OPA1_MOUSE
ID OPA1_MOUSE Reviewed; 960 AA.
AC P58281; A6H6Q3; Q3ULA5; Q8BKU7; Q8BLL3; Q8BM08; Q8R3J7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE EC=3.6.5.5;
DE AltName: Full=Large GTP-binding protein;
DE Short=LargeG;
DE AltName: Full=Optic atrophy protein 1 homolog;
DE Contains:
DE RecName: Full=Dynamin-like 120 kDa protein, form S1;
DE Flags: Precursor;
GN Name=Opa1 {ECO:0000303|PubMed:28746876, ECO:0000312|MGI:MGI:1921393};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11847212; DOI=10.1074/jbc.m109260200;
RA Misaka T., Miyashita T., Kubo Y.;
RT "Primary structure of a dynamin-related mouse mitochondrial GTPase and its
RT distribution in brain, subcellular localization, and effect on
RT mitochondrial morphology.";
RL J. Biol. Chem. 277:15834-15842(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-365 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, Hypothalamus, Liver, Retina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Brain, and Mammary gland;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PARL.
RX PubMed=16839884; DOI=10.1016/j.cell.2006.06.021;
RA Cipolat S., Rudka T., Hartmann D., Costa V., Serneels L., Craessaerts K.,
RA Metzger K., Frezza C., Annaert W., D'Adamio L., Derks C., Dejaegere T.,
RA Pellegrini L., D'Hooge R., Scorrano L., De Strooper B.;
RT "Mitochondrial rhomboid PARL regulates cytochrome c release during
RT apoptosis via OPA1-dependent cristae remodeling.";
RL Cell 126:163-175(2006).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16839885; DOI=10.1016/j.cell.2006.06.025;
RA Frezza C., Cipolat S., Martins de Brito O., Micaroni M., Beznoussenko G.V.,
RA Rudka T., Bartoli D., Polishuck R.S., Danial N.N., De Strooper B.,
RA Scorrano L.;
RT "OPA1 controls apoptotic cristae remodeling independently from
RT mitochondrial fusion.";
RL Cell 126:177-189(2006).
RN [6]
RP FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=20038678; DOI=10.1083/jcb.200906084;
RA Ehses S., Raschke I., Mancuso G., Bernacchia A., Geimer S., Tondera D.,
RA Martinou J.C., Westermann B., Rugarli E.I., Langer T.;
RT "Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease
RT isoenzymes and OMA1.";
RL J. Cell Biol. 187:1023-1036(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH CHCHD3 AND IMMT, AND SUBCELLULAR LOCATION.
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 [9]
RP FUNCTION (DYNAMIN-LIKE 120 KDA PROTEIN; FORM S1), AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=22433842; DOI=10.1038/emboj.2012.70;
RA Quiros P.M., Ramsay A.J., Sala D., Fernandez-Vizarra E., Rodriguez F.,
RA Peinado J.R., Fernandez-Garcia M.S., Vega J.A., Enriquez J.A., Zorzano A.,
RA Lopez-Otin C.;
RT "Loss of mitochondrial protease OMA1 alters processing of the GTPase OPA1
RT and causes obesity and defective thermogenesis in mice.";
RL EMBO J. 31:2117-2133(2012).
RN [10]
RP PROTEOLYTIC PROCESSING.
RX PubMed=24550258; DOI=10.1002/embj.201386474;
RA Baker M.J., Lampe P.A., Stojanovski D., Korwitz A., Anand R., Tatsuta T.,
RA Langer T.;
RT "Stress-induced OMA1 activation and autocatalytic turnover regulate OPA1-
RT dependent mitochondrial dynamics.";
RL EMBO J. 33:578-593(2014).
RN [11]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
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 [12]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=26785494; DOI=10.1126/science.aad0116;
RA Wai T., Garcia-Prieto J., Baker M.J., Merkwirth C., Benit P., Rustin P.,
RA Ruperez F.J., Barbas C., Ibanez B., Langer T.;
RT "Imbalanced OPA1 processing and mitochondrial fragmentation cause heart
RT failure in mice.";
RL Science 350:116-116(2015).
RN [13]
RP SUBUNIT, FUNCTION, AND SUBCELLULAR LOCATION.
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).
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:11847212,
CC PubMed:24616225, PubMed:26785494, PubMed:28746876). Coexpression of
CC isoform 1 with shorter alternative products is required for optimal
CC activity in promoting mitochondrial fusion (By similarity). Binds lipid
CC membranes enriched in negatively charged phospholipids, such as
CC cardiolipin, and promotes membrane tubulation. The intrinsic GTPase
CC activity is low, and is strongly increased by interaction with lipid
CC membranes (By similarity). Plays a role in remodeling cristae and the
CC release of cytochrome c during apoptosis (PubMed:16839884,
CC PubMed:16839885). Proteolytic processing in response to intrinsic
CC apoptotic signals may lead to disassembly of OPA1 oligomers and release
CC of the caspase activator cytochrome C (CYCS) into the mitochondrial
CC intermembrane space (PubMed:16839884, PubMed:16839885). Plays a role in
CC mitochondrial genome maintenance (By similarity).
CC {ECO:0000250|UniProtKB:O60313, ECO:0000269|PubMed:11847212,
CC ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:16839885,
CC ECO:0000269|PubMed:24616225, ECO:0000269|PubMed:26785494,
CC ECO:0000269|PubMed:28746876}.
CC -!- FUNCTION: [Dynamin-like 120 kDa protein, form S1]: Produced by cleavage
CC at position S1 by OMA1 following stress conditions that induce loss of
CC mitochondrial membrane potential, leading to negative regulation of
CC mitochondrial fusion. {ECO:0000269|PubMed:20038678,
CC ECO:0000269|PubMed:22433842}.
CC -!- FUNCTION: Isoforms that contain the alternative exon 4b (present in
CC isoform 2, but not in isoform 1) are required for mitochondrial genome
CC maintenance, possibly by anchoring the mitochondrial nucleoids to the
CC inner mitochondrial membrane. {ECO:0000250|UniProtKB:O60313}.
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:0000250|UniProtKB:O60313};
CC -!- ACTIVITY REGULATION: Activated by guanine nucleotide exchange factor
CC RCC1L. {ECO:0000250|UniProtKB:O60313}.
CC -!- SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble
CC forms of OPA1 (PubMed:16839885). Interacts with CHCHD3 and IMMT; these
CC interactions occur preferentially with soluble OPA1 forms
CC (PubMed:21081504). Interacts with RCC1L; this interaction is direct
CC (PubMed:28746876). Binds PARL (PubMed:16839884). Interacts with PRELID1
CC (By similarity). {ECO:0000250|UniProtKB:O60313,
CC ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:16839885,
CC ECO:0000269|PubMed:21081504, ECO:0000269|PubMed:28746876}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16839884, ECO:0000269|PubMed:21081504,
CC ECO:0000269|PubMed:28746876}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:11847212}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:O60313}. Note=Detected at
CC contact sites between endoplasmic reticulum and mitochondrion
CC membranes. {ECO:0000250|UniProtKB:O60313}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P58281-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58281-2; Sequence=VSP_021037;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:11847212). Detected in brain, brain stem, heart, kidney, liver
CC and skeletal muscle (PubMed:11847212). {ECO:0000269|PubMed:11847212}.
CC -!- PTM: PARL-dependent proteolytic processing releases an antiapoptotic
CC soluble form not required for mitochondrial fusion (PubMed:20038678,
CC PubMed:24550258, PubMed:22433842). Cleaved by OMA1 at position S1
CC following stress conditions (PubMed:20038678, PubMed:24550258,
CC PubMed:22433842). {ECO:0000269|PubMed:20038678,
CC ECO:0000269|PubMed:22433842, ECO:0000269|PubMed:24550258}.
CC -!- PTM: [Isoform 2]: Cleavage at position S2 is mediated by YME1L
CC (PubMed:24616225, PubMed:26785494). Cleavage may occur in the sequence
CC motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ) (By similarity).
CC {ECO:0000250|UniProtKB:Q2TA68, ECO:0000269|PubMed:24616225,
CC ECO:0000269|PubMed:26785494}.
CC -!- MISCELLANEOUS: Embryonic fibroblasts that lack Opa1 show a defect in
CC apoptosis in response to intrinsic signals. This defect can be
CC complemented by a soluble form of Opa1 targeted to the mitochondrial
CC intermembrane space. {ECO:0000269|PubMed:16839884}.
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=AAH25160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB044138; BAB59000.1; -; mRNA.
DR EMBL; AK029157; BAC26331.1; -; mRNA.
DR EMBL; AK038446; BAC30002.1; -; mRNA.
DR EMBL; AK044657; BAC32021.1; -; mRNA.
DR EMBL; AK050383; BAC34224.1; -; mRNA.
DR EMBL; AK145620; BAE26544.1; -; mRNA.
DR EMBL; BC025160; AAH25160.1; ALT_INIT; mRNA.
DR EMBL; BC138665; AAI38666.1; -; mRNA.
DR EMBL; BC145959; AAI45960.1; -; mRNA.
DR CCDS; CCDS28096.1; -. [P58281-1]
DR RefSeq; NP_598513.1; NM_133752.3. [P58281-1]
DR RefSeq; XP_006522720.1; XM_006522657.2.
DR AlphaFoldDB; P58281; -.
DR SMR; P58281; -.
DR BioGRID; 216522; 11.
DR IntAct; P58281; 17.
DR MINT; P58281; -.
DR STRING; 10090.ENSMUSP00000124223; -.
DR iPTMnet; P58281; -.
DR PhosphoSitePlus; P58281; -.
DR SwissPalm; P58281; -.
DR EPD; P58281; -.
DR jPOST; P58281; -.
DR MaxQB; P58281; -.
DR PaxDb; P58281; -.
DR PeptideAtlas; P58281; -.
DR PRIDE; P58281; -.
DR ProteomicsDB; 294077; -. [P58281-1]
DR ProteomicsDB; 294078; -. [P58281-2]
DR Antibodypedia; 33885; 316 antibodies from 32 providers.
DR Ensembl; ENSMUST00000160597; ENSMUSP00000124223; ENSMUSG00000038084. [P58281-1]
DR Ensembl; ENSMUST00000161186; ENSMUSP00000123880; ENSMUSG00000038084. [P58281-2]
DR GeneID; 74143; -.
DR KEGG; mmu:74143; -.
DR UCSC; uc007ywf.2; mouse. [P58281-1]
DR CTD; 4976; -.
DR MGI; MGI:1921393; Opa1.
DR VEuPathDB; HostDB:ENSMUSG00000038084; -.
DR eggNOG; KOG0447; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR HOGENOM; CLU_012302_0_0_1; -.
DR InParanoid; P58281; -.
DR OMA; IRKQWKL; -.
DR OrthoDB; 609213at2759; -.
DR PhylomeDB; P58281; -.
DR TreeFam; TF314250; -.
DR BRENDA; 3.6.5.5; 3474.
DR Reactome; R-MMU-169911; Regulation of Apoptosis.
DR BioGRID-ORCS; 74143; 16 hits in 73 CRISPR screens.
DR ChiTaRS; Opa1; mouse.
DR PRO; PR:P58281; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P58281; protein.
DR Bgee; ENSMUSG00000038084; Expressed in dorsal striatum and 241 other tissues.
DR ExpressionAtlas; P58281; baseline and differential.
DR Genevisible; P58281; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0036444; P:calcium import into the mitochondrion; ISO:MGI.
DR GO; GO:0090398; P:cellular senescence; ISO:MGI.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR GO; GO:0097749; P:membrane tubulation; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:CACAO.
DR GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:1900006; P:positive regulation of dendrite development; ISO:MGI.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; ISO:MGI.
DR GO; GO:0014042; P:positive regulation of neuron maturation; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0007601; P:visual perception; ISS: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 Acetylation; Alternative splicing; Apoptosis; Coiled coil; GTP-binding;
KW Hydrolase; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Sensory transduction; Transit peptide; Transmembrane; Transmembrane helix;
KW 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_0000007398"
FT CHAIN 195..960
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000253480"
FT TOPO_DOM 88..96
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..960
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
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:0000250|UniProtKB:O60313"
FT VAR_SEQ 208
FT /note="K -> KGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021037"
FT CONFLICT 236
FT /note="L -> P (in Ref. 2; BAC30002)"
FT /evidence="ECO:0000305"
FT CONFLICT 330..331
FT /note="TL -> NN (in Ref. 2; BAC32021)"
FT /evidence="ECO:0000305"
FT MOTIF P58281-2:217..222
FT /note="LQQQIQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
SQ SEQUENCE 960 AA; 111339 MW; 0F103FB1FD570F49 CRC64;
MWRAGRAAVA CEVCQSLVKH SSGIQRNVPL QKLHLVSRSI YRSHHPALKL QRPQLRTPFQ
QFSSLTHLSL HKLKLSPIKY GYQPRRNFWP ARLAARLLKL RYIILGSAVG GGYTAKKTFD
EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE KIRKALPSSE DLASLAPDLD KITESLSLLK
DFFTAGSPGE TAFRATDHGS ESDKHYRKVS 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 ALQGRLKDTE NAIENMIGPD WKKRWMYWKN
RTQEQCVHNE TKNELEKMLK VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV
YRRHFLKTAL NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK
