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

 OPA1_RAT                Reviewed;         960 AA.
Q2TA68; O08681; Q5MPP1; Q5MPP2; Q5QJE9; Q6B435; Q6R611;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 1.
05-DEC-2018, entry version 106.
RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
EC=3.6.5.5;
AltName: Full=Optic atrophy protein 1 homolog;
Contains:
RecName: Full=Dynamin-like 120 kDa protein, form S1;
Flags: Precursor;
Name=Opa1 {ECO:0000312|EMBL:AAI11072.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:AAR04100.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
SPECIFICITY.
TISSUE=Retinal ganglion {ECO:0000269|PubMed:15505078};
PubMed=15505078; DOI=10.1167/iovs.03-1261;
Pesch U.E.A., Fries J.E., Bette S., Kalbacher H., Wissinger B.,
Alexander C., Kohler K.;
"OPA1, the disease gene for autosomal dominant optic atrophy, is
specifically expressed in ganglion cells and intrinsic neurons of the
retina.";
Invest. Ophthalmol. Vis. Sci. 45:4217-4225(2004).
[2] {ECO:0000312|EMBL:AAS79791.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain {ECO:0000312|EMBL:AAS79791.1};
PubMed=16249510; DOI=10.1167/iovs.03-1407;
Kamei S., Chen-Kuo-Chang M., Cazevieille C., Lenaers G., Olichon A.,
Belenguer P., Roussignol G., Renard N., Eybalin M., Michelin A.,
Delettre C., Brabet P., Hamel C.P.;
"Expression of the Opa1 mitochondrial protein in retinal ganglion
cells: its downregulation causes aggregation of the mitochondrial
network.";
Invest. Ophthalmol. Vis. Sci. 46:4288-4294(2005).
[3] {ECO:0000312|EMBL:AAI11072.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver {ECO:0000312|EMBL:AAI11072.1};
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).
[4] {ECO:0000305, ECO:0000312|EMBL:AAT92526.1}
PROTEIN SEQUENCE OF 302-312; 416-423; 446-460; 801-818 AND 825-834,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Diao W.;
Submitted (APR-2007) to UniProtKB.
[5] {ECO:0000305, ECO:0000312|EMBL:AAB51724.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 556-960.
STRAIN=R21 {ECO:0000312|EMBL:AAB51724.1};
TISSUE=Spleen {ECO:0000312|EMBL:AAB51724.1};
Yuan X.J., Salgar S.K., Kunz H.W., Gill T.J. III;
"A novel gene in the rat genome.";
Rat Genome 2:150-153(1996).
[6] {ECO:0000305, ECO:0000312|EMBL:AAT92526.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 686-788.
STRAIN=OFA {ECO:0000312|EMBL:AAT92526.1}; TISSUE=Intestine;
Fabregas P.J., Nebot-Cegarra J., Capella G., Peinado M.A.;
"Differential gene expression in gut during rat fetal period.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305}
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBCELLULAR LOCATION.
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).
-!- FUNCTION: Dynamin-related GTPase that is essential for normal
mitochondrial morphology by regulating the equilibrium between
mitochondrial fusion and mitochondrial fission (PubMed:16778770).
Coexpression of isoform 1 with shorter alternative products is
required for optimal activity in promoting mitochondrial fusion.
Binds lipid membranes enriched in negatively charged
phospholipids, such as cardiolipin, and promotes membrane
tubulation. The intrinsic GTPase activity is low, and is strongly
increased by interaction with lipid membranes (By similarity).
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 (By similarity).
{ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281,
ECO:0000269|PubMed:16778770}.
-!- 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:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
-!- FUNCTION: Isoforms that contain the alternative exon 4b (present
in isoform 2 and isoform 3, but not in isoform 1) are required for
mitochondrial genome maintenance, possibly by anchoring the
mitochondrial nucleoids to the inner mitochondrial membrane.
{ECO:0000250|UniProtKB:O60313}.
-!- CATALYTIC ACTIVITY:
Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
Evidence={ECO:0000250|UniProtKB:O60313};
-!- ACTIVITY REGULATION: Activated by guanine nucleotide exchange
factor RCC1L. {ECO:0000250|UniProtKB:O60313}.
-!- 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.
Interacts with RCC1L; this interaction is direct (By similarity).
Binds PARL (By similarity). Interacts with PRELID1 (By
similarity). {ECO:0000250|UniProtKB:O60313,
ECO:0000250|UniProtKB:P58281}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:16778770}; Single-pass membrane protein
{ECO:0000255}. Mitochondrion intermembrane space
{ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane
{ECO:0000250|UniProtKB:O60313}. Note=Detected at contact sites
between endoplamic reticulum and mitochondrion membranes.
{ECO:0000250|UniProtKB:O60313}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms may exist. {ECO:0000305};
Name=1 {ECO:0000303|PubMed:15505078};
IsoId=Q2TA68-1; Sequence=Displayed;
Name=2 {ECO:0000303|PubMed:15505078};
IsoId=Q2TA68-2; Sequence=VSP_052186, VSP_052187;
Name=3 {ECO:0000303|PubMed:15505078}; Synonyms=7
{ECO:0000303|PubMed:16778770};
IsoId=Q2TA68-3; Sequence=VSP_052187;
-!- TISSUE SPECIFICITY: Expressed in brain as well as retinal
ganglion, starbust amacrine and horizontal cells of the retina.
Absent from nerve fibers and photoreceptor cells of the retina.
{ECO:0000269|PubMed:15505078}.
-!- 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:0000250|UniProtKB:O60313}.
-!- PTM: Cleavage at position S2 is mediated by YME1L. Cleavage may
occur in the sequence motif Leu-Gln-Gln-Gln-Ile-Gln (LQQQIQ). This
motif is present in isoform 2 and isoform 3, but is absent in the
displayed isoform 1. {ECO:0000305|PubMed:16778770}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
-!- SEQUENCE CAUTION:
Sequence=AAB51724.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY333988; AAR04100.1; -; mRNA.
EMBL; AY660011; AAV97815.1; -; mRNA.
EMBL; AY660012; AAV97816.1; -; mRNA.
EMBL; AY510274; AAS79791.1; -; mRNA.
EMBL; BC111071; AAI11072.1; -; mRNA.
EMBL; U93197; AAB51724.1; ALT_INIT; mRNA.
EMBL; AY683458; AAT92526.1; -; mRNA.
RefSeq; NP_598269.3; NM_133585.3. [Q2TA68-1]
RefSeq; XP_006248560.1; XM_006248498.1. [Q2TA68-3]
UniGene; Rn.225901; -.
UniGene; Rn.9783; -.
ProteinModelPortal; Q2TA68; -.
BioGrid; 251124; 1.
IntAct; Q2TA68; 2.
MINT; Q2TA68; -.
iPTMnet; Q2TA68; -.
PhosphoSitePlus; Q2TA68; -.
SwissPalm; Q2TA68; -.
PRIDE; Q2TA68; -.
Ensembl; ENSRNOT00000002338; ENSRNOP00000002338; ENSRNOG00000001717. [Q2TA68-1]
Ensembl; ENSRNOT00000002343; ENSRNOP00000002343; ENSRNOG00000001717. [Q2TA68-1]
GeneID; 171116; -.
KEGG; rno:171116; -.
UCSC; RGD:708423; rat. [Q2TA68-1]
CTD; 4976; -.
RGD; 708423; Opa1.
GeneTree; ENSGT00550000074851; -.
HOVERGEN; HBG019108; -.
InParanoid; Q2TA68; -.
KO; K17079; -.
OMA; YEDWKDG; -.
OrthoDB; EOG091G01NV; -.
Reactome; R-RNO-169911; Regulation of Apoptosis.
PMAP-CutDB; Q2TA68; -.
PRO; PR:Q2TA68; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001717; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
Genevisible; Q2TA68; RN.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0030061; C:mitochondrial crista; ISS:ParkinsonsUK-UCL.
GO; GO:0005758; C:mitochondrial intermembrane space; ISS:ParkinsonsUK-UCL.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0036444; P:calcium import into the mitochondrion; IMP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD.
GO; GO:0090398; P:cellular senescence; ISS:ParkinsonsUK-UCL.
GO; GO:0090102; P:cochlea development; IEP:RGD.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:ParkinsonsUK-UCL.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0097749; P:membrane tubulation; ISS:UniProtKB.
GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
GO; GO:0008053; P:mitochondrial fusion; ISS:ParkinsonsUK-UCL.
GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IMP:RGD.
GO; GO:0007005; P:mitochondrion organization; IDA:RGD.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:ParkinsonsUK-UCL.
GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IMP:RGD.
GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:RGD.
GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:RGD.
GO; GO:0014042; P:positive regulation of neuron maturation; IMP:RGD.
GO; GO:0051259; P:protein complex oligomerization; IDA:RGD.
GO; GO:1904643; P:response to curcumin; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0014850; P:response to muscle activity; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
GO; GO:0007601; P:visual perception; ISS:ParkinsonsUK-UCL.
CDD; cd08771; DLP_1; 1.
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; Coiled coil;
Complete proteome; Direct protein sequencing; GTP-binding; Hydrolase;
Lipid-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Reference proteome; Sensory transduction;
Transit peptide; Transmembrane; Transmembrane helix.
TRANSIT 1 87 Mitochondrion.
{ECO:0000269|PubMed:16778770}.
CHAIN 88 960 Dynamin-like 120 kDa protein,
mitochondrial.
/FTId=PRO_0000257994.
CHAIN 195 960 Dynamin-like 120 kDa protein, form S1.
{ECO:0000269|PubMed:16778770,
ECO:0000305|PubMed:16778770}.
/FTId=PRO_0000257995.
TOPO_DOM 88 96 Mitochondrial matrix.
{ECO:0000269|PubMed:16778770}.
TRANSMEM 97 113 Helical. {ECO:0000255}.
TOPO_DOM 114 960 Mitochondrial intermembrane.
{ECO:0000269|PubMed:16778770}.
DOMAIN 285 561 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
NP_BIND 295 302 GTP. {ECO:0000255}.
NP_BIND 398 402 GTP. {ECO:0000255}.
NP_BIND 467 470 GTP. {ECO:0000255}.
REGION 295 302 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 321 324 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 398 401 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 467 470 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 501 504 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
COILED 210 254 {ECO:0000255}.
COILED 895 960 {ECO:0000255}.
SITE 194 195 Cleavage at site S1.
{ECO:0000269|PubMed:16778770}.
MOD_RES 228 228 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60313}.
VAR_SEQ 158 158 S -> PKLVSEVIEASEPLLLLS (in isoform 2).
{ECO:0000303|PubMed:15505078}.
/FTId=VSP_052186.
VAR_SEQ 209 209 V -> GLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKR
KV (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15505078}.
/FTId=VSP_052187.
CONFLICT 187 187 T -> S (in Ref. 1; AAR04100).
{ECO:0000305}.
CONFLICT 316 316 R -> P (in Ref. 2; AAS79791).
{ECO:0000305}.
CONFLICT 687 687 E -> G (in Ref. 6; AAT92526).
{ECO:0000305}.
CONFLICT 692 692 E -> G (in Ref. 6; AAT92526).
{ECO:0000305}.
CONFLICT 730 730 L -> P (in Ref. 6; AAT92526).
{ECO:0000305}.
SEQUENCE 960 AA; 111307 MW; 0C4BE54FCD7A53B3 CRC64;
MWRAGRAALA CEVCQSLVKH SSGVQRNVPL QKLHLVSRSI YRSHHPALKL QRPQLRTSFQ
QFSSLTNLSL HKLKLSPTKY GYQPRRNFWP ARLAARLLKL RYIILGSAVG GGYTAKKTFD
EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE KIRKALPSSE DLANFAPDLD KIAESLSLLK
DFFTAGTPGE 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 EVAWETLQDE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED
SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQGRLKDTE NAIENMIGPD WKKRWIYWKN
RTQEQCVHNE TKNELEKMLK VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV
YRRHFLKTAL NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK


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