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P58281

- OPA1_MOUSE

UniProt

P58281 - OPA1_MOUSE

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Protein
Dynamin-like 120 kDa protein, mitochondrial
Gene
Opa1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications
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.4 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi295 – 3028GTP Reviewed prediction
Nucleotide bindingi398 – 4025GTP Reviewed prediction
Nucleotide bindingi467 – 4704GTP Reviewed prediction

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. GTPase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. apoptotic process Source: UniProtKB-KW
  3. inner mitochondrial membrane organization Source: UniProtKB
  4. mitochondrial fusion Source: MGI
  5. mitochondrion organization Source: UniProtKB
  6. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  7. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
  8. neural tube closure Source: MGI
  9. response to stimulus Source: UniProtKB-KW
  10. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Sensory transduction, Vision

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:Opa1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1921393. Opa1.

Subcellular locationi

Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion intermembrane space 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini88 – 969Mitochondrial matrix Reviewed prediction
Transmembranei97 – 11317Helical; Reviewed prediction
Add
BLAST
Topological domaini114 – 960847Mitochondrial intermembrane Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. dendrite Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial crista Source: UniProtKB
  4. mitochondrial inner membrane Source: UniProtKB
  5. mitochondrial intermembrane space Source: UniProtKB
  6. mitochondrial outer membrane Source: UniProtKB
  7. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8787Mitochondrion By similarity
Add
BLAST
Chaini88 – 960873Dynamin-like 120 kDa protein, mitochondrial
PRO_0000007398Add
BLAST
Chaini195 – 960766Dynamin-like 120 kDa protein, form S1 By similarity
PRO_0000253480Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281N6-acetyllysine By similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP58281.
PaxDbiP58281.
PRIDEiP58281.

PTM databases

PhosphoSiteiP58281.

Expressioni

Gene expression databases

ArrayExpressiP58281.
BgeeiP58281.
CleanExiMM_OPA1.
GenevestigatoriP58281.

Interactioni

Subunit structurei

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 PRELID1.3 Publications

Protein-protein interaction databases

IntActiP58281. 7 interactions.
MINTiMINT-4105859.

Structurei

3D structure databases

ProteinModelPortaliP58281.
SMRiP58281. Positions 262-601.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini285 – 561277Dynamin-type G
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili210 – 25445 Reviewed prediction
Add
BLAST
Coiled coili895 – 96066 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00550000074851.
HOVERGENiHBG019108.
KOiK17079.
OMAiKRHKWNE.
OrthoDBiEOG7TMZR4.
PhylomeDBiP58281.
TreeFamiTF314250.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11566. PTHR11566. 1 hit.
PfamiPF00350. Dynamin_N. 1 hit.
[Graphical view]
PRINTSiPR00195. DYNAMIN.
SMARTiSM00053. DYNc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P58281-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MWRAGRAAVA CEVCQSLVKH SSGIQRNVPL QKLHLVSRSI YRSHHPALKL    50
QRPQLRTPFQ QFSSLTHLSL HKLKLSPIKY GYQPRRNFWP ARLAARLLKL 100
RYIILGSAVG GGYTAKKTFD EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE 150
KIRKALPSSE DLASLAPDLD KITESLSLLK DFFTAGSPGE TAFRATDHGS 200
ESDKHYRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN KELRKLVLQK 250
DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG 300
KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL 350
TKEEDLAALR HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP 400
GVINTVTSGM APDTKETIFS ISKAYMQNPN AIILCIQDGS VDAERSIVTD 450
LVSQMDPHGR RTIFVLTKVD LAEKNVASPS RIQQIIEGKL FPMKALGYFA 500
VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT TRNLSLAVSD 550
CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE 600
ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN 650
TTVDIKLKQW TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL 700
KEAVKEESIK RHKWNDFAED SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE 750
ALQGRLKDTE NAIENMIGPD WKKRWMYWKN RTQEQCVHNE TKNELEKMLK 800
VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV YRRHFLKTAL 850
NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN 900
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD 950
AFIEALHQEK 960
Length:960
Mass (Da):111,339
Last modified:September 26, 2001 - v1
Checksum:i0F103FB1FD570F49
GO
Isoform 2 (identifier: P58281-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:997
Mass (Da):115,593
Checksum:iFADCB1430E585522
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei208 – 2081K → KGLLGELILLQQQIQEHEEE ARRAAGQYSTSYAQQKRK in isoform 2.
VSP_021037

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361L → P in BAC30002. 1 Publication
Sequence conflicti330 – 3312TL → NN in BAC32021. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28096.1. [P58281-1]
RefSeqiNP_598513.1. NM_133752.3. [P58281-1]
XP_006522720.1. XM_006522657.1. [P58281-2]
UniGeneiMm.274285.

Genome annotation databases

EnsembliENSMUST00000160597; ENSMUSP00000124223; ENSMUSG00000038084. [P58281-1]
ENSMUST00000161186; ENSMUSP00000123880; ENSMUSG00000038084. [P58281-2]
GeneIDi74143.
KEGGimmu:74143.
UCSCiuc007ywf.2. mouse. [P58281-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28096.1. [P58281-1 ]
RefSeqi NP_598513.1. NM_133752.3. [P58281-1 ]
XP_006522720.1. XM_006522657.1. [P58281-2 ]
UniGenei Mm.274285.

3D structure databases

ProteinModelPortali P58281.
SMRi P58281. Positions 262-601.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P58281. 7 interactions.
MINTi MINT-4105859.

PTM databases

PhosphoSitei P58281.

Proteomic databases

MaxQBi P58281.
PaxDbi P58281.
PRIDEi P58281.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000160597 ; ENSMUSP00000124223 ; ENSMUSG00000038084 . [P58281-1 ]
ENSMUST00000161186 ; ENSMUSP00000123880 ; ENSMUSG00000038084 . [P58281-2 ]
GeneIDi 74143.
KEGGi mmu:74143.
UCSCi uc007ywf.2. mouse. [P58281-1 ]

Organism-specific databases

CTDi 4976.
MGIi MGI:1921393. Opa1.

Phylogenomic databases

eggNOGi COG0699.
GeneTreei ENSGT00550000074851.
HOVERGENi HBG019108.
KOi K17079.
OMAi KRHKWNE.
OrthoDBi EOG7TMZR4.
PhylomeDBi P58281.
TreeFami TF314250.

Miscellaneous databases

ChiTaRSi OPA1. mouse.
NextBioi 339890.
PROi P58281.
SOURCEi Search...

Gene expression databases

ArrayExpressi P58281.
Bgeei P58281.
CleanExi MM_OPA1.
Genevestigatori P58281.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11566. PTHR11566. 1 hit.
Pfami PF00350. Dynamin_N. 1 hit.
[Graphical view ]
PRINTSi PR00195. DYNAMIN.
SMARTi SM00053. DYNc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiOPA1_MOUSE
AccessioniPrimary (citable) accession number: P58281
Secondary accession number(s): A6H6Q3
, Q3ULA5, Q8BKU7, Q8BLL3, Q8BM08, Q8R3J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: September 26, 2001
Last modified: July 9, 2014
This is version 111 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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