OPA1_HUMAN
ID OPA1_HUMAN Reviewed; 960 AA.
AC O60313; D3DNW4; E5KLJ5; E5KLJ6; E5KLJ7; E5KLK1; E5KLK2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE EC=3.6.5.5 {ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:28746876};
DE AltName: Full=Optic atrophy protein 1;
DE Contains:
DE RecName: Full=Dynamin-like 120 kDa protein, form S1;
DE Flags: Precursor;
GN Name=OPA1 {ECO:0000303|PubMed:11810270, ECO:0000303|PubMed:28746876,
GN ECO:0000312|HGNC:HGNC:8140}; Synonyms=KIAA0567;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-158.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 3; 4; 5 AND 7).
RX PubMed=20843780; DOI=10.1093/nar/gkq750;
RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M.,
RA Speed T.P., Scharfe C.;
RT "Identification of rare DNA variants in mitochondrial disorders with
RT improved array-based sequencing.";
RL Nucleic Acids Res. 39:44-58(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-158.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND VARIANTS OPA1 GLN-290; ARG-785 AND
RP PRO-939.
RX PubMed=11810270; DOI=10.1007/s00439-001-0633-y;
RA Delettre C., Griffoin J.-M., Kaplan J., Dollfus H., Lorenz B., Faivre L.,
RA Lenaers G., Belenguer P., Hamel C.P.;
RT "Mutation spectrum and splicing variants in the OPA1 gene.";
RL Hum. Genet. 109:584-591(2001).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT OPA1 GLU-300.
RX PubMed=11017079; DOI=10.1038/79936;
RA Delettre C., Lenaers G., Griffoin J.-M., Gigarel N., Lorenzo C.,
RA Belenguer P., Pelloquin L., Grosgeorge J., Turc-Carel C., Perret E.,
RA Astarie-Dequeker C., Lasquellec L., Arnaud B., Ducommun B., Kaplan J.,
RA Hamel C.P.;
RT "Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is
RT mutated in dominant optic atrophy.";
RL Nat. Genet. 26:207-210(2000).
RN [8]
RP TISSUE SPECIFICITY, AND VARIANTS OPA1 GLN-290 AND ILE-432 DEL.
RX PubMed=11017080; DOI=10.1038/79944;
RA Alexander C., Votruba M., Pesch U.E.A., Thiselton D.L., Mayer S., Moore A.,
RA Rodriguez M., Kellner U., Leo-Kottler B., Auburger G., Bhattacharya S.S.,
RA Wissinger B.;
RT "OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant
RT optic atrophy linked to chromosome 3q28.";
RL Nat. Genet. 26:211-215(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC PROCESSING.
RX PubMed=16778770; DOI=10.1038/sj.emboj.7601184;
RA Ishihara N., Fujita Y., Oka T., Mihara K.;
RT "Regulation of mitochondrial morphology through proteolytic cleavage of
RT OPA1.";
RL EMBO J. 25:2966-2977(2006).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=17709429; DOI=10.1083/jcb.200704110;
RA Song Z., Chen H., Fiket M., Alexander C., Chan D.C.;
RT "OPA1 processing controls mitochondrial fusion and is regulated by mRNA
RT splicing, membrane potential, and Yme1L.";
RL J. Cell Biol. 178:749-755(2007).
RN [11]
RP FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=20038677; DOI=10.1083/jcb.200906083;
RA Head B., Griparic L., Amiri M., Gandre-Babbe S., van der Bliek A.M.;
RT "Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease
RT in mammalian cells.";
RL J. Cell Biol. 187:959-966(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP INTERACTION WITH PRELID1.
RX PubMed=21364629; DOI=10.1038/cddis.2009.19;
RA McKeller M.R., Herrera-Rodriguez S., Ma W., Ortiz-Quintero B., Rangel R.,
RA Cande C., Sims-Mourtada J.C., Melnikova V., Kashi C., Phan L.M., Chen Z.,
RA Huang P., Dunner K. Jr., Kroemer G., Singh K.K., Martinez-Valdez H.;
RT "Vital function of PRELI and essential requirement of its LEA motif.";
RL Cell Death Dis. 1:E21-E21(2010).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, CHARACTERIZATION OF VARIANTS OPA1
RP GLU-300; VAL-439; HIS-445; ARG-545; LYS-728; ARG-785 AND PRO-939, AND
RP CHARACTERIZATION OF VARIANTS VARIANT DOA+ THR-357; VAL-439; HIS-445;
RP ARG-545 AND ASP-910.
RX PubMed=20185555; DOI=10.1093/hmg/ddq088;
RA Ban T., Heymann J.A., Song Z., Hinshaw J.E., Chan D.C.;
RT "OPA1 disease alleles causing dominant optic atrophy have defects in
RT cardiolipin-stimulated GTP hydrolysis and membrane tubulation.";
RL Hum. Mol. Genet. 19:2113-2122(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP INVOLVEMENT IN DOA+, AND VARIANT DOA+ TYR-551.
RX PubMed=21112924; DOI=10.1093/brain/awq306;
RA Marelli C., Amati-Bonneau P., Reynier P., Layet V., Layet A., Stevanin G.,
RA Brissaud E., Bonneau D., Durr A., Brice A.;
RT "Heterozygous OPA1 mutations in Behr syndrome.";
RL Brain 134:E169-E169(2011).
RN [17]
RP FUNCTION (ISOFORMS 4 AND 5), AND SUBCELLULAR LOCATION.
RX PubMed=20974897; DOI=10.1101/gr.108696.110;
RA Elachouri G., Vidoni S., Zanna C., Pattyn A., Boukhaddaoui H., Gaget K.,
RA Yu-Wai-Man P., Gasparre G., Sarzi E., Delettre C., Olichon A., Loiseau D.,
RA Reynier P., Chinnery P.F., Rotig A., Carelli V., Hamel C.P., Rugolo M.,
RA Lenaers G.;
RT "OPA1 links human mitochondrial genome maintenance to mtDNA replication and
RT distribution.";
RL Genome Res. 21:12-20(2011).
RN [18]
RP INTERACTION WITH CHCHD3 AND IMMT.
RX PubMed=21081504; DOI=10.1074/jbc.m110.171975;
RA Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A.,
RA Perkins G.A., Ellisman M.H., Taylor S.S.;
RT "ChChd3, an inner mitochondrial membrane protein, is essential for
RT maintaining crista integrity and mitochondrial function.";
RL J. Biol. Chem. 286:2918-2932(2011).
RN [19]
RP INVOLVEMENT IN BEHRS, AND VARIANT BEHRS MET-382.
RX PubMed=21636302; DOI=10.1016/j.ymgme.2011.04.018;
RA Schaaf C.P., Blazo M., Lewis R.A., Tonini R.E., Takei H., Wang J.,
RA Wong L.J., Scaglia F.;
RT "Early-onset severe neuromuscular phenotype associated with compound
RT heterozygosity for OPA1 mutations.";
RL Mol. Genet. Metab. 103:383-387(2011).
RN [20]
RP INVOLVEMENT IN BEHRS, AND VARIANTS BEHRS MET-382; MET-402 AND LYS-487.
RX PubMed=25012220; DOI=10.1093/brain/awu184;
RA Bonneau D., Colin E., Oca F., Ferre M., Chevrollier A., Gueguen N.,
RA Desquiret-Dumas V., N'Guyen S., Barth M., Zanlonghi X., Rio M.,
RA Desguerre I., Barnerias C., Momtchilova M., Rodriguez D., Slama A.,
RA Lenaers G., Procaccio V., Amati-Bonneau P., Reynier P.;
RT "Early-onset Behr syndrome due to compound heterozygous mutations in
RT OPA1.";
RL Brain 137:E301-E301(2014).
RN [21]
RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=24616225; DOI=10.1083/jcb.201308006;
RA Anand R., Wai T., Baker M.J., Kladt N., Schauss A.C., Rugarli E.,
RA Langer T.;
RT "The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial
RT fusion and fission.";
RL J. Cell Biol. 204:919-929(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP INVOLVEMENT IN BEHRS, AND VARIANT BEHRS MET-382.
RX PubMed=25146916; DOI=10.1093/brain/awu234;
RA Carelli V., Sabatelli M., Carrozzo R., Rizza T., Schimpf S., Wissinger B.,
RA Zanna C., Rugolo M., La Morgia C., Caporali L., Carbonelli M., Barboni P.,
RA Tonon C., Lodi R., Bertini E.;
RT "'Behr syndrome' with OPA1 compound heterozygote mutations.";
RL Brain 138:E321-E321(2015).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP PROTEOLYTIC CLEAVAGE BY YME1L.
RX PubMed=27495975; DOI=10.7554/elife.16078;
RA Hartmann B., Wai T., Hu H., MacVicar T., Musante L., Fischer-Zirnsak B.,
RA Stenzel W., Graef R., van den Heuvel L., Ropers H.H., Wienker T.F.,
RA Huebner C., Langer T., Kaindl A.M.;
RT "Homozygous YME1L1 mutation causes mitochondriopathy with optic atrophy and
RT mitochondrial network fragmentation.";
RL Elife 5:0-0(2016).
RN [26]
RP INVOLVEMENT IN MTDPS14, AND VARIANT MTDPS14 ARG-534.
RX PubMed=26561570; DOI=10.1136/jmedgenet-2015-103361;
RA Spiegel R., Saada A., Flannery P.J., Burte F., Soiferman D., Khayat M.,
RA Eisner V., Vladovski E., Taylor R.W., Bindoff L.A., Shaag A., Mandel H.,
RA Schuler-Furman O., Shalev S.A., Elpeleg O., Yu-Wai-Man P.;
RT "Fatal infantile mitochondrial encephalomyopathy, hypertrophic
RT cardiomyopathy and optic atrophy associated with a homozygous OPA1
RT mutation.";
RL J. Med. Genet. 53:127-131(2016).
RN [27]
RP ACTIVITY REGULATION, SUBUNIT, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=28746876; DOI=10.1016/j.celrep.2017.06.090;
RA Huang G., Massoudi D., Muir A.M., Joshi D.C., Zhang C.L., Chiu S.Y.,
RA Greenspan D.S.;
RT "WBSCR16 Is a Guanine Nucleotide Exchange Factor Important for
RT Mitochondrial Fusion.";
RL Cell Rep. 20:923-934(2017).
RN [28]
RP VARIANTS OPA1 LYS-270; ALA-273; GLN-290; TRP-290; VAL-438; GLU-468; CYS-551
RP DEL AND ARG-785, AND VARIANTS ASN-158; VAL-192 AND ASN-550.
RX PubMed=11440988; DOI=10.1093/hmg/10.13.1359;
RA Pesch U.E.A., Leo-Kottler B., Mayer S., Jurklies B., Kellner U.,
RA Apfelstedt-Sylla E., Zrenner E., Alexander C., Wissinger B.;
RT "OPA1 mutations in patients with autosomal dominant optic atrophy and
RT evidence for semi-dominant inheritance.";
RL Hum. Mol. Genet. 10:1359-1368(2001).
RN [29]
RP VARIANTS OPA1 GLN-290; GLU-300; PHE-384; LYS-503 AND ASN-505, AND VARIANTS
RP ASN-158 AND GLY-907.
RX PubMed=11440989; DOI=10.1093/hmg/10.13.1369;
RA Toomes C., Marchbank N.J., Mackey D.A., Craig J.E., Newbury-Ecob R.A.,
RA Bennett C.P., Vize C.J., Desai S.P., Black G.C.M., Patel N., Teimory M.,
RA Markham A.F., Inglehearn C.F., Churchill A.J.;
RT "Spectrum, frequency and penetrance of OPA1 mutations in dominant optic
RT atrophy.";
RL Hum. Mol. Genet. 10:1369-1378(2001).
RN [30]
RP VARIANTS OPA1 38-ARG--SER-43 DEL; 586-ARG--ASP-589 DEL; ARG-396; ILE-432
RP DEL; LYS-503 AND HIS-571, AND VARIANTS ASN-158; LEU-167 AND VAL-192.
RX PubMed=12036970;
RA Thiselton D.L., Alexander C., Taanman J.-W., Brooks S., Rosenberg T.,
RA Eiberg H., Andreasson S., Van Regemorter N., Munier F.L., Moore A.T.,
RA Bhattacharya S.S., Votruba M.;
RT "A comprehensive survey of mutations in the OPA1 gene in patients with
RT autosomal dominant optic atrophy.";
RL Invest. Ophthalmol. Vis. Sci. 43:1715-1724(2002).
RN [31]
RP VARIANT OPA1 HIS-445.
RX PubMed=12566046; DOI=10.1016/s0002-9394(02)01929-3;
RA Shimizu S., Mori N., Kishi M., Sugata H., Tsuda A., Kubota N.;
RT "A novel mutation in the OPA1 gene in a Japanese patient with optic
RT atrophy.";
RL Am. J. Ophthalmol. 135:256-257(2003).
RN [32]
RP VARIANTS OPA1 PRO-272; GLY-470; PRO-574 AND 700-LEU-LYS-701 DEL.
RX PubMed=14961560; DOI=10.1002/humu.9152;
RA Baris O., Delettre C., Amati-Bonneau P., Surget M.-O., Charlin J.-F.,
RA Catier A., Derieux L., Guyomard J.-L., Dollfus H., Jonveaux P., Ayuso C.,
RA Maumenee I., Lorenz B., Mohammed S., Tourmen Y., Bonneau D., Malthiery Y.,
RA Hamel C., Reynier P.;
RT "Fourteen novel OPA1 mutations in autosomal dominant optic atrophy
RT including two de novo mutations in sporadic optic atrophy.";
RL Hum. Mutat. 21:656-656(2003).
RN [33]
RP VARIANT DOA+ HIS-445.
RX PubMed=15531309; DOI=10.1016/j.ajo.2004.06.011;
RA Payne M., Yang Z., Katz B.J., Warner J.E.A., Weight C.J., Zhao Y.,
RA Pearson E.D., Treft R.L., Hillman T., Kennedy R.J., Meire F.M., Zhang K.;
RT "Dominant optic atrophy, sensorineural hearing loss, ptosis, and
RT ophthalmoplegia: a syndrome caused by a missense mutation in OPA1.";
RL Am. J. Ophthalmol. 138:749-755(2004).
RN [34]
RP VARIANTS OPA1 324-ARG--PRO-326 DEL; TRP-590 AND LYS-728, AND VARIANT
RP ASN-158.
RX PubMed=15948788; DOI=10.1111/j.1600-0420.2005.00448.x;
RA Puomila A., Huoponen K., Maentyjaervi M., Haemaelaeinen P., Paananen R.,
RA Sankila E.-M., Savontaus M.-L., Somer M., Nikoskelainen E.;
RT "Dominant optic atrophy: correlation between clinical and molecular genetic
RT studies.";
RL Acta Ophthalmol. Scand. 83:337-346(2005).
RN [35]
RP VARIANT DOA+ HIS-445.
RX PubMed=16240368; DOI=10.1002/ana.20681;
RA Amati-Bonneau P., Guichet A., Olichon A., Chevrollier A., Viala F.,
RA Miot S., Ayuso C., Odent S., Arrouet C., Verny C., Calmels M.-N.,
RA Simard G., Belenguer P., Wang J., Puel J.-L., Hamel C., Malthiery Y.,
RA Bonneau D., Lenaers G., Reynier P.;
RT "OPA1 R445H mutation in optic atrophy associated with sensorineural
RT deafness.";
RL Ann. Neurol. 58:958-963(2005).
RN [36]
RP VARIANTS OPA1 SER-8; CYS-80 AND CYS-841, AND VARIANTS ASN-158 AND VAL-192.
RX PubMed=16617242; DOI=10.1097/01.gim.0000214299.61930.c0;
RA Han J., Thompson-Lowrey A.J., Reiss A., Mayorov V., Jia H., Biousse V.,
RA Newman N.J., Brown M.D.;
RT "OPA1 mutations and mitochondrial DNA haplotypes in autosomal dominant
RT optic atrophy.";
RL Genet. Med. 8:217-225(2006).
RN [37]
RP VARIANT OPA1 ARG-545.
RX PubMed=16513463; DOI=10.1016/j.ophtha.2005.10.054;
RA Nakamura M., Lin J., Ueno S., Asaoka R., Hirai T., Hotta Y., Miyake Y.,
RA Terasaki H.;
RT "Novel mutations in the OPA1 gene and associated clinical features in
RT Japanese patients with optic atrophy.";
RL Ophthalmology 113:483-488(2006).
RN [38]
RP VARIANT OPA1 HIS-229 (ISOFORM 2).
RX PubMed=18360822; DOI=10.1002/ana.21376;
RA Cornille K., Milea D., Amati-Bonneau P., Procaccio V., Zazoun L.,
RA Guillet V., El Achouri G., Delettre C., Gueguen N., Loiseau D., Muller A.,
RA Ferre M., Chevrollier A., Wallace D.C., Bonneau D., Hamel C., Reynier P.,
RA Lenaers G.;
RT "Reversible optic neuropathy with OPA1 exon 5b mutation.";
RL Ann. Neurol. 63:667-671(2008).
RN [39]
RP VARIANT DOA+ CYS-582.
RX PubMed=18195150; DOI=10.1001/archneurol.2007.9;
RA Ferraris S., Clark S., Garelli E., Davidzon G., Moore S.A., Kardon R.H.,
RA Bienstock R.J., Longley M.J., Mancuso M., Gutierrez Rios P., Hirano M.,
RA Copeland W.C., DiMauro S.;
RT "Progressive external ophthalmoplegia and vision and hearing loss in a
RT patient with mutations in POLG2 and OPA1.";
RL Arch. Neurol. 65:125-131(2008).
RN [40]
RP VARIANT DOA+ ARG-545.
RX PubMed=18065439; DOI=10.1093/brain/awm272;
RA Hudson G., Amati-Bonneau P., Blakely E.L., Stewart J.D., He L.,
RA Schaefer A.M., Griffiths P.G., Ahlqvist K., Suomalainen A., Reynier P.,
RA McFarland R., Turnbull D.M., Chinnery P.F., Taylor R.W.;
RT "Mutation of OPA1 causes dominant optic atrophy with external
RT ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions:
RT a novel disorder of mtDNA maintenance.";
RL Brain 131:329-337(2008).
RN [41]
RP VARIANTS DOA+ THR-357; VAL-439; HIS-445; ARG-545 AND ASP-910, AND FUNCTION.
RX PubMed=18158317; DOI=10.1093/brain/awm298;
RA Amati-Bonneau P., Valentino M.L., Reynier P., Gallardo M.E., Bornstein B.,
RA Boissiere A., Campos Y., Rivera H., de la Aleja J.G., Carroccia R.,
RA Iommarini L., Labauge P., Figarella-Branger D., Marcorelles P., Furby A.,
RA Beauvais K., Letournel F., Liguori R., La Morgia C., Montagna P.,
RA Liguori M., Zanna C., Rugolo M., Cossarizza A., Wissinger B., Verny C.,
RA Schwarzenbacher R., Martin M.A., Arenas J., Ayuso C., Garesse R.,
RA Lenaers G., Bonneau D., Carelli V.;
RT "OPA1 mutations induce mitochondrial DNA instability and optic atrophy
RT 'plus' phenotypes.";
RL Brain 131:338-351(2008).
RN [42]
RP VARIANT OPA1 VAL-439.
RX PubMed=18204809; DOI=10.1007/s00415-008-0571-x;
RA Liguori M., La Russa A., Manna I., Andreoli V., Caracciolo M.,
RA Spadafora P., Cittadella R., Quattrone A.;
RT "A phenotypic variation of dominant optic atrophy and deafness (ADOAD) due
RT to a novel OPA1 mutation.";
RL J. Neurol. 255:127-129(2008).
RN [43]
RP VARIANTS OPA1 MET-95; CYS-102; 293-VAL-VAL-294 DEL; ARG-310; THR-357;
RP MET-382; PRO-396; 429-PRO-ASN-430 DEL; ASP-430; ARG-449; 463-ILE-PHE-464
RP INS; LYS-487; ARG-545; TYR-551; GLN-590; PRO-593; LEU-646; ASP-768;
RP TRP-781; TYR-823; LEU-882; PRO-887; CYS-932 AND PRO-949.
RX PubMed=19319978; DOI=10.1002/humu.21025;
RA Ferre M., Bonneau D., Milea D., Chevrollier A., Verny C., Dollfus H.,
RA Ayuso C., Defoort S., Vignal C., Zanlonghi X., Charlin J.-F., Kaplan J.,
RA Odent S., Hamel C.P., Procaccio V., Reynier P., Amati-Bonneau P.;
RT "Molecular screening of 980 cases of suspected hereditary optic neuropathy
RT with a report on 77 novel OPA1 mutations.";
RL Hum. Mutat. 30:E692-E705(2009).
RN [44]
RP VARIANT OPA1 CYS-932.
RX PubMed=19325939;
RA Nochez Y., Arsene S., Gueguen N., Chevrollier A., Ferre M., Guillet V.,
RA Desquiret V., Toutain A., Bonneau D., Procaccio V., Amati-Bonneau P.,
RA Pisella P.-J., Reynier P.;
RT "Acute and late-onset optic atrophy due to a novel OPA1 mutation leading to
RT a mitochondrial coupling defect.";
RL Mol. Vis. 15:598-608(2009).
RN [45]
RP VARIANTS OPA1 LEU-593 DEL AND PRO-949, AND VARIANT GLY-502.
RX PubMed=19969356; DOI=10.1016/j.ophtha.2009.07.019;
RA Yen M.Y., Wang A.G., Lin Y.C., Fann M.J., Hsiao K.J.;
RT "Novel mutations of the OPA1 gene in Chinese dominant optic atrophy.";
RL Ophthalmology 117:392-396(2010).
RN [46]
RP VARIANT OPA1 ALA-400.
RX PubMed=22382025; DOI=10.1016/j.bbrc.2012.02.073;
RA Zhang J., Yuan Y., Lin B., Feng H., Li Y., Dai X., Zhou H., Dong X.,
RA Liu X.L., Guan M.X.;
RT "A novel OPA1 mutation in a Chinese family with autosomal dominant optic
RT atrophy.";
RL Biochem. Biophys. Res. Commun. 419:670-675(2012).
RN [47]
RP VARIANTS OPA1 GLU-459 AND VAL-910 DEL.
RX PubMed=22857269; DOI=10.1186/1471-2350-13-65;
RA Almind G.J., Ek J., Rosenberg T., Eiberg H., Larsen M., Lucamp L.,
RA Brondum-Nielsen K., Gronskov K.;
RT "Dominant optic atrophy in Denmark - report of 15 novel mutations in OPA1,
RT using a strategy with a detection rate of 90%.";
RL BMC Med. Genet. 13:65-65(2012).
RN [48]
RP VARIANT DOA+ PRO-449.
RX PubMed=23387428; DOI=10.1111/aos.12038;
RA Liskova P., Ulmanova O., Tesina P., Melsova H., Diblik P., Hansikova H.,
RA Tesarova M., Votruba M.;
RT "Novel OPA1 missense mutation in a family with optic atrophy and severe
RT widespread neurological disorder.";
RL Acta Ophthalmol. 91:E225-E231(2013).
RN [49]
RP VARIANTS OPA1 SER-330 AND ILE-377.
RX PubMed=23401657;
RA Chen Y., Jia X., Wang P., Xiao X., Li S., Guo X., Zhang Q.;
RT "Mutation survey of the optic atrophy 1 gene in 193 Chinese families with
RT suspected hereditary optic neuropathy.";
RL Mol. Vis. 19:292-302(2013).
CC -!- FUNCTION: Dynamin-related GTPase that is essential for normal
CC mitochondrial morphology by regulating the equilibrium between
CC mitochondrial fusion and mitochondrial fission (PubMed:16778770,
CC PubMed:17709429, PubMed:20185555, PubMed:24616225, PubMed:28746876).
CC Coexpression of isoform 1 with shorter alternative products is required
CC for optimal activity in promoting mitochondrial fusion
CC (PubMed:17709429). Binds lipid membranes enriched in negatively charged
CC phospholipids, such as cardiolipin, and promotes membrane tubulation
CC (PubMed:20185555). The intrinsic GTPase activity is low, and is
CC strongly increased by interaction with lipid membranes
CC (PubMed:20185555). Plays a role in remodeling cristae and the release
CC of cytochrome c during apoptosis (By similarity). Proteolytic
CC processing in response to intrinsic apoptotic signals may lead to
CC disassembly of OPA1 oligomers and release of the caspase activator
CC cytochrome C (CYCS) into the mitochondrial intermembrane space (By
CC similarity). Plays a role in mitochondrial genome maintenance
CC (PubMed:20974897, PubMed:18158317). {ECO:0000250|UniProtKB:P58281,
CC ECO:0000269|PubMed:16778770, ECO:0000269|PubMed:17709429,
CC ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:20185555,
CC ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:24616225,
CC ECO:0000269|PubMed:28746876}.
CC -!- FUNCTION: [Dynamin-like 120 kDa protein, form S1]: Inactive form
CC produced by cleavage at S1 position by OMA1 following stress conditions
CC that induce loss of mitochondrial membrane potential, leading to
CC negative regulation of mitochondrial fusion.
CC {ECO:0000269|PubMed:20038677}.
CC -!- FUNCTION: Isoforms that contain the alternative exon 4b (present in
CC isoform 4 and isoform 5) are required for mitochondrial genome
CC maintenance, possibly by anchoring the mitochondrial nucleoids to the
CC inner mitochondrial membrane. {ECO:0000269|PubMed:20974897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:28746876};
CC -!- ACTIVITY REGULATION: Activated by guanine nucleotide exchange factor
CC RCC1L. {ECO:0000269|PubMed:28746876}.
CC -!- SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble
CC forms of OPA1. Interacts with RCC1L; this interaction is direct
CC (PubMed:28746876). Interacts with CHCHD3 and IMMT; these interactions
CC occur preferentially with soluble OPA1 forms (PubMed:21081504). Binds
CC PARL (By similarity). Interacts with PRELID1 (PubMed:21364629).
CC {ECO:0000250|UniProtKB:P58281, ECO:0000269|PubMed:20185555,
CC ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:21364629,
CC ECO:0000269|PubMed:28746876}.
CC -!- INTERACTION:
CC O60313; Q12983: BNIP3; NbExp=10; IntAct=EBI-1054131, EBI-749464;
CC O60313; Q5S007: LRRK2; NbExp=5; IntAct=EBI-1054131, EBI-5323863;
CC O60313; Q9NTG7: SIRT3; NbExp=3; IntAct=EBI-1054131, EBI-724621;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:16778770,
CC ECO:0000269|PubMed:20974897, ECO:0000269|PubMed:28746876}; Single-pass
CC membrane protein {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane
CC {ECO:0000269|PubMed:24616225}. Note=Detected at contact sites between
CC endoplasmic reticulum and mitochondrion membranes.
CC {ECO:0000269|PubMed:24616225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000305|PubMed:11810270, ECO:0000305|PubMed:17709429};
CC Name=1; Synonyms=6;
CC IsoId=O60313-1; Sequence=Displayed;
CC Name=2; Synonyms=7 {ECO:0000303|PubMed:16778770};
CC IsoId=O60313-2; Sequence=VSP_021035;
CC Name=3;
CC IsoId=O60313-9; Sequence=VSP_059072, VSP_059074;
CC Name=4;
CC IsoId=O60313-10; Sequence=VSP_059073, VSP_059074;
CC Name=5;
CC IsoId=O60313-11; Sequence=VSP_059073;
CC Name=7;
CC IsoId=O60313-13; Sequence=VSP_059072;
CC -!- TISSUE SPECIFICITY: Highly expressed in retina. Also expressed in
CC brain, testis, heart and skeletal muscle. Isoform 1 expressed in
CC retina, skeletal muscle, heart, lung, ovary, colon, thyroid gland,
CC leukocytes and fetal brain. Isoform 2 expressed in colon, liver,
CC kidney, thyroid gland and leukocytes. Low levels of all isoforms
CC expressed in a variety of tissues. {ECO:0000269|PubMed:11017079,
CC ECO:0000269|PubMed:11017080, ECO:0000269|PubMed:11810270}.
CC -!- PTM: PARL-dependent proteolytic processing releases an antiapoptotic
CC soluble form not required for mitochondrial fusion. Cleaved by OMA1 at
CC position S1 following stress conditions. {ECO:0000269|PubMed:20038677}.
CC -!- PTM: [Isoform 2]: Cleavage at position S2 is mediated by YME1L
CC (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage may occur
CC in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ)
CC (PubMed:16778770). {ECO:0000269|PubMed:16778770,
CC ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225,
CC ECO:0000269|PubMed:27495975}.
CC -!- PTM: [Isoform 3]: Cleavage at position S2 is mediated by YME1L
CC (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage may occur
CC in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ)
CC (PubMed:16778770). {ECO:0000269|PubMed:16778770,
CC ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225,
CC ECO:0000269|PubMed:27495975}.
CC -!- PTM: [Isoform 4]: Cleavage at position S2 is mediated by YME1L
CC (PubMed:17709429, PubMed:24616225, PubMed:27495975). Cleavage may occur
CC in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ)
CC (PubMed:16778770). {ECO:0000269|PubMed:16778770,
CC ECO:0000269|PubMed:17709429, ECO:0000269|PubMed:24616225,
CC ECO:0000269|PubMed:27495975}.
CC -!- DISEASE: Optic atrophy 1 (OPA1) [MIM:165500]: A condition that features
CC progressive visual loss in association with optic atrophy. Atrophy of
CC the optic disk indicates a deficiency in the number of nerve fibers
CC which arise in the retina and converge to form the optic disk, optic
CC nerve, optic chiasm and optic tracts. OPA1 is characterized by an
CC insidious onset of visual impairment in early childhood with moderate
CC to severe loss of visual acuity, temporal optic disk pallor, color
CC vision deficits, and centrocecal scotoma of variable density.
CC {ECO:0000269|PubMed:11017079, ECO:0000269|PubMed:11017080,
CC ECO:0000269|PubMed:11440988, ECO:0000269|PubMed:11440989,
CC ECO:0000269|PubMed:11810270, ECO:0000269|PubMed:12036970,
CC ECO:0000269|PubMed:12566046, ECO:0000269|PubMed:14961560,
CC ECO:0000269|PubMed:15948788, ECO:0000269|PubMed:16513463,
CC ECO:0000269|PubMed:16617242, ECO:0000269|PubMed:18204809,
CC ECO:0000269|PubMed:18360822, ECO:0000269|PubMed:19319978,
CC ECO:0000269|PubMed:19325939, ECO:0000269|PubMed:19969356,
CC ECO:0000269|PubMed:20185555, ECO:0000269|PubMed:22382025,
CC ECO:0000269|PubMed:22857269, ECO:0000269|PubMed:23401657}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Dominant optic atrophy plus syndrome (DOA+) [MIM:125250]: A
CC neurologic disorder characterized most commonly by an insidious onset
CC of visual loss and sensorineural hearing loss in childhood with
CC variable presentation of other clinical manifestations including
CC progressive external ophthalmoplegia, muscle cramps, hyperreflexia, and
CC ataxia. There appears to be a wide range of intermediate phenotypes.
CC {ECO:0000269|PubMed:15531309, ECO:0000269|PubMed:16240368,
CC ECO:0000269|PubMed:18065439, ECO:0000269|PubMed:18158317,
CC ECO:0000269|PubMed:18195150, ECO:0000269|PubMed:20185555,
CC ECO:0000269|PubMed:21112924, ECO:0000269|PubMed:23387428}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Behr syndrome (BEHRS) [MIM:210000]: An autosomal recessive
CC syndrome characterized by optic atrophy beginning in early childhood
CC associated with ataxia, pyramidal signs, spasticity, intellectual
CC disability, and posterior column sensory loss. The ataxia, spasticity,
CC and muscle contractures, mainly of the hip adductors, hamstrings, and
CC soleus, are progressive and become more prominent in the second decade.
CC {ECO:0000269|PubMed:21636302, ECO:0000269|PubMed:25012220,
CC ECO:0000269|PubMed:25146916}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Mitochondrial DNA depletion syndrome 14,
CC cardioencephalomyopathic type (MTDPS14) [MIM:616896]: An autosomal
CC recessive mitochondrial disorder characterized by lethal infantile
CC encephalopathy, hypertrophic cardiomyopathy and optic atrophy. Skeletal
CC muscle biopsies show significant mtDNA depletion and abnormal
CC mitochondria. {ECO:0000269|PubMed:26561570}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: Contains the alternative exon 4b that is
CC important for mitochondrial genome maintenance. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Contains the alternative exon 4b that is
CC important for mitochondrial genome maintenance. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AF416919; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AB011139; BAA25493.1; -; mRNA.
DR EMBL; HQ204906; ADP90054.1; -; Genomic_DNA.
DR EMBL; HQ204906; ADP90055.1; -; Genomic_DNA.
DR EMBL; HQ204906; ADP90056.1; -; Genomic_DNA.
DR EMBL; HQ204906; ADP90057.1; -; Genomic_DNA.
DR EMBL; HQ204906; ADP90060.1; -; Genomic_DNA.
DR EMBL; HQ204906; ADP90061.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90062.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90063.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90064.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90065.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90068.1; -; Genomic_DNA.
DR EMBL; HQ204907; ADP90069.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90070.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90071.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90072.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90073.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90076.1; -; Genomic_DNA.
DR EMBL; HQ204908; ADP90077.1; -; Genomic_DNA.
DR EMBL; HQ204909; ADP90084.1; -; Genomic_DNA.
DR EMBL; HQ204909; ADP90085.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90086.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90087.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90088.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90089.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90092.1; -; Genomic_DNA.
DR EMBL; HQ204910; ADP90093.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90094.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90095.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90096.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90097.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90100.1; -; Genomic_DNA.
DR EMBL; HQ204911; ADP90101.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90102.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90103.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90104.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90105.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90108.1; -; Genomic_DNA.
DR EMBL; HQ204912; ADP90109.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90110.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90111.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90112.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90113.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90116.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90118.1; -; Genomic_DNA.
DR EMBL; HQ204913; ADP90117.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90119.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90120.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90121.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90124.1; -; Genomic_DNA.
DR EMBL; HQ204914; ADP90125.1; -; Genomic_DNA.
DR EMBL; HQ204915; ADP90132.1; -; Genomic_DNA.
DR EMBL; HQ204915; ADP90133.1; -; Genomic_DNA.
DR EMBL; HQ204916; ADP90140.1; -; Genomic_DNA.
DR EMBL; HQ204916; ADP90141.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90142.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90143.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90144.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90145.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90148.1; -; Genomic_DNA.
DR EMBL; HQ204917; ADP90149.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90150.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90151.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90152.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90153.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90156.1; -; Genomic_DNA.
DR EMBL; HQ204918; ADP90157.1; -; Genomic_DNA.
DR EMBL; HQ204919; ADP90164.1; -; Genomic_DNA.
DR EMBL; HQ204919; ADP90165.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90166.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90167.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90168.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90169.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90172.1; -; Genomic_DNA.
DR EMBL; HQ204920; ADP90173.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90174.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90175.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90176.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90177.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90180.1; -; Genomic_DNA.
DR EMBL; HQ204921; ADP90181.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90182.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90183.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90184.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90185.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90188.1; -; Genomic_DNA.
DR EMBL; HQ204922; ADP90189.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90190.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90191.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90192.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90193.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90196.1; -; Genomic_DNA.
DR EMBL; HQ204923; ADP90197.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90198.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90199.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90200.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90201.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90204.1; -; Genomic_DNA.
DR EMBL; HQ204924; ADP90205.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90206.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90207.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90208.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90209.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90212.1; -; Genomic_DNA.
DR EMBL; HQ204925; ADP90213.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90214.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90215.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90216.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90217.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90220.1; -; Genomic_DNA.
DR EMBL; HQ204926; ADP90221.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90222.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90223.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90224.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90225.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90228.1; -; Genomic_DNA.
DR EMBL; HQ204927; ADP90229.1; -; Genomic_DNA.
DR EMBL; HQ204928; ADP90236.1; -; Genomic_DNA.
DR EMBL; HQ204928; ADP90237.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90238.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90239.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90240.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90241.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90244.1; -; Genomic_DNA.
DR EMBL; HQ204929; ADP90245.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90246.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90247.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90248.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90249.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90252.1; -; Genomic_DNA.
DR EMBL; HQ204930; ADP90253.1; -; Genomic_DNA.
DR EMBL; HQ204931; ADP90260.1; -; Genomic_DNA.
DR EMBL; HQ204931; ADP90261.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90262.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90263.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90264.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90265.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90268.1; -; Genomic_DNA.
DR EMBL; HQ204932; ADP90269.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90270.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90271.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90272.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90273.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90276.1; -; Genomic_DNA.
DR EMBL; HQ204933; ADP90277.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90278.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90279.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90280.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90281.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90284.1; -; Genomic_DNA.
DR EMBL; HQ204934; ADP90285.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90286.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90287.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90288.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90289.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90292.1; -; Genomic_DNA.
DR EMBL; HQ204935; ADP90293.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90294.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90295.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90296.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90297.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90300.1; -; Genomic_DNA.
DR EMBL; HQ204936; ADP90301.1; -; Genomic_DNA.
DR EMBL; HQ204937; ADP90308.1; -; Genomic_DNA.
DR EMBL; HQ204937; ADP90309.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90310.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90311.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90312.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90313.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90316.1; -; Genomic_DNA.
DR EMBL; HQ204938; ADP90317.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90318.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90319.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90320.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90321.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90324.1; -; Genomic_DNA.
DR EMBL; HQ204939; ADP90325.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90326.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90327.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90328.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90329.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90332.1; -; Genomic_DNA.
DR EMBL; HQ204940; ADP90333.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90334.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90335.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90336.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90337.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90340.1; -; Genomic_DNA.
DR EMBL; HQ204941; ADP90341.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90342.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90343.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90344.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90345.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90348.1; -; Genomic_DNA.
DR EMBL; HQ204942; ADP90349.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90350.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90351.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90352.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90353.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90356.1; -; Genomic_DNA.
DR EMBL; HQ204943; ADP90357.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90358.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90359.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90360.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90361.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90364.1; -; Genomic_DNA.
DR EMBL; HQ204944; ADP90365.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90366.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90367.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90368.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90369.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90372.1; -; Genomic_DNA.
DR EMBL; HQ204945; ADP90373.1; -; Genomic_DNA.
DR EMBL; AC048351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78064.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78065.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78066.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78067.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78069.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78070.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78071.1; -; Genomic_DNA.
DR EMBL; BC075805; AAH75805.1; -; mRNA.
DR EMBL; AF416919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF416920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33917.1; -. [O60313-2]
DR CCDS; CCDS43186.1; -. [O60313-1]
DR CCDS; CCDS87183.1; -. [O60313-13]
DR PIR; T00336; T00336.
DR RefSeq; NP_056375.2; NM_015560.2. [O60313-1]
DR RefSeq; NP_570844.1; NM_130831.2. [O60313-13]
DR RefSeq; NP_570846.1; NM_130833.2. [O60313-9]
DR RefSeq; NP_570847.2; NM_130834.2. [O60313-11]
DR RefSeq; NP_570849.2; NM_130836.2. [O60313-2]
DR RefSeq; NP_570850.2; NM_130837.2. [O60313-10]
DR PDB; 6JTG; X-ray; 2.40 A; A=263-571.
DR PDBsum; 6JTG; -.
DR AlphaFoldDB; O60313; -.
DR SMR; O60313; -.
DR BioGRID; 111024; 188.
DR CORUM; O60313; -.
DR IntAct; O60313; 53.
DR MINT; O60313; -.
DR STRING; 9606.ENSP00000354681; -.
DR ChEMBL; CHEMBL4105705; -.
DR TCDB; 1.N.6.1.2; the mitochondrial inner/outer membrane fusion (mmf) family.
DR GlyGen; O60313; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60313; -.
DR PhosphoSitePlus; O60313; -.
DR SwissPalm; O60313; -.
DR BioMuta; OPA1; -.
DR EPD; O60313; -.
DR jPOST; O60313; -.
DR MassIVE; O60313; -.
DR MaxQB; O60313; -.
DR PaxDb; O60313; -.
DR PeptideAtlas; O60313; -.
DR PRIDE; O60313; -.
DR ProteomicsDB; 15297; -.
DR ProteomicsDB; 15298; -.
DR ProteomicsDB; 15300; -.
DR ProteomicsDB; 49340; -. [O60313-1]
DR ProteomicsDB; 49341; -. [O60313-2]
DR Antibodypedia; 33885; 316 antibodies from 32 providers.
DR DNASU; 4976; -.
DR Ensembl; ENST00000361150.6; ENSP00000354781.2; ENSG00000198836.11. [O60313-9]
DR Ensembl; ENST00000361510.8; ENSP00000355324.2; ENSG00000198836.11. [O60313-10]
DR Ensembl; ENST00000361828.7; ENSP00000354429.3; ENSG00000198836.11. [O60313-1]
DR Ensembl; ENST00000361908.8; ENSP00000354681.3; ENSG00000198836.11. [O60313-2]
DR Ensembl; ENST00000392437.6; ENSP00000376232.2; ENSG00000198836.11. [O60313-11]
DR Ensembl; ENST00000646793.1; ENSP00000494512.1; ENSG00000198836.11. [O60313-13]
DR GeneID; 4976; -.
DR KEGG; hsa:4976; -.
DR MANE-Select; ENST00000361510.8; ENSP00000355324.2; NM_130837.3; NP_570850.2. [O60313-10]
DR UCSC; uc003ftg.4; human.
DR UCSC; uc003fti.3; human. [O60313-1]
DR UCSC; uc003ftj.4; human.
DR UCSC; uc003ftk.4; human.
DR CTD; 4976; -.
DR DisGeNET; 4976; -.
DR GeneCards; OPA1; -.
DR GeneReviews; OPA1; -.
DR HGNC; HGNC:8140; OPA1.
DR HPA; ENSG00000198836; Low tissue specificity.
DR MalaCards; OPA1; -.
DR MIM; 125250; phenotype.
DR MIM; 165500; phenotype.
DR MIM; 210000; phenotype.
DR MIM; 605290; gene.
DR MIM; 616896; phenotype.
DR neXtProt; NX_O60313; -.
DR OpenTargets; ENSG00000198836; -.
DR Orphanet; 1215; Autosomal dominant optic atrophy plus syndrome.
DR Orphanet; 98673; Autosomal dominant optic atrophy, classic form.
DR PharmGKB; PA31927; -.
DR VEuPathDB; HostDB:ENSG00000198836; -.
DR eggNOG; KOG0447; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR InParanoid; O60313; -.
DR OMA; IRKQWKL; -.
DR OrthoDB; 609213at2759; -.
DR PhylomeDB; O60313; -.
DR TreeFam; TF314250; -.
DR BRENDA; 3.6.5.5; 2681.
DR PathwayCommons; O60313; -.
DR Reactome; R-HSA-169911; Regulation of Apoptosis.
DR SignaLink; O60313; -.
DR SIGNOR; O60313; -.
DR BioGRID-ORCS; 4976; 450 hits in 1086 CRISPR screens.
DR ChiTaRS; OPA1; human.
DR GeneWiki; Optic_atrophy_1; -.
DR GenomeRNAi; 4976; -.
DR Pharos; O60313; Tchem.
DR PRO; PR:O60313; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O60313; protein.
DR Bgee; ENSG00000198836; Expressed in adrenal tissue and 203 other tissues.
DR ExpressionAtlas; O60313; baseline and differential.
DR Genevisible; O60313; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:1901612; F:cardiolipin binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019896; P:axonal transport of mitochondrion; TAS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IDA:UniProtKB.
DR GO; GO:0097749; P:membrane tubulation; IDA:UniProtKB.
DR GO; GO:0000266; P:mitochondrial fission; TAS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IDA:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR033047; Opa1.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF67; PTHR11566:SF67; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cardiomyopathy;
KW Coiled coil; Deafness; Disease variant; GTP-binding; Hydrolase;
KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Neurodegeneration; Nucleotide-binding; Primary mitochondrial disease;
KW Reference proteome; Sensory transduction; Transit peptide; Transmembrane;
KW Transmembrane helix; Vision.
FT TRANSIT 1..87
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT CHAIN 88..960
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /id="PRO_0000007397"
FT CHAIN 195..960
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000253479"
FT TOPO_DOM 88..96
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 97..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..960
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT DOMAIN 285..561
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 295..302
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 321..324
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 398..401
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 467..470
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 501..504
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 210..254
FT /evidence="ECO:0000255"
FT COILED 895..960
FT /evidence="ECO:0000255"
FT BINDING 295..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 398..402
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 467..470
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 194..195
FT /note="Cleavage at site S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 150..185
FT /note="Missing (in isoform 3 and isoform 7)"
FT /id="VSP_059072"
FT VAR_SEQ 186
FT /note="G -> GHKLVSEVIGASDLLLLLG (in isoform 4 and isoform
FT 5)"
FT /id="VSP_059073"
FT VAR_SEQ 206
FT /note="F -> FRKGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQK (in
FT isoform 3 and isoform 4)"
FT /id="VSP_059074"
FT VAR_SEQ 209
FT /note="V -> GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRKV (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021035"
FT VARIANT 8
FT /note="A -> S (in OPA1; unknown pathological significance;
FT dbSNP:rs794726939)"
FT /evidence="ECO:0000269|PubMed:16617242"
FT /id="VAR_060825"
FT VARIANT 38..43
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:12036970"
FT /id="VAR_022923"
FT VARIANT 80
FT /note="Y -> C (in OPA1; dbSNP:rs151103940)"
FT /evidence="ECO:0000269|PubMed:16617242"
FT /id="VAR_060826"
FT VARIANT 95
FT /note="T -> M (in OPA1; dbSNP:rs201214736)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060827"
FT VARIANT 102
FT /note="Y -> C (in OPA1; dbSNP:rs530896300)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060828"
FT VARIANT 158
FT /note="S -> N (in dbSNP:rs7624750)"
FT /evidence="ECO:0000269|PubMed:11440988,
FT ECO:0000269|PubMed:11440989, ECO:0000269|PubMed:12036970,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15948788,
FT ECO:0000269|PubMed:16617242, ECO:0000269|PubMed:9628581"
FT /id="VAR_022924"
FT VARIANT 167
FT /note="P -> L (in dbSNP:rs754177232)"
FT /evidence="ECO:0000269|PubMed:12036970"
FT /id="VAR_022925"
FT VARIANT 192
FT /note="A -> V (in dbSNP:rs34307082)"
FT /evidence="ECO:0000269|PubMed:11440988,
FT ECO:0000269|PubMed:12036970, ECO:0000269|PubMed:16617242"
FT /id="VAR_022926"
FT VARIANT 270
FT /note="E -> K (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060829"
FT VARIANT 272
FT /note="L -> P (in OPA1)"
FT /evidence="ECO:0000269|PubMed:14961560"
FT /id="VAR_060830"
FT VARIANT 273
FT /note="D -> A (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060831"
FT VARIANT 290
FT /note="R -> Q (in OPA1; dbSNP:rs121908375)"
FT /evidence="ECO:0000269|PubMed:11017080,
FT ECO:0000269|PubMed:11440988, ECO:0000269|PubMed:11440989,
FT ECO:0000269|PubMed:11810270"
FT /id="VAR_011483"
FT VARIANT 290
FT /note="R -> W (in OPA1; dbSNP:rs780333963)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060832"
FT VARIANT 293..294
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060833"
FT VARIANT 300
FT /note="G -> E (in OPA1; loss of GTPase activity; loss of
FT function in promoting mitochondrial fusion;
FT dbSNP:rs28939082)"
FT /evidence="ECO:0000269|PubMed:11017079,
FT ECO:0000269|PubMed:11440989, ECO:0000269|PubMed:20185555"
FT /id="VAR_011484"
FT VARIANT 310
FT /note="Q -> R (in OPA1; dbSNP:rs770966290)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060834"
FT VARIANT 324..326
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:15948788"
FT /id="VAR_060835"
FT VARIANT 330
FT /note="T -> S (in OPA1)"
FT /evidence="ECO:0000269|PubMed:23401657"
FT /id="VAR_072125"
FT VARIANT 357
FT /note="A -> T (in DOA+ and OPA1; dbSNP:rs190223702)"
FT /evidence="ECO:0000269|PubMed:18158317,
FT ECO:0000269|PubMed:19319978"
FT /id="VAR_060836"
FT VARIANT 377
FT /note="V -> I (in OPA1; dbSNP:rs780922750)"
FT /evidence="ECO:0000269|PubMed:23401657"
FT /id="VAR_072126"
FT VARIANT 382
FT /note="I -> M (in OPA1 and BEHRS; dbSNP:rs143319805)"
FT /evidence="ECO:0000269|PubMed:19319978,
FT ECO:0000269|PubMed:21636302, ECO:0000269|PubMed:25146916"
FT /id="VAR_060837"
FT VARIANT 384
FT /note="L -> F (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440989"
FT /id="VAR_060838"
FT VARIANT 396
FT /note="L -> P (in OPA1; dbSNP:rs727504060)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060839"
FT VARIANT 396
FT /note="L -> R (in OPA1; dbSNP:rs727504060)"
FT /evidence="ECO:0000269|PubMed:12036970"
FT /id="VAR_022927"
FT VARIANT 400
FT /note="P -> A (in OPA1)"
FT /evidence="ECO:0000269|PubMed:22382025"
FT /id="VAR_067355"
FT VARIANT 402
FT /note="V -> M (in BEHRS; dbSNP:rs879255594)"
FT /evidence="ECO:0000269|PubMed:25012220"
FT /id="VAR_075903"
FT VARIANT 429..430
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060840"
FT VARIANT 430
FT /note="N -> D (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060841"
FT VARIANT 432
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11017080,
FT ECO:0000269|PubMed:12036970"
FT /id="VAR_011485"
FT VARIANT 438
FT /note="D -> V (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060842"
FT VARIANT 439
FT /note="G -> V (in DOA+ and OPA1; decreased GTPase activity;
FT loss of function in promoting mitochondrial fusion;
FT dbSNP:rs387906900)"
FT /evidence="ECO:0000269|PubMed:18158317,
FT ECO:0000269|PubMed:18204809, ECO:0000269|PubMed:20185555"
FT /id="VAR_072127"
FT VARIANT 445
FT /note="R -> H (in DOA+ and OPA1; decreased GTPase activity;
FT loss of function in promoting mitochondrial fusion;
FT dbSNP:rs80356529)"
FT /evidence="ECO:0000269|PubMed:12566046,
FT ECO:0000269|PubMed:15531309, ECO:0000269|PubMed:16240368,
FT ECO:0000269|PubMed:18158317, ECO:0000269|PubMed:20185555"
FT /id="VAR_015741"
FT VARIANT 449
FT /note="T -> P (in DOA+)"
FT /evidence="ECO:0000269|PubMed:23387428"
FT /id="VAR_072128"
FT VARIANT 449
FT /note="T -> R (in OPA1; dbSNP:rs1577244261)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060843"
FT VARIANT 459
FT /note="G -> E (in OPA1)"
FT /evidence="ECO:0000269|PubMed:22857269"
FT /id="VAR_072129"
FT VARIANT 463
FT /note="I -> IFIF (in OPA1)"
FT /id="VAR_060844"
FT VARIANT 468
FT /note="K -> E (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060845"
FT VARIANT 470
FT /note="D -> G (in OPA1)"
FT /evidence="ECO:0000269|PubMed:14961560"
FT /id="VAR_060846"
FT VARIANT 487
FT /note="E -> K (in OPA1 and BEHRS)"
FT /evidence="ECO:0000269|PubMed:19319978,
FT ECO:0000269|PubMed:25012220"
FT /id="VAR_060847"
FT VARIANT 502
FT /note="V -> G"
FT /evidence="ECO:0000269|PubMed:19969356"
FT /id="VAR_072130"
FT VARIANT 503
FT /note="T -> K (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440989,
FT ECO:0000269|PubMed:12036970"
FT /id="VAR_022928"
FT VARIANT 505
FT /note="K -> N (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440989"
FT /id="VAR_060848"
FT VARIANT 534
FT /note="L -> R (in MTDPS14; dbSNP:rs869312995)"
FT /evidence="ECO:0000269|PubMed:26561570"
FT /id="VAR_075904"
FT VARIANT 545
FT /note="S -> R (in DOA+ and OPA1; decreased GTPase activity;
FT loss of function in promoting mitochondrial fusion;
FT dbSNP:rs398124298)"
FT /evidence="ECO:0000269|PubMed:16513463,
FT ECO:0000269|PubMed:18065439, ECO:0000269|PubMed:18158317,
FT ECO:0000269|PubMed:19319978, ECO:0000269|PubMed:20185555"
FT /id="VAR_026533"
FT VARIANT 550
FT /note="D -> N"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060849"
FT VARIANT 551
FT /note="C -> Y (in OPA1 and DOA+; dbSNP:rs879255592)"
FT /evidence="ECO:0000269|PubMed:19319978,
FT ECO:0000269|PubMed:21112924"
FT /id="VAR_060851"
FT VARIANT 551
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:11440988"
FT /id="VAR_060850"
FT VARIANT 571
FT /note="R -> H (in OPA1; dbSNP:rs140606054)"
FT /evidence="ECO:0000269|PubMed:12036970"
FT /id="VAR_022929"
FT VARIANT 574
FT /note="L -> P (in OPA1)"
FT /evidence="ECO:0000269|PubMed:14961560"
FT /id="VAR_060852"
FT VARIANT 582
FT /note="Y -> C (in DOA+; dbSNP:rs121908376)"
FT /evidence="ECO:0000269|PubMed:18195150"
FT /id="VAR_060853"
FT VARIANT 586..589
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:12036970"
FT /id="VAR_022930"
FT VARIANT 590
FT /note="R -> Q (in OPA1; dbSNP:rs147077380)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060854"
FT VARIANT 590
FT /note="R -> W (in OPA1; dbSNP:rs778998909)"
FT /evidence="ECO:0000269|PubMed:15948788"
FT /id="VAR_060855"
FT VARIANT 593
FT /note="L -> P (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060856"
FT VARIANT 593
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19969356"
FT /id="VAR_072131"
FT VARIANT 646
FT /note="S -> L (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060857"
FT VARIANT 700..701
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:14961560"
FT /id="VAR_060858"
FT VARIANT 728
FT /note="N -> K (in OPA1; loss of function in promoting
FT mitochondrial fusion; dbSNP:rs1292852465)"
FT /evidence="ECO:0000269|PubMed:15948788,
FT ECO:0000269|PubMed:20185555"
FT /id="VAR_060859"
FT VARIANT 768
FT /note="G -> D (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060860"
FT VARIANT 781
FT /note="R -> W (in OPA1; dbSNP:rs190235251)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060861"
FT VARIANT 785
FT /note="Q -> R (in OPA1; loss of lipid binding and partial
FT loss of function in promoting mitochondrial fusion;
FT dbSNP:rs1064797302)"
FT /evidence="ECO:0000269|PubMed:11440988,
FT ECO:0000269|PubMed:11810270, ECO:0000269|PubMed:20185555"
FT /id="VAR_060862"
FT VARIANT 823
FT /note="S -> Y (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060863"
FT VARIANT 841
FT /note="Y -> C (in OPA1)"
FT /evidence="ECO:0000269|PubMed:16617242"
FT /id="VAR_060864"
FT VARIANT 882
FT /note="R -> L (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060865"
FT VARIANT 887
FT /note="L -> P (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978"
FT /id="VAR_060866"
FT VARIANT 907
FT /note="E -> G (in dbSNP:rs863224138)"
FT /evidence="ECO:0000269|PubMed:11440989"
FT /id="VAR_060867"
FT VARIANT 910
FT /note="V -> D (in DOA+; impairs protein folding; loss of
FT function in promoting mitochondrial fusion;
FT dbSNP:rs387906901)"
FT /evidence="ECO:0000269|PubMed:18158317,
FT ECO:0000269|PubMed:20185555"
FT /id="VAR_072132"
FT VARIANT 910
FT /note="Missing (in OPA1)"
FT /evidence="ECO:0000269|PubMed:22857269"
FT /id="VAR_072133"
FT VARIANT 932
FT /note="R -> C (in OPA1; dbSNP:rs145710079)"
FT /evidence="ECO:0000269|PubMed:19319978,
FT ECO:0000269|PubMed:19325939"
FT /id="VAR_060868"
FT VARIANT 939
FT /note="L -> P (in OPA1; impairs protein folding; loss of
FT function in promoting mitochondrial fusion)"
FT /evidence="ECO:0000269|PubMed:11810270,
FT ECO:0000269|PubMed:20185555"
FT /id="VAR_028370"
FT VARIANT 949
FT /note="L -> P (in OPA1)"
FT /evidence="ECO:0000269|PubMed:19319978,
FT ECO:0000269|PubMed:19969356"
FT /id="VAR_060869"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 414..426
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 449..455
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 469..475
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 479..486
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:6JTG"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 541..559
FT /evidence="ECO:0007829|PDB:6JTG"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:6JTG"
FT MOTIF O60313-2:217..222
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000269|PubMed:16778770"
FT VARIANT O60313-2:229
FT /note="R -> H (in OPA1) (Ref.28; dbSNP:rs138350727)"
FT /evidence="ECO:0000269|PubMed:18360822"
FT /id="VAR_082805"
FT MOTIF O60313-9:181..186
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000269|PubMed:16778770"
FT MOTIF O60313-10:235..240
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000269|PubMed:16778770"
SQ 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
