OPA1_DANRE
ID OPA1_DANRE Reviewed; 966 AA.
AC Q5U3A7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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:0000312|EMBL:AAH85633.1}; ORFNames=zgc:92092;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAH85633.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
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).
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 -!- 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 -!- SUBUNIT: Oligomeric complex consisting of membrane-bound and soluble
CC forms of OPA1. Binds PARL (By similarity).
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: Proteolytic processing produces an antiapoptotic soluble form
CC Cleaved by oma1 at position S1 following stress conditions.
CC {ECO:0000250}.
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; BC085633; AAH85633.1; -; mRNA.
DR RefSeq; NP_001007299.1; NM_001007298.1.
DR AlphaFoldDB; Q5U3A7; -.
DR SMR; Q5U3A7; -.
DR STRING; 7955.ENSDARP00000065102; -.
DR PaxDb; Q5U3A7; -.
DR PRIDE; Q5U3A7; -.
DR Ensembl; ENSDART00000104256; ENSDARP00000095031; ENSDARG00000070801.
DR GeneID; 492332; -.
DR KEGG; dre:492332; -.
DR CTD; 4976; -.
DR ZFIN; ZDB-GENE-041114-7; opa1.
DR eggNOG; KOG0447; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR HOGENOM; CLU_012302_0_0_1; -.
DR InParanoid; Q5U3A7; -.
DR OMA; XIQQIIE; -.
DR PhylomeDB; Q5U3A7; -.
DR TreeFam; TF314250; -.
DR PRO; PR:Q5U3A7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000070801; Expressed in muscle tissue and 28 other tissues.
DR ExpressionAtlas; Q5U3A7; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
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:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
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:0070584; P:mitochondrion morphogenesis; IMP:ZFIN.
DR GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:ZFIN.
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 Apoptosis; Coiled coil; GTP-binding; Hydrolase; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT CHAIN 87..966
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /id="PRO_0000257997"
FT CHAIN 194..966
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000417514"
FT TOPO_DOM 87..95
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..966
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 291..567
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 189..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..308
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 327..330
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 404..407
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 473..476
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 507..510
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 213..259
FT /evidence="ECO:0000255"
FT COILED 901..966
FT /evidence="ECO:0000255"
FT BINDING 301..308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 404..408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 473..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 193..194
FT /note="Cleavage at site S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
SQ SEQUENCE 966 AA; 111333 MW; 53B7AA4BDB7B39EC CRC64;
MLRAGSVVTC IACKGLLPSR MGVKFRVPLQ KLHPLSRAIH HRYSANNNPQ RPPHCSAARH
YTSLSRLPMR PPKSRSGGHG YQQHRTFWVA RLAARLLKLR YILLGSAVGG GYTAKKTYDE
WKEMLPDMSE YTWIVPDFVW ELSENIDLDK LASALPELEE IAKLLPDMEK IGENFTFLKS
LLSSETTGES ALRAPDVPPA SAAMADSGDK QFKKSSDKEK VDQLQEELLR TQLKYQRMLE
RLEKENKELR KVVLQKDDKG IHQRKVKKSL IDMYSEVLDI LSDYDSNYNT QDHLPRVVVV
GDQSAGKTSV LEMIAQARIF PRGSGEMMTR SPVKVTLSEG PHHVAMFKDS SREFDLGKEE
DLAALRHEIE LRMRKSVKEG QTVSPETISL SVKGPGIQRM VLVDLPGVIS TVTTGMAADT
KETIFSISKA YMQNPNAIIL CIQDGSVDAE RSIVTDLVSQ MDPQGKRTIF VLTKVDLAEK
NLASPSRIQQ IVEGKLFPMK ALGYFAVVTG KGSPNESIDS IKDYEEDFFQ NSRLLKDGML
KAHQVTTKNL SLAVSDCFWK MVRESVEQQA DAFKASRFNL ETEWKNNYPR LRELDRNELY
EKAKNEILDE VISLSQVTPK HWESILQKKL WERVSTHVIE NIYLPAAQTM NSGTFNTTVD
IKLKQWTDKQ LPHKALEVAW ETLQEEFARF MAEYKGKDQD DIFDKLKEAV KDESIKRHKW
NERAMDSLRV IQHNALEDRS ITDKPQWDAA IQFMEETLQS RLKDTESVIA DMVGPDWKQR
WMSWKNRTPE QHTRNETKNE LERLLKLHED HTAYLANDEV TTVRKNLEAR GVEVDPVLIK
DTWHQLFRRH FLQKALLHCN LCRRGFYYYQ RHFVDSELEC NDVVLFWRIQ RMLGITANTL
RQQLTNTEVR RLEKNVKEVL EDFGEDNEKK VQLITGRRVQ LAEDLKKVRE IQEKLEAFIE
ALHKEK
