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O60313 (OPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Optic atrophy protein 1

Cleaved into the following chain:

  1. Dynamin-like 120 kDa protein, form S1
Gene names
Name:OPA1
Synonyms:KIAA0567
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.9 Ref.10

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.9 Ref.10

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.12 Ref.14

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion intermembrane space Ref.7 Ref.9.

Tissue specificity

Highly expressed in retina. Also expressed in brain, testis, heart and skeletal muscle. Isoform 1 expressed in retina, skeletal muscle, heart, lung, ovary, colon, thyroid gland, leukocytes and fetal brain. Isoform 2 expressed in colon, liver, kidney, thyroid gland and leukocytes. Low levels of all isoforms expressed in a variety of tissues. Ref.6 Ref.7 Ref.8

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.

Involvement in disease

Optic atrophy 1 (OPA1) [MIM:165500]: A condition that features progressive visual loss in association with optic atrophy. Atrophy of the optic disk indicates a deficiency in the number of nerve fibers which arise in the retina and converge to form the optic disk, optic nerve, optic chiasm and optic tracts. OPA1 is characterized by an insidious onset of visual impairment in early childhood with moderate to severe loss of visual acuity, temporal optic disk pallor, color vision deficits, and centrocecal scotoma of variable density.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.8 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28

Dominant optic atrophy plus syndrome (DOA+) [MIM:125250]: A neurologic disorder characterized most commonly by an insidious onset of visual loss and sensorineural hearing loss in childhood with variable presentation of other clinical manifestations including progressive external ophthalmoplegia, muscle cramps, hyperreflexia, and ataxia. There appears to be a wide range of intermediate phenotypes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.22 Ref.25

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Sequence caution

The sequence AF416919 differs from that shown. Reason:

Ontologies

Keywords
   Biological processApoptosis
Sensory transduction
Vision
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
   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.8. Source: GOC

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axon transport of mitochondrion

Traceable author statement Ref.8. Source: UniProtKB

cellular senescence

Inferred from direct assay PubMed 17545159. Source: UniProtKB

inner mitochondrial membrane organization

Inferred from direct assay PubMed 12509422. Source: UniProtKB

mitochondrial fission

Traceable author statement PubMed 12509422. Source: UniProtKB

mitochondrial fusion

Inferred from direct assay PubMed 17545159. Source: UniProtKB

mitochondrion organization

Non-traceable author statement Ref.8. Source: UniProtKB

negative regulation of release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 21149567. Source: UniProtKB

neural tube closure

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentdendrite

Inferred from sequence or structural similarity PubMed 11847212. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial crista

Inferred from direct assay PubMed 12504110. Source: UniProtKB

mitochondrial inner membrane

Non-traceable author statement PubMed 20436456. Source: BHF-UCL

mitochondrial intermembrane space

Inferred from sequence or structural similarity PubMed 11847212. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 12504110. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 17545159. Source: UniProtKB

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement Ref.8. Source: UniProtKB

magnesium ion binding

Non-traceable author statement Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.14Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BNIP3Q1298310EBI-1054131,EBI-749464
LRRK2Q5S0073EBI-1054131,EBI-5323863

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60313-1)

Also known as: 6;

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: O60313-2)

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: V → GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRKV
Note: Proteolytic processing near Gln-220 produces form S2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 8787Mitochondrion By similarity
Chain88 – 960873Dynamin-like 120 kDa protein, mitochondrial
PRO_0000007397
Chain195 – 960766Dynamin-like 120 kDa protein, form S1 By similarity
PRO_0000253479

Regions

Topological domain88 – 969Mitochondrial matrix By similarity
Transmembrane97 – 11317Helical; Potential
Topological domain114 – 960847Mitochondrial intermembrane By similarity
Domain285 – 561277Dynamin-type G
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 Ref.11

Natural variations

Alternative sequence2091V → GLLGELILLQQQIQEHEEEA RRAAGQYSTSYAQQKRKV in isoform 2.
VSP_021035
Natural variant81A → S in OPA1. Ref.23
VAR_060825
Natural variant38 – 436Missing in OPA1.
VAR_022923
Natural variant801Y → C in OPA1. Ref.23
Corresponds to variant rs151103940 [ dbSNP | Ensembl ].
VAR_060826
Natural variant951T → M in OPA1. Ref.26
VAR_060827
Natural variant1021Y → C in OPA1. Ref.26
VAR_060828
Natural variant1581S → N. Ref.1 Ref.5 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23
Corresponds to variant rs7624750 [ dbSNP | Ensembl ].
VAR_022924
Natural variant1671P → L. Ref.17
VAR_022925
Natural variant1921A → V. Ref.15 Ref.17 Ref.23
Corresponds to variant rs34307082 [ dbSNP | Ensembl ].
VAR_022926
Natural variant2701E → K in OPA1. Ref.15
VAR_060829
Natural variant2721L → P in OPA1. Ref.19
VAR_060830
Natural variant2731D → A in OPA1. Ref.15
VAR_060831
Natural variant2901R → Q in OPA1. Ref.6 Ref.8 Ref.15 Ref.16
VAR_011483
Natural variant2901R → W in OPA1. Ref.15
VAR_060832
Natural variant293 – 2942Missing in OPA1.
VAR_060833
Natural variant3001G → E in OPA1. Ref.7 Ref.16
VAR_011484
Natural variant3101Q → R in OPA1. Ref.26
VAR_060834
Natural variant324 – 3263Missing in OPA1.
VAR_060835
Natural variant3571A → T in OPA1. Ref.26
Corresponds to variant rs190223702 [ dbSNP | Ensembl ].
VAR_060836
Natural variant3821I → M in OPA1. Ref.26
Corresponds to variant rs143319805 [ dbSNP | Ensembl ].
VAR_060837
Natural variant3841L → F in OPA1. Ref.16
VAR_060838
Natural variant3961L → P in OPA1. Ref.26
VAR_060839
Natural variant3961L → R in OPA1. Ref.17
VAR_022927
Natural variant4001P → A in OPA1. Ref.28
VAR_067355
Natural variant429 – 4302Missing in OPA1.
VAR_060840
Natural variant4301N → D in OPA1. Ref.26
VAR_060841
Natural variant4321Missing in OPA1. Ref.8 Ref.17
VAR_011485
Natural variant4381D → V in OPA1. Ref.15
VAR_060842
Natural variant4451R → H in OPA1 and DOA+. Ref.18 Ref.20 Ref.22
VAR_015741
Natural variant4491T → R in OPA1. Ref.26
VAR_060843
Natural variant4631I → IFIF in OPA1.
VAR_060844
Natural variant4681K → E in OPA1. Ref.15
VAR_060845
Natural variant4701D → G in OPA1. Ref.19
VAR_060846
Natural variant4871E → K in OPA1. Ref.26
VAR_060847
Natural variant5031T → K in OPA1. Ref.16 Ref.17
VAR_022928
Natural variant5051K → N in OPA1. Ref.16
VAR_060848
Natural variant5451S → R in OPA1. Ref.24 Ref.26
VAR_026533
Natural variant5501D → N. Ref.15
VAR_060849
Natural variant5511C → Y in OPA1. Ref.26
VAR_060851
Natural variant5511Missing in OPA1. Ref.15
VAR_060850
Natural variant5711R → H in OPA1. Ref.17
VAR_022929
Natural variant5741L → P in OPA1. Ref.19
VAR_060852
Natural variant5821Y → C in DOA+. Ref.25
VAR_060853
Natural variant586 – 5894Missing in OPA1.
VAR_022930
Natural variant5901R → Q in OPA1. Ref.26
VAR_060854
Natural variant5901R → W in OPA1. Ref.21
VAR_060855
Natural variant5931L → P in OPA1. Ref.26
VAR_060856
Natural variant6461S → L in OPA1. Ref.26
VAR_060857
Natural variant700 – 7012Missing in OPA1.
VAR_060858
Natural variant7281N → K in OPA1. Ref.21
VAR_060859
Natural variant7681G → D in OPA1. Ref.26
VAR_060860
Natural variant7811R → W in OPA1. Ref.26
Corresponds to variant rs190235251 [ dbSNP | Ensembl ].
VAR_060861
Natural variant7851Q → R in OPA1. Ref.6 Ref.15
VAR_060862
Natural variant8231S → Y in OPA1. Ref.26
VAR_060863
Natural variant8411Y → C in OPA1. Ref.23
VAR_060864
Natural variant8821R → L in OPA1. Ref.26
VAR_060865
Natural variant8871L → P in OPA1. Ref.26
VAR_060866
Natural variant9071E → G. Ref.16
VAR_060867
Natural variant9321R → C in OPA1. Ref.26 Ref.27
VAR_060868
Natural variant9391L → P in OPA1. Ref.6
VAR_028370
Natural variant9491L → P in OPA1. Ref.26
VAR_060869

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (6) [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 1C397109787AEB4D

FASTA960111,631
        10         20         30         40         50         60 
MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHHPTLKL QRPQLRTSFQ 

        70         80         90        100        110        120 
QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD 

       130        140        150        160        170        180 
QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPSSE DLVKLAPDFD KIVESLSLLK 

       190        200        210        220        230        240 
DFFTSGSPEE TAFRATDRGS ESDKHFRKVS 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 ALQARLKDTE NAIENMVGPD WKKRWLYWKN 

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

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

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

« Hide

Isoform 2 [UniParc].

Checksum: 5D1F6B9BF800F35E
Show »

FASTA997115,884

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-158.
Tissue: Brain.
[2]"Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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), VARIANT ASN-158.
Tissue: Brain.
[6]"Mutation spectrum and splicing variants in the OPA1 gene."
Delettre C., Griffoin J.-M., Kaplan J., Dollfus H., Lorenz B., Faivre L., Lenaers G., Belenguer P., Hamel C.P.
Hum. Genet. 109:584-591(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANTS OPA1 GLN-290; ARG-785 AND PRO-939.
[7]"Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy."
Delettre C., Lenaers G., Griffoin J.-M., Gigarel N., Lorenzo C., Belenguer P., Pelloquin L., Grosgeorge J., Turc-Carel C., Perret E., Astarie-Dequeker C., Lasquellec L., Arnaud B., Ducommun B., Kaplan J., Hamel C.P.
Nat. Genet. 26:207-210(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT OPA1 GLU-300.
[8]"OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28."
Alexander C., Votruba M., Pesch U.E.A., Thiselton D.L., Mayer S., Moore A., Rodriguez M., Kellner U., Leo-Kottler B., Auburger G., Bhattacharya S.S., Wissinger B.
Nat. Genet. 26:211-215(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, VARIANTS OPA1 GLN-290 AND ILE-432 DEL.
[9]"Regulation of mitochondrial morphology through proteolytic cleavage of OPA1."
Ishihara N., Fujita Y., Oka T., Mihara K.
EMBO J. 25:2966-2977(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells."
Head B., Griparic L., Amiri M., Gandre-Babbe S., van der Bliek A.M.
J. Cell Biol. 187:959-966(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), PROTEOLYTIC PROCESSING.
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Vital function of PRELI and essential requirement of its LEA motif."
McKeller M.R., Herrera-Rodriguez S., Ma W., Ortiz-Quintero B., Rangel R., Cande C., Sims-Mourtada J.C., Melnikova V., Kashi C., Phan L.M., Chen Z., Huang P., Dunner K. Jr., Kroemer G., Singh K.K., Martinez-Valdez H.
Cell Death Dis. 1:E21-E21(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRELID1.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 AND IMMT.
[15]"OPA1 mutations in patients with autosomal dominant optic atrophy and evidence for semi-dominant inheritance."
Pesch U.E.A., Leo-Kottler B., Mayer S., Jurklies B., Kellner U., Apfelstedt-Sylla E., Zrenner E., Alexander C., Wissinger B.
Hum. Mol. Genet. 10:1359-1368(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 LYS-270; ALA-273; GLN-290; TRP-290; VAL-438; GLU-468; CYS-551 DEL AND ARG-785, VARIANTS ASN-158; VAL-192 AND ASN-550.
[16]"Spectrum, frequency and penetrance of OPA1 mutations in dominant optic atrophy."
Toomes C., Marchbank N.J., Mackey D.A., Craig J.E., Newbury-Ecob R.A., Bennett C.P., Vize C.J., Desai S.P., Black G.C.M., Patel N., Teimory M., Markham A.F., Inglehearn C.F., Churchill A.J.
Hum. Mol. Genet. 10:1369-1378(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505, VARIANTS ASN-158 AND GLY-907.
[17]"A comprehensive survey of mutations in the OPA1 gene in patients with autosomal dominant optic atrophy."
Thiselton D.L., Alexander C., Taanman J.-W., Brooks S., Rosenberg T., Eiberg H., Andreasson S., Van Regemorter N., Munier F.L., Moore A.T., Bhattacharya S.S., Votruba M.
Invest. Ophthalmol. Vis. Sci. 43:1715-1724(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 38-ARG--SER-43 DEL; 586-ARG--ASP-589 DEL; ARG-396; ILE-432 DEL; LYS-503 AND HIS-571, VARIANTS ASN-158; LEU-167 AND VAL-192.
[18]"A novel mutation in the OPA1 gene in a Japanese patient with optic atrophy."
Shimizu S., Mori N., Kishi M., Sugata H., Tsuda A., Kubota N.
Am. J. Ophthalmol. 135:256-257(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPA1 HIS-445.
[19]"Fourteen novel OPA1 mutations in autosomal dominant optic atrophy including two de novo mutations in sporadic optic atrophy."
Baris O., Delettre C., Amati-Bonneau P., Surget M.-O., Charlin J.-F., Catier A., Derieux L., Guyomard J.-L., Dollfus H., Jonveaux P., Ayuso C., Maumenee I., Lorenz B., Mohammed S., Tourmen Y., Bonneau D., Malthiery Y., Hamel C., Reynier P.
Hum. Mutat. 21:656-656(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 PRO-272; GLY-470; PRO-574 AND 700-LEU-LYS-701 DEL.
[20]"Dominant optic atrophy, sensorineural hearing loss, ptosis, and ophthalmoplegia: a syndrome caused by a missense mutation in OPA1."
Payne M., Yang Z., Katz B.J., Warner J.E.A., Weight C.J., Zhao Y., Pearson E.D., Treft R.L., Hillman T., Kennedy R.J., Meire F.M., Zhang K.
Am. J. Ophthalmol. 138:749-755(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DOA+ HIS-445.
[21]"Dominant optic atrophy: correlation between clinical and molecular genetic studies."
Puomila A., Huoponen K., Maentyjaervi M., Haemaelaeinen P., Paananen R., Sankila E.-M., Savontaus M.-L., Somer M., Nikoskelainen E.
Acta Ophthalmol. Scand. 83:337-346(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 324-ARG--PRO-326 DEL; TRP-590 AND LYS-728, VARIANT ASN-158.
[22]"OPA1 R445H mutation in optic atrophy associated with sensorineural deafness."
Amati-Bonneau P., Guichet A., Olichon A., Chevrollier A., Viala F., Miot S., Ayuso C., Odent S., Arrouet C., Verny C., Calmels M.-N., Simard G., Belenguer P., Wang J., Puel J.-L., Hamel C., Malthiery Y., Bonneau D., Lenaers G., Reynier P.
Ann. Neurol. 58:958-963(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DOA+ HIS-445.
[23]"OPA1 mutations and mitochondrial DNA haplotypes in autosomal dominant optic atrophy."
Han J., Thompson-Lowrey A.J., Reiss A., Mayorov V., Jia H., Biousse V., Newman N.J., Brown M.D.
Genet. Med. 8:217-225(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 SER-8; CYS-80 AND CYS-841, VARIANTS ASN-158 AND VAL-192.
[24]"Novel mutations in the OPA1 gene and associated clinical features in Japanese patients with optic atrophy."
Nakamura M., Lin J., Ueno S., Asaoka R., Hirai T., Hotta Y., Miyake Y., Terasaki H.
Ophthalmology 113:483-488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPA1 ARG-545.
[25]"Progressive external ophthalmoplegia and vision and hearing loss in a patient with mutations in POLG2 and OPA1."
Ferraris S., Clark S., Garelli E., Davidzon G., Moore S.A., Kardon R.H., Bienstock R.J., Longley M.J., Mancuso M., Gutierrez Rios P., Hirano M., Copeland W.C., DiMauro S.
Arch. Neurol. 65:125-131(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DOA+ CYS-582.
[26]"Molecular screening of 980 cases of suspected hereditary optic neuropathy with a report on 77 novel OPA1 mutations."
Ferre M., Bonneau D., Milea D., Chevrollier A., Verny C., Dollfus H., Ayuso C., Defoort S., Vignal C., Zanlonghi X., Charlin J.-F., Kaplan J., Odent S., Hamel C.P., Procaccio V., Reynier P., Amati-Bonneau P.
Hum. Mutat. 30:E692-E705(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPA1 MET-95; CYS-102; 293-VAL-VAL-294 DEL; ARG-310; THR-357; MET-382; PRO-396; 429-PRO-ASN-430 DEL; ASP-430; ARG-449; 463-ILE-PHE-464 INS; LYS-487; ARG-545; TYR-551; GLN-590; PRO-593; LEU-646; ASP-768; TRP-781; TYR-823; LEU-882; PRO-887; CYS-932 AND PRO-949.
[27]"Acute and late-onset optic atrophy due to a novel OPA1 mutation leading to a mitochondrial coupling defect."
Nochez Y., Arsene S., Gueguen N., Chevrollier A., Ferre M., Guillet V., Desquiret V., Toutain A., Bonneau D., Procaccio V., Amati-Bonneau P., Pisella P.-J., Reynier P.
Mol. Vis. 15:598-608(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPA1 CYS-932.
[28]"A novel OPA1 mutation in a Chinese family with autosomal dominant optic atrophy."
Zhang J., Yuan Y., Lin B., Feng H., Li Y., Dai X., Zhou H., Dong X., Liu X.L., Guan M.X.
Biochem. Biophys. Res. Commun. 419:670-675(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPA1 ALA-400.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011139 mRNA. Translation: BAA25493.1.
HQ204906 Genomic DNA. Translation: ADP90057.1.
HQ204907 Genomic DNA. Translation: ADP90065.1.
HQ204908 Genomic DNA. Translation: ADP90073.1.
HQ204910 Genomic DNA. Translation: ADP90089.1.
HQ204911 Genomic DNA. Translation: ADP90097.1.
HQ204912 Genomic DNA. Translation: ADP90105.1.
HQ204913 Genomic DNA. Translation: ADP90113.1.
HQ204914 Genomic DNA. Translation: ADP90121.1.
HQ204917 Genomic DNA. Translation: ADP90145.1.
HQ204918 Genomic DNA. Translation: ADP90153.1.
HQ204920 Genomic DNA. Translation: ADP90169.1.
HQ204921 Genomic DNA. Translation: ADP90177.1.
HQ204922 Genomic DNA. Translation: ADP90185.1.
HQ204923 Genomic DNA. Translation: ADP90193.1.
HQ204924 Genomic DNA. Translation: ADP90201.1.
HQ204925 Genomic DNA. Translation: ADP90209.1.
HQ204926 Genomic DNA. Translation: ADP90217.1.
HQ204927 Genomic DNA. Translation: ADP90225.1.
HQ204929 Genomic DNA. Translation: ADP90241.1.
HQ204930 Genomic DNA. Translation: ADP90249.1.
HQ204932 Genomic DNA. Translation: ADP90265.1.
HQ204933 Genomic DNA. Translation: ADP90273.1.
HQ204934 Genomic DNA. Translation: ADP90281.1.
HQ204935 Genomic DNA. Translation: ADP90289.1.
HQ204936 Genomic DNA. Translation: ADP90297.1.
HQ204938 Genomic DNA. Translation: ADP90313.1.
HQ204939 Genomic DNA. Translation: ADP90321.1.
HQ204940 Genomic DNA. Translation: ADP90329.1.
HQ204941 Genomic DNA. Translation: ADP90337.1.
HQ204942 Genomic DNA. Translation: ADP90345.1.
HQ204943 Genomic DNA. Translation: ADP90353.1.
HQ204944 Genomic DNA. Translation: ADP90361.1.
HQ204945 Genomic DNA. Translation: ADP90369.1.
AC048351 Genomic DNA. No translation available.
AC106710 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78064.1.
CH471052 Genomic DNA. Translation: EAW78071.1.
BC075805 mRNA. Translation: AAH75805.1.
AF416919 Genomic DNA. No translation available.
AF416920 Genomic DNA. No translation available.
CCDSCCDS33917.1. [O60313-2]
CCDS43186.1. [O60313-1]
PIRT00336.
RefSeqNP_056375.2. NM_015560.2. [O60313-1]
UniGeneHs.594504.

3D structure databases

ProteinModelPortalO60313.
SMRO60313. Positions 262-601.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111024. 22 interactions.
IntActO60313. 7 interactions.
MINTMINT-4991595.
STRING9606.ENSP00000354681.

Protein family/group databases

TCDB9.B.25.2.1. the mitochondrial inner/outer membrane fusion (mmf) family.

PTM databases

PhosphoSiteO60313.

Proteomic databases

MaxQBO60313.
PaxDbO60313.
PRIDEO60313.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361908; ENSP00000354681; ENSG00000198836. [O60313-2]
ENST00000392438; ENSP00000376233; ENSG00000198836. [O60313-1]
GeneID4976.
KEGGhsa:4976.
UCSCuc003ftm.3. human. [O60313-1]

Organism-specific databases

CTD4976.
GeneCardsGC03P193311.
GeneReviewsOPA1.
HGNCHGNC:8140. OPA1.
HPAHPA036926.
HPA036927.
MIM125250. phenotype.
165500. phenotype.
605290. gene.
neXtProtNX_O60313.
Orphanet3212. Autosomal dominant optic atrophy and congenital deafness.
1215. Autosomal dominant optic atrophy plus syndrome.
98673. Autosomal dominant optic atrophy, classic type.
PharmGKBPA31927.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000230714.
HOVERGENHBG019108.
KOK17079.
OrthoDBEOG7TMZR4.
PhylomeDBO60313.
TreeFamTF314250.

Gene expression databases

ArrayExpressO60313.
BgeeO60313.
CleanExHS_OPA1.
GenevestigatorO60313.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR001401. Dynamin_GTPase.
IPR022812. Dynamin_SF.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOPA1. human.
GeneWikiOptic_atrophy_1.
GenomeRNAi4976.
NextBio19154.
PMAP-CutDBO60313.
PROO60313.
SOURCESearch...

Entry information

Entry nameOPA1_HUMAN
AccessionPrimary (citable) accession number: O60313
Secondary accession number(s): D3DNW4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM