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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_DANRE              Reviewed;         966 AA.
Q5U3A7;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 1.
20-DEC-2017, entry version 109.
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:AAH85633.1}; ORFNames=zgc:92092;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1] {ECO:0000312|EMBL:AAH85633.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Dynamin-related GTPase that is essential for normal
mitochondrial morphology by regulating the equilibrium between
mitochondrial fusion and mitochondrial fission. 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). {ECO:0000250|UniProtKB:O60313,
ECO:0000250|UniProtKB:P58281}.
-!- 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}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
{ECO:0000250|UniProtKB:O60313}.
-!- SUBUNIT: Oligomeric complex consisting of membrane-bound and
soluble forms of OPA1. Binds PARL (By similarity).
{ECO:0000250|UniProtKB:P58281}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:O60313}; 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}.
-!- PTM: Proteolytic processing produces an antiapoptotic soluble form
Cleaved by oma1 at position S1 following stress conditions.
{ECO:0000250}.
-!- 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}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
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EMBL; BC085633; AAH85633.1; -; mRNA.
RefSeq; NP_001007299.1; NM_001007298.1.
UniGene; Dr.37656; -.
ProteinModelPortal; Q5U3A7; -.
SMR; Q5U3A7; -.
STRING; 7955.ENSDARP00000095031; -.
PaxDb; Q5U3A7; -.
PRIDE; Q5U3A7; -.
Ensembl; ENSDART00000104256; ENSDARP00000095031; ENSDARG00000070801.
GeneID; 492332; -.
KEGG; dre:492332; -.
CTD; 4976; -.
ZFIN; ZDB-GENE-041114-7; opa1.
eggNOG; KOG0447; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00550000074851; -.
HOGENOM; HOG000230714; -.
HOVERGEN; HBG019108; -.
InParanoid; Q5U3A7; -.
KO; K17079; -.
PhylomeDB; Q5U3A7; -.
TreeFam; TF314250; -.
Reactome; R-DRE-169911; Regulation of Apoptosis.
PRO; PR:Q5U3A7; -.
Proteomes; UP000000437; Chromosome 6.
Bgee; ENSDARG00000070801; -.
ExpressionAtlas; Q5U3A7; baseline.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
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:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
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: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:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IMP:ZFIN.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:ZFIN.
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.
2: Evidence at transcript level;
Apoptosis; Coiled coil; Complete proteome; GTP-binding; Hydrolase;
Lipid-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Reference proteome; Transit peptide;
Transmembrane; Transmembrane helix.
TRANSIT 1 86 Mitochondrion.
{ECO:0000250|UniProtKB:Q2TA68}.
CHAIN 87 966 Dynamin-like 120 kDa protein,
mitochondrial.
/FTId=PRO_0000257997.
CHAIN 194 966 Dynamin-like 120 kDa protein, form S1.
{ECO:0000250|UniProtKB:Q2TA68}.
/FTId=PRO_0000417514.
TOPO_DOM 87 95 Mitochondrial matrix. {ECO:0000255}.
TRANSMEM 96 112 Helical. {ECO:0000255}.
TOPO_DOM 113 966 Mitochondrial intermembrane.
{ECO:0000255}.
DOMAIN 291 567 Dynamin-type G.
NP_BIND 301 308 GTP. {ECO:0000255}.
NP_BIND 404 408 GTP. {ECO:0000255}.
NP_BIND 473 476 GTP. {ECO:0000255}.
COILED 213 259 {ECO:0000255}.
COILED 901 966 {ECO:0000255}.
SITE 193 194 Cleavage at site S1.
{ECO:0000250|UniProtKB:Q2TA68}.
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


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