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Dynamin-like 120 kDa protein, mitochondrial (EC 3.6.5.5) (Optic atrophy protein 1) [Cleaved into: Dynamin-like 120 kDa protein, form S1]

 OPA1_HUMAN              Reviewed;         960 AA.
O60313; D3DNW4; E5KLJ5; E5KLJ6; E5KLJ7; E5KLK1; E5KLK2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
22-NOV-2017, entry version 171.
RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
EC=3.6.5.5 {ECO:0000269|PubMed:20185555};
AltName: Full=Optic atrophy protein 1;
Contains:
RecName: Full=Dynamin-like 120 kDa protein, form S1;
Flags: Precursor;
Name=OPA1; Synonyms=KIAA0567;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-158.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"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.";
DNA Res. 5:31-39(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 7).
PubMed=20843780; DOI=10.1093/nar/gkq750;
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.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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., 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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ASN-158.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), ALTERNATIVE
SPLICING, TISSUE SPECIFICITY, AND VARIANTS OPA1 GLN-290; ARG-785 AND
PRO-939.
PubMed=11810270; DOI=10.1007/s00439-001-0633-y;
Delettre C., Griffoin J.-M., Kaplan J., Dollfus H., Lorenz B.,
Faivre L., Lenaers G., Belenguer P., Hamel C.P.;
"Mutation spectrum and splicing variants in the OPA1 gene.";
Hum. Genet. 109:584-591(2001).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT OPA1 GLU-300.
PubMed=11017079; DOI=10.1038/79936;
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.;
"Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein,
is mutated in dominant optic atrophy.";
Nat. Genet. 26:207-210(2000).
[8]
TISSUE SPECIFICITY, AND VARIANTS OPA1 GLN-290 AND ILE-432 DEL.
PubMed=11017080; DOI=10.1038/79944;
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.;
"OPA1, encoding a dynamin-related GTPase, is mutated in autosomal
dominant optic atrophy linked to chromosome 3q28.";
Nat. Genet. 26:211-215(2000).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
PubMed=16778770; DOI=10.1038/sj.emboj.7601184;
Ishihara N., Fujita Y., Oka T., Mihara K.;
"Regulation of mitochondrial morphology through proteolytic cleavage
of OPA1.";
EMBO J. 25:2966-2977(2006).
[10]
FUNCTION, ALTERNATIVE SPLICING, AND PROTEOLYTIC CLEAVAGE.
PubMed=17709429; DOI=10.1083/jcb.200704110;
Song Z., Chen H., Fiket M., Alexander C., Chan D.C.;
"OPA1 processing controls mitochondrial fusion and is regulated by
mRNA splicing, membrane potential, and Yme1L.";
J. Cell Biol. 178:749-755(2007).
[11]
FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), AND PROTEOLYTIC
PROCESSING.
PubMed=20038677; DOI=10.1083/jcb.200906083;
Head B., Griparic L., Amiri M., Gandre-Babbe S., van der Bliek A.M.;
"Inducible proteolytic inactivation of OPA1 mediated by the OMA1
protease in mammalian cells.";
J. Cell Biol. 187:959-966(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
INTERACTION WITH PRELID1.
PubMed=21364629; DOI=10.1038/cddis.2009.19;
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.;
"Vital function of PRELI and essential requirement of its LEA motif.";
Cell Death Dis. 1:E21-E21(2010).
[14]
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF VARIANTS
OPA1 GLU-300; VAL-439; HIS-445; ARG-545; LYS-728; ARG-785 AND PRO-939,
AND CHARACTERIZATION OF VARIANTS VARIANT DOA+ THR-357; VAL-439;
HIS-445; ARG-545 AND ASP-910.
PubMed=20185555; DOI=10.1093/hmg/ddq088;
Ban T., Heymann J.A., Song Z., Hinshaw J.E., Chan D.C.;
"OPA1 disease alleles causing dominant optic atrophy have defects in
cardiolipin-stimulated GTP hydrolysis and membrane tubulation.";
Hum. Mol. Genet. 19:2113-2122(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
INVOLVEMENT IN DOA+, AND VARIANT DOA+ TYR-551.
PubMed=21112924; DOI=10.1093/brain/awq306;
Marelli C., Amati-Bonneau P., Reynier P., Layet V., Layet A.,
Stevanin G., Brissaud E., Bonneau D., Durr A., Brice A.;
"Heterozygous OPA1 mutations in Behr syndrome.";
Brain 134:E169-E169(2011).
[17]
FUNCTION (ISOFORMS 4 AND 5), AND SUBCELLULAR LOCATION.
PubMed=20974897; DOI=10.1101/gr.108696.110;
Elachouri G., Vidoni S., Zanna C., Pattyn A., Boukhaddaoui H.,
Gaget K., Yu-Wai-Man P., Gasparre G., Sarzi E., Delettre C.,
Olichon A., Loiseau D., Reynier P., Chinnery P.F., Rotig A.,
Carelli V., Hamel C.P., Rugolo M., Lenaers G.;
"OPA1 links human mitochondrial genome maintenance to mtDNA
replication and distribution.";
Genome Res. 21:12-20(2011).
[18]
INTERACTION WITH CHCHD3 AND IMMT.
PubMed=21081504; DOI=10.1074/jbc.M110.171975;
Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
Perkins G.A., Ellisman M.H., Taylor S.S.;
"ChChd3, an inner mitochondrial membrane protein, is essential for
maintaining crista integrity and mitochondrial function.";
J. Biol. Chem. 286:2918-2932(2011).
[19]
INVOLVEMENT IN BEHRS, AND VARIANT BEHRS MET-382.
PubMed=21636302; DOI=10.1016/j.ymgme.2011.04.018;
Schaaf C.P., Blazo M., Lewis R.A., Tonini R.E., Takei H., Wang J.,
Wong L.J., Scaglia F.;
"Early-onset severe neuromuscular phenotype associated with compound
heterozygosity for OPA1 mutations.";
Mol. Genet. Metab. 103:383-387(2011).
[20]
INVOLVEMENT IN BEHRS, AND VARIANTS BEHRS MET-382; MET-402 AND LYS-487.
PubMed=25012220; DOI=10.1093/brain/awu184;
Bonneau D., Colin E., Oca F., Ferre M., Chevrollier A., Gueguen N.,
Desquiret-Dumas V., N'Guyen S., Barth M., Zanlonghi X., Rio M.,
Desguerre I., Barnerias C., Momtchilova M., Rodriguez D., Slama A.,
Lenaers G., Procaccio V., Amati-Bonneau P., Reynier P.;
"Early-onset Behr syndrome due to compound heterozygous mutations in
OPA1.";
Brain 137:E301-E301(2014).
[21]
FUNCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
PubMed=24616225; DOI=10.1083/jcb.201308006;
Anand R., Wai T., Baker M.J., Kladt N., Schauss A.C., Rugarli E.,
Langer T.;
"The i-AAA protease YME1L and OMA1 cleave OPA1 to balance
mitochondrial fusion and fission.";
J. Cell Biol. 204:919-929(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
INVOLVEMENT IN BEHRS, AND VARIANT BEHRS MET-382.
PubMed=25146916; DOI=10.1093/brain/awu234;
Carelli V., Sabatelli M., Carrozzo R., Rizza T., Schimpf S.,
Wissinger B., Zanna C., Rugolo M., La Morgia C., Caporali L.,
Carbonelli M., Barboni P., Tonon C., Lodi R., Bertini E.;
"'Behr syndrome' with OPA1 compound heterozygote mutations.";
Brain 138:E321-E321(2015).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[25]
PROTEOLYTIC CLEAVAGE BY YME1L.
PubMed=27495975; DOI=10.7554/eLife.16078;
Hartmann B., Wai T., Hu H., MacVicar T., Musante L.,
Fischer-Zirnsak B., Stenzel W., Graef R., van den Heuvel L.,
Ropers H.H., Wienker T.F., Huebner C., Langer T., Kaindl A.M.;
"Homozygous YME1L1 mutation causes mitochondriopathy with optic
atrophy and mitochondrial network fragmentation.";
Elife 5:0-0(2016).
[26]
INVOLVEMENT IN MTDPS14, AND VARIANT MTDPS14 ARG-534.
PubMed=26561570; DOI=10.1136/jmedgenet-2015-103361;
Spiegel R., Saada A., Flannery P.J., Burte F., Soiferman D.,
Khayat M., Eisner V., Vladovski E., Taylor R.W., Bindoff L.A.,
Shaag A., Mandel H., Schuler-Furman O., Shalev S.A., Elpeleg O.,
Yu-Wai-Man P.;
"Fatal infantile mitochondrial encephalomyopathy, hypertrophic
cardiomyopathy and optic atrophy associated with a homozygous OPA1
mutation.";
J. Med. Genet. 53:127-131(2016).
[27]
VARIANTS OPA1 LYS-270; ALA-273; GLN-290; TRP-290; VAL-438; GLU-468;
CYS-551 DEL AND ARG-785, AND VARIANTS ASN-158; VAL-192 AND ASN-550.
PubMed=11440988; DOI=10.1093/hmg/10.13.1359;
Pesch U.E.A., Leo-Kottler B., Mayer S., Jurklies B., Kellner U.,
Apfelstedt-Sylla E., Zrenner E., Alexander C., Wissinger B.;
"OPA1 mutations in patients with autosomal dominant optic atrophy and
evidence for semi-dominant inheritance.";
Hum. Mol. Genet. 10:1359-1368(2001).
[28]
VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505, AND
VARIANTS ASN-158 AND GLY-907.
PubMed=11440989; DOI=10.1093/hmg/10.13.1369;
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.;
"Spectrum, frequency and penetrance of OPA1 mutations in dominant
optic atrophy.";
Hum. Mol. Genet. 10:1369-1378(2001).
[29]
VARIANTS OPA1 38-ARG--SER-43 DEL; 586-ARG--ASP-589 DEL; ARG-396;
ILE-432 DEL; LYS-503 AND HIS-571, AND VARIANTS ASN-158; LEU-167 AND
VAL-192.
PubMed=12036970;
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.;
"A comprehensive survey of mutations in the OPA1 gene in patients with
autosomal dominant optic atrophy.";
Invest. Ophthalmol. Vis. Sci. 43:1715-1724(2002).
[30]
VARIANT OPA1 HIS-445.
PubMed=12566046; DOI=10.1016/S0002-9394(02)01929-3;
Shimizu S., Mori N., Kishi M., Sugata H., Tsuda A., Kubota N.;
"A novel mutation in the OPA1 gene in a Japanese patient with optic
atrophy.";
Am. J. Ophthalmol. 135:256-257(2003).
[31]
VARIANTS OPA1 PRO-272; GLY-470; PRO-574 AND 700-LEU-LYS-701 DEL.
PubMed=14961560; DOI=10.1002/humu.9152;
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.;
"Fourteen novel OPA1 mutations in autosomal dominant optic atrophy
including two de novo mutations in sporadic optic atrophy.";
Hum. Mutat. 21:656-656(2003).
[32]
VARIANT DOA+ HIS-445.
PubMed=15531309; DOI=10.1016/j.ajo.2004.06.011;
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.;
"Dominant optic atrophy, sensorineural hearing loss, ptosis, and
ophthalmoplegia: a syndrome caused by a missense mutation in OPA1.";
Am. J. Ophthalmol. 138:749-755(2004).
[33]
VARIANTS OPA1 324-ARG--PRO-326 DEL; TRP-590 AND LYS-728, AND VARIANT
ASN-158.
PubMed=15948788; DOI=10.1111/j.1600-0420.2005.00448.x;
Puomila A., Huoponen K., Maentyjaervi M., Haemaelaeinen P.,
Paananen R., Sankila E.-M., Savontaus M.-L., Somer M.,
Nikoskelainen E.;
"Dominant optic atrophy: correlation between clinical and molecular
genetic studies.";
Acta Ophthalmol. Scand. 83:337-346(2005).
[34]
VARIANT DOA+ HIS-445.
PubMed=16240368; DOI=10.1002/ana.20681;
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.;
"OPA1 R445H mutation in optic atrophy associated with sensorineural
deafness.";
Ann. Neurol. 58:958-963(2005).
[35]
VARIANTS OPA1 SER-8; CYS-80 AND CYS-841, AND VARIANTS ASN-158 AND
VAL-192.
PubMed=16617242; DOI=10.1097/01.gim.0000214299.61930.c0;
Han J., Thompson-Lowrey A.J., Reiss A., Mayorov V., Jia H.,
Biousse V., Newman N.J., Brown M.D.;
"OPA1 mutations and mitochondrial DNA haplotypes in autosomal dominant
optic atrophy.";
Genet. Med. 8:217-225(2006).
[36]
VARIANT OPA1 ARG-545.
PubMed=16513463; DOI=10.1016/j.ophtha.2005.10.054;
Nakamura M., Lin J., Ueno S., Asaoka R., Hirai T., Hotta Y.,
Miyake Y., Terasaki H.;
"Novel mutations in the OPA1 gene and associated clinical features in
Japanese patients with optic atrophy.";
Ophthalmology 113:483-488(2006).
[37]
VARIANT OPA1 HIS-229 (ISOFORM 2).
PubMed=18360822; DOI=10.1002/ana.21376;
Cornille K., Milea D., Amati-Bonneau P., Procaccio V., Zazoun L.,
Guillet V., El Achouri G., Delettre C., Gueguen N., Loiseau D.,
Muller A., Ferre M., Chevrollier A., Wallace D.C., Bonneau D.,
Hamel C., Reynier P., Lenaers G.;
"Reversible optic neuropathy with OPA1 exon 5b mutation.";
Ann. Neurol. 63:667-671(2008).
[38]
VARIANT DOA+ CYS-582.
PubMed=18195150; DOI=10.1001/archneurol.2007.9;
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.;
"Progressive external ophthalmoplegia and vision and hearing loss in a
patient with mutations in POLG2 and OPA1.";
Arch. Neurol. 65:125-131(2008).
[39]
VARIANT DOA+ ARG-545.
PubMed=18065439; DOI=10.1093/brain/awm272;
Hudson G., Amati-Bonneau P., Blakely E.L., Stewart J.D., He L.,
Schaefer A.M., Griffiths P.G., Ahlqvist K., Suomalainen A.,
Reynier P., McFarland R., Turnbull D.M., Chinnery P.F., Taylor R.W.;
"Mutation of OPA1 causes dominant optic atrophy with external
ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA
deletions: a novel disorder of mtDNA maintenance.";
Brain 131:329-337(2008).
[40]
VARIANTS DOA+ THR-357; VAL-439; HIS-445; ARG-545 AND ASP-910, AND
FUNCTION.
PubMed=18158317; DOI=10.1093/brain/awm298;
Amati-Bonneau P., Valentino M.L., Reynier P., Gallardo M.E.,
Bornstein B., Boissiere A., Campos Y., Rivera H., de la Aleja J.G.,
Carroccia R., Iommarini L., Labauge P., Figarella-Branger D.,
Marcorelles P., Furby A., Beauvais K., Letournel F., Liguori R.,
La Morgia C., Montagna P., Liguori M., Zanna C., Rugolo M.,
Cossarizza A., Wissinger B., Verny C., Schwarzenbacher R.,
Martin M.A., Arenas J., Ayuso C., Garesse R., Lenaers G., Bonneau D.,
Carelli V.;
"OPA1 mutations induce mitochondrial DNA instability and optic atrophy
'plus' phenotypes.";
Brain 131:338-351(2008).
[41]
VARIANT OPA1 VAL-439.
PubMed=18204809; DOI=10.1007/s00415-008-0571-x;
Liguori M., La Russa A., Manna I., Andreoli V., Caracciolo M.,
Spadafora P., Cittadella R., Quattrone A.;
"A phenotypic variation of dominant optic atrophy and deafness (ADOAD)
due to a novel OPA1 mutation.";
J. Neurol. 255:127-129(2008).
[42]
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.
PubMed=19319978; DOI=10.1002/humu.21025;
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.;
"Molecular screening of 980 cases of suspected hereditary optic
neuropathy with a report on 77 novel OPA1 mutations.";
Hum. Mutat. 30:E692-E705(2009).
[43]
VARIANT OPA1 CYS-932.
PubMed=19325939;
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.;
"Acute and late-onset optic atrophy due to a novel OPA1 mutation
leading to a mitochondrial coupling defect.";
Mol. Vis. 15:598-608(2009).
[44]
VARIANTS OPA1 LEU-593 DEL AND PRO-949, AND VARIANT GLY-502.
PubMed=19969356; DOI=10.1016/j.ophtha.2009.07.019;
Yen M.Y., Wang A.G., Lin Y.C., Fann M.J., Hsiao K.J.;
"Novel mutations of the OPA1 gene in Chinese dominant optic atrophy.";
Ophthalmology 117:392-396(2010).
[45]
VARIANT OPA1 ALA-400.
PubMed=22382025; DOI=10.1016/j.bbrc.2012.02.073;
Zhang J., Yuan Y., Lin B., Feng H., Li Y., Dai X., Zhou H., Dong X.,
Liu X.L., Guan M.X.;
"A novel OPA1 mutation in a Chinese family with autosomal dominant
optic atrophy.";
Biochem. Biophys. Res. Commun. 419:670-675(2012).
[46]
VARIANTS OPA1 GLU-459 AND VAL-910 DEL.
PubMed=22857269; DOI=10.1186/1471-2350-13-65;
Almind G.J., Ek J., Rosenberg T., Eiberg H., Larsen M., Lucamp L.,
Brondum-Nielsen K., Gronskov K.;
"Dominant optic atrophy in Denmark - report of 15 novel mutations in
OPA1, using a strategy with a detection rate of 90%.";
BMC Med. Genet. 13:65-65(2012).
[47]
VARIANT DOA+ PRO-449.
PubMed=23387428; DOI=10.1111/aos.12038;
Liskova P., Ulmanova O., Tesina P., Melsova H., Diblik P.,
Hansikova H., Tesarova M., Votruba M.;
"Novel OPA1 missense mutation in a family with optic atrophy and
severe widespread neurological disorder.";
Acta Ophthalmol. 91:E225-E231(2013).
[48]
VARIANTS OPA1 SER-330 AND ILE-377.
PubMed=23401657;
Chen Y., Jia X., Wang P., Xiao X., Li S., Guo X., Zhang Q.;
"Mutation survey of the optic atrophy 1 gene in 193 Chinese families
with suspected hereditary optic neuropathy.";
Mol. Vis. 19:292-302(2013).
-!- FUNCTION: Dynamin-related GTPase that is essential for normal
mitochondrial morphology by regulating the equilibrium between
mitochondrial fusion and mitochondrial fission (PubMed:16778770,
PubMed:17709429, PubMed:20185555, PubMed:24616225). Coexpression
of isoform 1 with shorter alternative products is required for
optimal activity in promoting mitochondrial fusion
(PubMed:17709429). Binds lipid membranes enriched in negatively
charged phospholipids, such as cardiolipin, and promotes membrane
tubulation (PubMed:20185555). The intrinsic GTPase activity is
low, and is strongly increased by interaction with lipid membranes
(PubMed:20185555). Plays a role in remodeling cristae and the
release of cytochrome c during apoptosis (By similarity).
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 (By similarity). Plays a role in mitochondrial
genome maintenance (PubMed:20974897, PubMed:18158317).
{ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:16778770,
ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:20974897,
ECO:0000269|PubMed:24616225}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:20038677}.
-!- FUNCTION: Isoforms that contain the alternative exon 4b (present
in isoform 4 and isoform 5) are required for mitochondrial genome
maintenance, possibly by anchoring the mitochondrial nucleoids to
the inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
{ECO:0000269|PubMed:20185555}.
-!- SUBUNIT: Oligomeric complex consisting of membrane-bound and
soluble forms of OPA1. Interacts with CHCHD3 and IMMT; these
interactions occur preferentially with soluble OPA1 forms
(PubMed:21081504). Binds PARL (By similarity). Interacts with
PRELID1 (PubMed:21364629). {ECO:0000250|UniProtKB:P58281,
ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:21081504,
ECO:0000269|PubMed:21364629}.
-!- INTERACTION:
Q12983:BNIP3; NbExp=10; IntAct=EBI-1054131, EBI-749464;
Q5S007:LRRK2; NbExp=3; IntAct=EBI-1054131, EBI-5323863;
Q9NTG7:SIRT3; NbExp=3; IntAct=EBI-1054131, EBI-724621;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:16778770,
ECO:0000269|PubMed:20974897}; Single-pass membrane protein
{ECO:0000255}. Mitochondrion intermembrane space
{ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane
{ECO:0000269|PubMed:24616225}. Note=Detected at contact sites
between endoplamic reticulum and mitochondrion membranes.
{ECO:0000269|PubMed:24616225}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.
{ECO:0000305|PubMed:11810270, ECO:0000305|PubMed:17709429};
Name=1; Synonyms=6;
IsoId=O60313-1; Sequence=Displayed;
Name=2; Synonyms=7 {ECO:0000303|PubMed:16778770};
IsoId=O60313-2; Sequence=VSP_021035;
Note=Proteolytic processing near Gln-220 produces form S2
(Ref.9). Variant in position: 229:R->H (in OPA1) (Ref.28).
{ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:18360822};
Name=3;
IsoId=O60313-9; Sequence=VSP_059072, VSP_059074;
Name=4;
IsoId=O60313-10; Sequence=VSP_059073, VSP_059074;
Note=Contains the alternative exon 4b that is important for
mitochondrial genome maintenance. {ECO:0000305|PubMed:20974897};
Name=5;
IsoId=O60313-11; Sequence=VSP_059073;
Note=Contains the alternative exon 4b that is important for
mitochondrial genome maintenance. {ECO:0000305|PubMed:20974897};
Name=7;
IsoId=O60313-13; Sequence=VSP_059072;
-!- 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. {ECO:0000269|PubMed:11017079,
ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11810270}.
-!- PTM: PARL-dependent proteolytic processing releases an
antiapoptotic soluble form not required for mitochondrial fusion.
Cleaved by OMA1 at position S1 following stress conditions.
{ECO:0000269|PubMed:20038677}.
-!- PTM: Cleavage at position S2 is mediated by YME1L
(PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage may
occur in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ)
(PubMed:16778770). This motif is present in isoform 2, isoform 3,
isoform 4 and isoform 7, but is absent in the displayed isoform 1
and in isoform 5. {ECO:0000250|UniProtKB:Q2TA68,
ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429,
ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:27495975,
ECO:0000305}.
-!- 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. {ECO:0000269|PubMed:11017079,
ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11440988,
ECO:0000269|PubMed:11440989, ECO:0000269|PubMed:11810270,
ECO:0000269|PubMed:12036970, ECO:0000269|PubMed:12566046,
ECO:0000269|PubMed:14961560, ECO:0000269|PubMed:15948788,
ECO:0000269|PubMed:16513463, ECO:0000269|PubMed:16617242,
ECO:0000269|PubMed:18204809, ECO:0000269|PubMed:18360822,
ECO:0000269|PubMed:19319978, ECO:0000269|PubMed:19325939,
ECO:0000269|PubMed:19969356, ECO:0000269|PubMed:20185555,
ECO:0000269|PubMed:22382025, ECO:0000269|PubMed:22857269,
ECO:0000269|PubMed:23401657}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:15531309,
ECO:0000269|PubMed:16240368, ECO:0000269|PubMed:18065439,
ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:18195150,
ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:21112924,
ECO:0000269|PubMed:23387428}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Behr syndrome (BEHRS) [MIM:210000]: An autosomal
recessive syndrome characterized by optic atrophy beginning in
early childhood associated with ataxia, pyramidal signs,
spasticity, mental retardation, and posterior column sensory loss.
The ataxia, spasticity, and muscle contractures, mainly of the hip
adductors, hamstrings, and soleus, are progressive and become more
prominent in the second decade. {ECO:0000269|PubMed:21636302,
ECO:0000269|PubMed:25012220, ECO:0000269|PubMed:25146916}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Mitochondrial DNA depletion syndrome 14,
cardioencephalomyopathic type (MTDPS14) [MIM:616896]: An autosomal
recessive mitochondrial disorder characterized by lethal infantile
encephalopathy, hypertrophic cardiomyopathy and optic atrophy.
Skeletal muscle biopsies show significant mtDNA depletion and
abnormal mitochondria. {ECO:0000269|PubMed:26561570}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AF416919; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB011139; BAA25493.1; -; mRNA.
EMBL; HQ204906; ADP90054.1; -; Genomic_DNA.
EMBL; HQ204906; ADP90055.1; -; Genomic_DNA.
EMBL; HQ204906; ADP90056.1; -; Genomic_DNA.
EMBL; HQ204906; ADP90057.1; -; Genomic_DNA.
EMBL; HQ204906; ADP90060.1; -; Genomic_DNA.
EMBL; HQ204906; ADP90061.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90062.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90063.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90064.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90065.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90068.1; -; Genomic_DNA.
EMBL; HQ204907; ADP90069.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90070.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90071.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90072.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90073.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90076.1; -; Genomic_DNA.
EMBL; HQ204908; ADP90077.1; -; Genomic_DNA.
EMBL; HQ204909; ADP90084.1; -; Genomic_DNA.
EMBL; HQ204909; ADP90085.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90086.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90087.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90088.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90089.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90092.1; -; Genomic_DNA.
EMBL; HQ204910; ADP90093.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90094.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90095.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90096.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90097.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90100.1; -; Genomic_DNA.
EMBL; HQ204911; ADP90101.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90102.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90103.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90104.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90105.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90108.1; -; Genomic_DNA.
EMBL; HQ204912; ADP90109.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90110.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90111.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90112.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90113.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90116.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90118.1; -; Genomic_DNA.
EMBL; HQ204913; ADP90117.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90119.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90120.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90121.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90124.1; -; Genomic_DNA.
EMBL; HQ204914; ADP90125.1; -; Genomic_DNA.
EMBL; HQ204915; ADP90132.1; -; Genomic_DNA.
EMBL; HQ204915; ADP90133.1; -; Genomic_DNA.
EMBL; HQ204916; ADP90140.1; -; Genomic_DNA.
EMBL; HQ204916; ADP90141.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90142.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90143.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90144.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90145.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90148.1; -; Genomic_DNA.
EMBL; HQ204917; ADP90149.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90150.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90151.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90152.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90153.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90156.1; -; Genomic_DNA.
EMBL; HQ204918; ADP90157.1; -; Genomic_DNA.
EMBL; HQ204919; ADP90164.1; -; Genomic_DNA.
EMBL; HQ204919; ADP90165.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90166.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90167.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90168.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90169.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90172.1; -; Genomic_DNA.
EMBL; HQ204920; ADP90173.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90174.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90175.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90176.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90177.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90180.1; -; Genomic_DNA.
EMBL; HQ204921; ADP90181.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90182.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90183.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90184.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90185.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90188.1; -; Genomic_DNA.
EMBL; HQ204922; ADP90189.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90190.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90191.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90192.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90193.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90196.1; -; Genomic_DNA.
EMBL; HQ204923; ADP90197.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90198.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90199.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90200.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90201.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90204.1; -; Genomic_DNA.
EMBL; HQ204924; ADP90205.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90206.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90207.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90208.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90209.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90212.1; -; Genomic_DNA.
EMBL; HQ204925; ADP90213.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90214.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90215.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90216.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90217.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90220.1; -; Genomic_DNA.
EMBL; HQ204926; ADP90221.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90222.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90223.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90224.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90225.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90228.1; -; Genomic_DNA.
EMBL; HQ204927; ADP90229.1; -; Genomic_DNA.
EMBL; HQ204928; ADP90236.1; -; Genomic_DNA.
EMBL; HQ204928; ADP90237.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90238.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90239.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90240.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90241.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90244.1; -; Genomic_DNA.
EMBL; HQ204929; ADP90245.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90246.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90247.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90248.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90249.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90252.1; -; Genomic_DNA.
EMBL; HQ204930; ADP90253.1; -; Genomic_DNA.
EMBL; HQ204931; ADP90260.1; -; Genomic_DNA.
EMBL; HQ204931; ADP90261.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90262.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90263.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90264.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90265.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90268.1; -; Genomic_DNA.
EMBL; HQ204932; ADP90269.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90270.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90271.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90272.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90273.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90276.1; -; Genomic_DNA.
EMBL; HQ204933; ADP90277.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90278.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90279.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90280.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90281.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90284.1; -; Genomic_DNA.
EMBL; HQ204934; ADP90285.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90286.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90287.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90288.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90289.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90292.1; -; Genomic_DNA.
EMBL; HQ204935; ADP90293.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90294.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90295.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90296.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90297.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90300.1; -; Genomic_DNA.
EMBL; HQ204936; ADP90301.1; -; Genomic_DNA.
EMBL; HQ204937; ADP90308.1; -; Genomic_DNA.
EMBL; HQ204937; ADP90309.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90310.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90311.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90312.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90313.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90316.1; -; Genomic_DNA.
EMBL; HQ204938; ADP90317.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90318.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90319.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90320.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90321.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90324.1; -; Genomic_DNA.
EMBL; HQ204939; ADP90325.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90326.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90327.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90328.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90329.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90332.1; -; Genomic_DNA.
EMBL; HQ204940; ADP90333.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90334.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90335.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90336.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90337.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90340.1; -; Genomic_DNA.
EMBL; HQ204941; ADP90341.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90342.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90343.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90344.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90345.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90348.1; -; Genomic_DNA.
EMBL; HQ204942; ADP90349.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90350.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90351.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90352.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90353.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90356.1; -; Genomic_DNA.
EMBL; HQ204943; ADP90357.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90358.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90359.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90360.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90361.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90364.1; -; Genomic_DNA.
EMBL; HQ204944; ADP90365.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90366.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90367.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90368.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90369.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90372.1; -; Genomic_DNA.
EMBL; HQ204945; ADP90373.1; -; Genomic_DNA.
EMBL; AC048351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC106710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78064.1; -; Genomic_DNA.
EMBL; CH471052; EAW78065.1; -; Genomic_DNA.
EMBL; CH471052; EAW78066.1; -; Genomic_DNA.
EMBL; CH471052; EAW78067.1; -; Genomic_DNA.
EMBL; CH471052; EAW78069.1; -; Genomic_DNA.
EMBL; CH471052; EAW78070.1; -; Genomic_DNA.
EMBL; CH471052; EAW78071.1; -; Genomic_DNA.
EMBL; BC075805; AAH75805.1; -; mRNA.
EMBL; AF416919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF416920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS43186.1; -. [O60313-1]
PIR; T00336; T00336.
RefSeq; NP_056375.2; NM_015560.2. [O60313-1]
RefSeq; NP_570844.1; NM_130831.2. [O60313-13]
RefSeq; NP_570846.1; NM_130833.2. [O60313-9]
RefSeq; NP_570847.2; NM_130834.2. [O60313-11]
RefSeq; NP_570850.2; NM_130837.2. [O60313-10]
UniGene; Hs.594504; -.
ProteinModelPortal; O60313; -.
SMR; O60313; -.
BioGrid; 111024; 44.
CORUM; O60313; -.
IntAct; O60313; 13.
MINT; MINT-4991595; -.
STRING; 9606.ENSP00000354681; -.
TCDB; 9.B.25.2.1; the mitochondrial inner/outer membrane fusion (mmf) family.
iPTMnet; O60313; -.
PhosphoSitePlus; O60313; -.
SwissPalm; O60313; -.
BioMuta; OPA1; -.
EPD; O60313; -.
MaxQB; O60313; -.
PaxDb; O60313; -.
PeptideAtlas; O60313; -.
PRIDE; O60313; -.
Ensembl; ENST00000361150; ENSP00000354781; ENSG00000198836. [O60313-9]
Ensembl; ENST00000361510; ENSP00000355324; ENSG00000198836. [O60313-10]
Ensembl; ENST00000361828; ENSP00000354429; ENSG00000198836. [O60313-11]
Ensembl; ENST00000361908; ENSP00000354681; ENSG00000198836. [O60313-2]
Ensembl; ENST00000392438; ENSP00000376233; ENSG00000198836. [O60313-1]
GeneID; 4976; -.
KEGG; hsa:4976; -.
UCSC; uc003ftg.4; human.
UCSC; uc003fti.3; human. [O60313-1]
UCSC; uc003ftj.4; human.
UCSC; uc003ftk.4; human.
CTD; 4976; -.
DisGeNET; 4976; -.
EuPathDB; HostDB:ENSG00000198836.8; -.
GeneCards; OPA1; -.
GeneReviews; OPA1; -.
HGNC; HGNC:8140; OPA1.
HPA; HPA036926; -.
HPA; HPA036927; -.
MalaCards; OPA1; -.
MIM; 125250; phenotype.
MIM; 165500; phenotype.
MIM; 210000; phenotype.
MIM; 605290; gene.
MIM; 616896; phenotype.
neXtProt; NX_O60313; -.
OpenTargets; ENSG00000198836; -.
Orphanet; 1215; Autosomal dominant optic atrophy plus syndrome.
Orphanet; 98673; Autosomal dominant optic atrophy, classic type.
PharmGKB; PA31927; -.
eggNOG; KOG0447; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00550000074851; -.
HOGENOM; HOG000230714; -.
HOVERGEN; HBG019108; -.
InParanoid; O60313; -.
KO; K17079; -.
OMA; AIRRHSW; -.
OrthoDB; EOG091G01NV; -.
PhylomeDB; O60313; -.
TreeFam; TF314250; -.
Reactome; R-HSA-169911; Regulation of Apoptosis.
ChiTaRS; OPA1; human.
GeneWiki; Optic_atrophy_1; -.
GenomeRNAi; 4976; -.
PMAP-CutDB; O60313; -.
PRO; PR:O60313; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000198836; -.
CleanEx; HS_OPA1; -.
ExpressionAtlas; O60313; baseline and differential.
Genevisible; O60313; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030061; C:mitochondrial crista; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0019896; P:axonal transport of mitochondrion; TAS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
GO; GO:0090102; P:cochlea development; IEA:Ensembl.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
GO; GO:0007007; P:inner mitochondrial membrane organization; IDA:UniProtKB.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0097749; P:membrane tubulation; IDA:UniProtKB.
GO; GO:0036444; P:mitochondrial calcium uptake; IEA:Ensembl.
GO; GO:0000266; P:mitochondrial fission; TAS:UniProtKB.
GO; GO:0008053; P:mitochondrial fusion; IDA:UniProtKB.
GO; GO:0000002; P:mitochondrial genome maintenance; IMP:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:Ensembl.
GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR033047; Opa1.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF67; PTHR11566:SF67; 1.
Pfam; PF00350; Dynamin_N; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Cardiomyopathy;
Coiled coil; Complete proteome; Deafness; Disease mutation;
GTP-binding; Hydrolase; Lipid-binding; Membrane; Mitochondrion;
Mitochondrion inner membrane; Neurodegeneration; Nucleotide-binding;
Polymorphism; Primary mitochondrial disease; Reference proteome;
Sensory transduction; Transit peptide; Transmembrane;
Transmembrane helix; Vision.
TRANSIT 1 87 Mitochondrion.
{ECO:0000250|UniProtKB:Q2TA68}.
CHAIN 88 960 Dynamin-like 120 kDa protein,
mitochondrial.
/FTId=PRO_0000007397.
CHAIN 195 960 Dynamin-like 120 kDa protein, form S1.
{ECO:0000250|UniProtKB:Q2TA68}.
/FTId=PRO_0000253479.
TOPO_DOM 88 96 Mitochondrial matrix. {ECO:0000250}.
TRANSMEM 97 113 Helical. {ECO:0000255}.
TOPO_DOM 114 960 Mitochondrial intermembrane.
{ECO:0000250}.
DOMAIN 285 561 Dynamin-type G.
NP_BIND 295 302 GTP. {ECO:0000255}.
NP_BIND 398 402 GTP. {ECO:0000255}.
NP_BIND 467 470 GTP. {ECO:0000255}.
COILED 210 254 {ECO:0000255}.
COILED 895 960 {ECO:0000255}.
SITE 194 195 Cleavage at site S1.
{ECO:0000250|UniProtKB:Q2TA68}.
MOD_RES 228 228 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 150 185 Missing (in isoform 3 and isoform 7).
/FTId=VSP_059072.
VAR_SEQ 186 186 G -> GHKLVSEVIGASDLLLLLG (in isoform 4
and isoform 5).
/FTId=VSP_059073.
VAR_SEQ 206 206 F -> FRKGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQ
QK (in isoform 3 and isoform 4).
/FTId=VSP_059074.
VAR_SEQ 209 209 V -> GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKR
KV (in isoform 2). {ECO:0000305}.
/FTId=VSP_021035.
VARIANT 8 8 A -> S (in OPA1; dbSNP:rs794726939).
{ECO:0000269|PubMed:16617242}.
/FTId=VAR_060825.
VARIANT 38 43 Missing (in OPA1).
{ECO:0000269|PubMed:12036970}.
/FTId=VAR_022923.
VARIANT 80 80 Y -> C (in OPA1; dbSNP:rs151103940).
{ECO:0000269|PubMed:16617242}.
/FTId=VAR_060826.
VARIANT 95 95 T -> M (in OPA1; dbSNP:rs201214736).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060827.
VARIANT 102 102 Y -> C (in OPA1; dbSNP:rs530896300).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060828.
VARIANT 158 158 S -> N (in dbSNP:rs7624750).
{ECO:0000269|PubMed:11440988,
ECO:0000269|PubMed:11440989,
ECO:0000269|PubMed:12036970,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15948788,
ECO:0000269|PubMed:16617242,
ECO:0000269|PubMed:9628581}.
/FTId=VAR_022924.
VARIANT 167 167 P -> L. {ECO:0000269|PubMed:12036970}.
/FTId=VAR_022925.
VARIANT 192 192 A -> V (in dbSNP:rs34307082).
{ECO:0000269|PubMed:11440988,
ECO:0000269|PubMed:12036970,
ECO:0000269|PubMed:16617242}.
/FTId=VAR_022926.
VARIANT 270 270 E -> K (in OPA1).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060829.
VARIANT 272 272 L -> P (in OPA1).
{ECO:0000269|PubMed:14961560}.
/FTId=VAR_060830.
VARIANT 273 273 D -> A (in OPA1).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060831.
VARIANT 290 290 R -> Q (in OPA1; dbSNP:rs121908375).
{ECO:0000269|PubMed:11017080,
ECO:0000269|PubMed:11440988,
ECO:0000269|PubMed:11440989,
ECO:0000269|PubMed:11810270}.
/FTId=VAR_011483.
VARIANT 290 290 R -> W (in OPA1; dbSNP:rs780333963).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060832.
VARIANT 293 294 Missing (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060833.
VARIANT 300 300 G -> E (in OPA1; loss of GTPase activity;
loss of function in promoting
mitochondrial fusion; dbSNP:rs28939082).
{ECO:0000269|PubMed:11017079,
ECO:0000269|PubMed:11440989,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_011484.
VARIANT 310 310 Q -> R (in OPA1; dbSNP:rs770966290).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060834.
VARIANT 324 326 Missing (in OPA1).
{ECO:0000269|PubMed:15948788}.
/FTId=VAR_060835.
VARIANT 330 330 T -> S (in OPA1).
{ECO:0000269|PubMed:23401657}.
/FTId=VAR_072125.
VARIANT 357 357 A -> T (in DOA+ and OPA1;
dbSNP:rs190223702).
{ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:19319978}.
/FTId=VAR_060836.
VARIANT 377 377 V -> I (in OPA1; dbSNP:rs780922750).
{ECO:0000269|PubMed:23401657}.
/FTId=VAR_072126.
VARIANT 382 382 I -> M (in OPA1 and BEHRS;
dbSNP:rs143319805).
{ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:21636302,
ECO:0000269|PubMed:25146916}.
/FTId=VAR_060837.
VARIANT 384 384 L -> F (in OPA1).
{ECO:0000269|PubMed:11440989}.
/FTId=VAR_060838.
VARIANT 396 396 L -> P (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060839.
VARIANT 396 396 L -> R (in OPA1; dbSNP:rs727504060).
{ECO:0000269|PubMed:12036970}.
/FTId=VAR_022927.
VARIANT 400 400 P -> A (in OPA1).
{ECO:0000269|PubMed:22382025}.
/FTId=VAR_067355.
VARIANT 402 402 V -> M (in BEHRS; dbSNP:rs879255594).
{ECO:0000269|PubMed:25012220}.
/FTId=VAR_075903.
VARIANT 429 430 Missing (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060840.
VARIANT 430 430 N -> D (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060841.
VARIANT 432 432 Missing (in OPA1).
{ECO:0000269|PubMed:11017080,
ECO:0000269|PubMed:12036970}.
/FTId=VAR_011485.
VARIANT 438 438 D -> V (in OPA1).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060842.
VARIANT 439 439 G -> V (in DOA+ and OPA1; decreased
GTPase activity; loss of function in
promoting mitochondrial fusion;
dbSNP:rs387906900).
{ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:18204809,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_072127.
VARIANT 445 445 R -> H (in DOA+ and OPA1; decreased
GTPase activity; loss of function in
promoting mitochondrial fusion;
dbSNP:rs80356529).
{ECO:0000269|PubMed:12566046,
ECO:0000269|PubMed:15531309,
ECO:0000269|PubMed:16240368,
ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_015741.
VARIANT 449 449 T -> P (in DOA+).
{ECO:0000269|PubMed:23387428}.
/FTId=VAR_072128.
VARIANT 449 449 T -> R (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060843.
VARIANT 459 459 G -> E (in OPA1).
{ECO:0000269|PubMed:22857269}.
/FTId=VAR_072129.
VARIANT 463 463 I -> IFIF (in OPA1).
/FTId=VAR_060844.
VARIANT 468 468 K -> E (in OPA1).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060845.
VARIANT 470 470 D -> G (in OPA1).
{ECO:0000269|PubMed:14961560}.
/FTId=VAR_060846.
VARIANT 487 487 E -> K (in OPA1 and BEHRS).
{ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:25012220}.
/FTId=VAR_060847.
VARIANT 502 502 V -> G. {ECO:0000269|PubMed:19969356}.
/FTId=VAR_072130.
VARIANT 503 503 T -> K (in OPA1).
{ECO:0000269|PubMed:11440989,
ECO:0000269|PubMed:12036970}.
/FTId=VAR_022928.
VARIANT 505 505 K -> N (in OPA1).
{ECO:0000269|PubMed:11440989}.
/FTId=VAR_060848.
VARIANT 534 534 L -> R (in MTDPS14; dbSNP:rs869312995).
{ECO:0000269|PubMed:26561570}.
/FTId=VAR_075904.
VARIANT 545 545 S -> R (in DOA+ and OPA1; decreased
GTPase activity; loss of function in
promoting mitochondrial fusion;
dbSNP:rs398124298).
{ECO:0000269|PubMed:16513463,
ECO:0000269|PubMed:18065439,
ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_026533.
VARIANT 550 550 D -> N. {ECO:0000269|PubMed:11440988}.
/FTId=VAR_060849.
VARIANT 551 551 C -> Y (in OPA1 and DOA+;
dbSNP:rs879255592).
{ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:21112924}.
/FTId=VAR_060851.
VARIANT 551 551 Missing (in OPA1).
{ECO:0000269|PubMed:11440988}.
/FTId=VAR_060850.
VARIANT 571 571 R -> H (in OPA1; dbSNP:rs140606054).
{ECO:0000269|PubMed:12036970}.
/FTId=VAR_022929.
VARIANT 574 574 L -> P (in OPA1).
{ECO:0000269|PubMed:14961560}.
/FTId=VAR_060852.
VARIANT 582 582 Y -> C (in DOA+; dbSNP:rs121908376).
{ECO:0000269|PubMed:18195150}.
/FTId=VAR_060853.
VARIANT 586 589 Missing (in OPA1).
{ECO:0000269|PubMed:12036970}.
/FTId=VAR_022930.
VARIANT 590 590 R -> Q (in OPA1; dbSNP:rs147077380).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060854.
VARIANT 590 590 R -> W (in OPA1; dbSNP:rs778998909).
{ECO:0000269|PubMed:15948788}.
/FTId=VAR_060855.
VARIANT 593 593 L -> P (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060856.
VARIANT 593 593 Missing (in OPA1).
{ECO:0000269|PubMed:19969356}.
/FTId=VAR_072131.
VARIANT 646 646 S -> L (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060857.
VARIANT 700 701 Missing (in OPA1).
{ECO:0000269|PubMed:14961560}.
/FTId=VAR_060858.
VARIANT 728 728 N -> K (in OPA1; loss of function in
promoting mitochondrial fusion).
{ECO:0000269|PubMed:15948788,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_060859.
VARIANT 768 768 G -> D (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060860.
VARIANT 781 781 R -> W (in OPA1; dbSNP:rs190235251).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060861.
VARIANT 785 785 Q -> R (in OPA1; loss of lipid binding
and partial loss of function in promoting
mitochondrial fusion).
{ECO:0000269|PubMed:11440988,
ECO:0000269|PubMed:11810270,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_060862.
VARIANT 823 823 S -> Y (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060863.
VARIANT 841 841 Y -> C (in OPA1).
{ECO:0000269|PubMed:16617242}.
/FTId=VAR_060864.
VARIANT 882 882 R -> L (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060865.
VARIANT 887 887 L -> P (in OPA1).
{ECO:0000269|PubMed:19319978}.
/FTId=VAR_060866.
VARIANT 907 907 E -> G (in dbSNP:rs863224138).
{ECO:0000269|PubMed:11440989}.
/FTId=VAR_060867.
VARIANT 910 910 V -> D (in DOA+; impairs protein folding;
loss of function in promoting
mitochondrial fusion; dbSNP:rs387906901).
{ECO:0000269|PubMed:18158317,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_072132.
VARIANT 910 910 Missing (in OPA1).
{ECO:0000269|PubMed:22857269}.
/FTId=VAR_072133.
VARIANT 932 932 R -> C (in OPA1; dbSNP:rs145710079).
{ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:19325939}.
/FTId=VAR_060868.
VARIANT 939 939 L -> P (in OPA1; impairs protein folding;
loss of function in promoting
mitochondrial fusion).
{ECO:0000269|PubMed:11810270,
ECO:0000269|PubMed:20185555}.
/FTId=VAR_028370.
VARIANT 949 949 L -> P (in OPA1).
{ECO:0000269|PubMed:19319978,
ECO:0000269|PubMed:19969356}.
/FTId=VAR_060869.
SEQUENCE 960 AA; 111631 MW; 1C397109787AEB4D CRC64;
MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHHPTLKL QRPQLRTSFQ
QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD
QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPSSE DLVKLAPDFD KIVESLSLLK
DFFTSGSPEE TAFRATDRGS ESDKHFRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN
KELRKLVLQK DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG
KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL TKEEDLAALR
HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP GVINTVTSGM APDTKETIFS
ISKAYMQNPN AIILCIQDGS VDAERSIVTD LVSQMDPHGR RTIFVLTKVD LAEKNVASPS
RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT
TRNLSLAVSD CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE
ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW
TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED
SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQARLKDTE NAIENMVGPD WKKRWLYWKN
RTQEQCVHNE TKNELEKMLK CNEEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV
YRRHFLKTAL NHCNLCRRGF YYYQRHFVDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
TEVRRLEKNV KEVLEDFAED GEKKIKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK


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