craessaerts K., Metzger K., Frezza C., Annaert W., D'Adamio L., Derks C., Dejaegere T., Pellegrini L., D'Hooge R., Scorrano L., De Strooper B.
Cell 126:163-175(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARL, DISRUPTION PHENOTYPE.
[5]"OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion."
Frezza C., Cipolat S., Martins de Brito O., Micaroni M., Beznoussenko G.V., Rudka T., Bartoli D., Polishuck R.S., Danial N.N., De Strooper B., Scorrano L.
Cell 126:177-189(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[6]"Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1."
Ehses S., Raschke I., Mancuso G., Bernacchia A., Geimer S., Tondera D., Martinou J.C., Westermann B., Rugarli E.I., Langer T.
J. Cell Biol. 187:1023-1036(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.
[7]"ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function."
Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S.
J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHCHD3, IMMT.
[8]"Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1 and causes obesity and defective thermogenesis in mice."
Quiros P.M., Ramsay A.J., Sala D., Fernandez-Vizarra E., Rodriguez F., Peinado J.R., Fernandez-Garcia M.S., Vega J.A., Enriquez J.A., Zorzano A., Lopez-Otin C.
EMBO J. 31:2117-2133(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB044138 mRNA. Translation: BAB59000.1.
AK029157 mRNA. Translation: BAC26331.1.
AK038446 mRNA. Translation: BAC30002.1.
AK044657 mRNA. Translation: BAC32021.1.
AK050383 mRNA. Translation: BAC34224.1.
AK145620 mRNA. Translation: BAE26544.1.
BC025160 mRNA. Translation: AAH25160.1. Different initiation.
BC138665 mRNA. Translation: AAI38666.1.
BC145959 mRNA. Translation: AAI45960.1.
RefSeqNP_598513.1. NM_133752.3.
XP_006522720.1. XM_006522657.1.
UniGeneMm.274285.

3D structure databases

ProteinModelPortalP58281.
SMRP58281. Positions 262-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP58281. 7 interactions.
MINTMINT-4105859.

PTM databases

PhosphoSiteP58281.

Proteomic databases

PaxDbP58281.
PRIDEP58281.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000160597; ENSMUSP00000124223; ENSMUSG00000038084. [P58281-1]
ENSMUST00000161186; ENSMUSP00000123880; ENSMUSG00000038084. [P58281-2]
GeneID74143.
KEGGmmu:74143.
UCSCuc007ywf.2. mouse. [P58281-1]

Organism-specific databases

CTD4976.
MGIMGI:1921393. Opa1.

Phylogenomic databases

eggNOGCOG0699.
GeneTreeENSGT00550000074851.
HOVERGENHBG019108.
KOK17079.
OMAKRHKWNE.
OrthoDBEOG7TMZR4.
PhylomeDBP58281.
TreeFamTF314250.

Gene expression databases

ArrayExpressP58281.
BgeeP58281.
CleanExMM_OPA1.
GenevestigatorP58281.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR027740. OPA1.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PTHR11566:SF8. PTHR11566:SF8. 1 hit.
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSOPA1. mouse.
NextBio339890.
PROP58281.
SOURCESearch...

Entry information

Entry nameOPA1_MOUSE
AccessionPrimary (citable) accession number: P58281
Secondary accession number(s): A6H6Q3 expand/collapse secondary AC list , Q3ULA5, Q8BKU7, Q8BLL3, Q8BM08, Q8R3J7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot