OPA1_ONCMA
ID OPA1_ONCMA Reviewed; 971 AA.
AC O93248;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE EC=3.6.5.5;
DE AltName: Full=120 kDa G protein expressed in motor neurons;
DE AltName: Full=Optic atrophy protein 1 homolog;
DE AltName: Full=mG120;
DE Contains:
DE RecName: Full=Dynamin-like 120 kDa protein, form S1;
DE Flags: Precursor;
GN Name=opa1;
OS Oncorhynchus masou (Cherry salmon) (Masu salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8020;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9708909; DOI=10.1016/s0014-5793(98)00762-5;
RA Kubokawa K., Miyashita T., Kubo Y.;
RT "Isolation of a cDNA for a novel 120-kDa GTP-binding protein expressed in
RT motor neurons in the salmon brain.";
RL FEBS Lett. 431:231-235(1998).
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). {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Strongly expressed in the brain, ovary and skeletal
CC muscle. In the brain, expression of the mRNA was observed specifically
CC in motor neurons, in nucleus oculomotorius, in nucleus valvulae
CC lateralis, in the medulla oblongata and in the spinal cord.
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; AB012720; BAA32279.1; -; mRNA.
DR PIR; T00394; T00394.
DR AlphaFoldDB; O93248; -.
DR SMR; O93248; -.
DR PRIDE; O93248; -.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030061; C:mitochondrial crista; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
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; IDA: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:0007007; P:inner mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0097749; P:membrane tubulation; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; GTP-binding; Hydrolase; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..89
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT CHAIN 90..971
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /id="PRO_0000007399"
FT CHAIN 201..971
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000417515"
FT TOPO_DOM 90..98
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..971
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 297..572
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 204..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..314
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 333..336
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 410..413
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 478..481
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 512..515
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 219..265
FT /evidence="ECO:0000255"
FT COILED 906..971
FT /evidence="ECO:0000255"
FT BINDING 307..314
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 410..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 478..481
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 200..201
FT /note="Cleavage at site S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
SQ SEQUENCE 971 AA; 112070 MW; 462958C03C1A4F02 CRC64;
MLRVGRAVAC VACNNLASKN MGVRFRMPLQ KLHPLSRAIH HRYNASANAQ RPPHCSAARH
FTSMSRLPMR PPKPSPGGHG GWRYQQHRSF WMLRLASRLL KLRYIVLGSA VGGGYTAKKT
YEEWKDMLPD MSAYNWVIPD FVWELSDQID LDKLTKILPE LEEIAKLLPE LPDFDKIGEN
FTFLKSILFT AEAPGDTPVK AATEAPVTAT PEASDKQFKK SSDKEKVDQL QEELLRTQMK
YQRMLERLEK ENKDLRKVVL QKDEKGIHQR KIKKSLIDMY SEVLDILSDF DSNYNTQDHL
PRVVVVGDQS AGKTSVLEMI AQARIFPRGS GEMMTRSPVK VTLSEGPHHV AMFKDSSREF
DLGKEEDLAA LRHEIELRMR KSVKEGQTVS PETISLSVKG PGIQRMVLVD LPGVISTVTA
GMAADTKETI FSISKNYMQN PNAIILCIQD GSVDAEADRH RPGQSNGPAG ERTIFVLTKV
DLAEKNLASP NRIQQIVEGK LFPMKALGYF AVVTGKGSAG ESIDSIKDYE EDFFQNSRLL
RDGMLKAHQV TTKNLSLAVS DCFWKMVRES VEQQADAFKA SRFNLETEWK NNYPRLRELD
RNELFEKAKN EILDEVISLS QVTPKHWEAI LQKKLWERVS THVIENIYLP AAQTMNSGTF
NTTVDIKLKQ WTDKQLPHKA LEVAWETLQE EFARFMAEYK GKDQDDIFDK LKEAVKDESI
KRHKWNERAM DSLRVIQHNA LEDRSITDKP QWDAAIQFME ETLQARLKDT DSVINDMVGP
DWKQRWMSWK NRSPEQHTRN ETRNELERLL KLHEDHTAYL ANDEVTTVRK NLEGRGVEVD
PALIKDTWHQ LYRRHFLQKA LQHCNLCRRG FYYYQRHFVD SELECNDVVL FWRIQRMLLI
TANTLRQQLT NTEVRRLEKN VKEVLEDFGE DNERKVHLIT GRRVQLAEDL KKVREIQEKL
EAFIEALHKE K
