OPA1_PONAB
ID OPA1_PONAB Reviewed; 960 AA.
AC Q5RAM3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE EC=3.6.5.5;
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:0000250|UniProtKB:O60313};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH91187.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dynamin-related GTPase that is essential for normal
CC mitochondrial morphology by regulating the equilibrium between
CC mitochondrial fusion and mitochondrial fission. Binds lipid membranes
CC enriched in negatively charged phospholipids, such as cardiolipin, and
CC promotes membrane tubulation. The intrinsic GTPase activity is low, and
CC is strongly increased by interaction with lipid membranes (By
CC similarity). Plays a role in remodeling cristae and the release of
CC cytochrome c during apoptosis (By similarity). Proteolytic processing
CC in response to intrinsic apoptotic signals may lead to disassembly of
CC OPA1 oligomers and release of the caspase activator cytochrome C (CYCS)
CC into the mitochondrial intermembrane space (By similarity). Plays a
CC role in mitochondrial genome maintenance (By similarity).
CC {ECO:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
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:0000250|UniProtKB:O60313, ECO:0000250|UniProtKB:P58281}.
CC -!- FUNCTION: Dynamin-like 120 kDa protein, form S2: Produced by cleavage
CC at position S2 by YME1L. Promotes mitochondrial fusion.
CC {ECO:0000250|UniProtKB:P58281}.
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. Interacts with CHCHD3 and IMMT; these interactions occur
CC preferentially with soluble OPA1 forms. Interacts with RCC1L; this
CC interaction is direct (By similarity). Binds PARL (By similarity).
CC Interacts with PRELID1 (By similarity). {ECO:0000250|UniProtKB:O60313,
CC ECO:0000250|UniProtKB:P58281}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O60313}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:P58281}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:O60313}. Note=Detected at contact sites between
CC endoplasmic reticulum and mitochondrion membranes.
CC {ECO:0000250|UniProtKB:O60313}.
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.
CC {ECO:0000250|UniProtKB:O60313}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; CR858992; CAH91187.1; -; mRNA.
DR RefSeq; NP_001125695.1; NM_001132223.1.
DR AlphaFoldDB; Q5RAM3; -.
DR SMR; Q5RAM3; -.
DR STRING; 9601.ENSPPYP00000016126; -.
DR PRIDE; Q5RAM3; -.
DR GeneID; 100172619; -.
DR KEGG; pon:100172619; -.
DR CTD; 4976; -.
DR eggNOG; KOG0447; Eukaryota.
DR InParanoid; Q5RAM3; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
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:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0097749; P:membrane tubulation; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0000002; P:mitochondrial genome maintenance; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Coiled coil; GTP-binding; Hydrolase; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Sensory transduction; Transit peptide; Transmembrane;
KW Transmembrane helix.
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_0000257992"
FT CHAIN 195..960
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000257993"
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"
SQ SEQUENCE 960 AA; 111492 MW; F876194A73F01F8D CRC64;
MWRLRRAAVA CEVCQSLVKH SSGIKGSLPL QKLHLVSRSI YHSHYPTLKL QRPQLRTSFQ
QFSSLTNLPL RKLKFSPIKY GYQPRRNFWP ARLATRLLKL RYLILGSAVG GGYTAKKTFD
QWKDMIPDLS EYKWIVPDIV WEIDEYIDFE KIRKALPNSE DLVKLAPDFD KIVESLSLLK
DFFTSGSPGE TAFRATDHGS 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 ATPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW
TDKQLPNKAV EVAWETLQGE 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
