OPA1_CHICK
ID OPA1_CHICK Reviewed; 977 AA.
AC Q5F499;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; ORFNames=RCJMB04_1m16;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAH65035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAH65035.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAH65035.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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: 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; AJ851401; CAH65035.1; -; mRNA.
DR RefSeq; NP_001034398.1; NM_001039309.1.
DR AlphaFoldDB; Q5F499; -.
DR SMR; Q5F499; -.
DR STRING; 9031.ENSGALP00000042204; -.
DR PaxDb; Q5F499; -.
DR PRIDE; Q5F499; -.
DR GeneID; 424900; -.
DR KEGG; gga:424900; -.
DR CTD; 4976; -.
DR VEuPathDB; HostDB:geneid_424900; -.
DR eggNOG; KOG0447; Eukaryota.
DR InParanoid; Q5F499; -.
DR PhylomeDB; Q5F499; -.
DR PRO; PR:Q5F499; -.
DR Proteomes; UP000000539; Unplaced.
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: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 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..977
FT /note="Dynamin-like 120 kDa protein, mitochondrial"
FT /id="PRO_0000257996"
FT CHAIN 212..977
FT /note="Dynamin-like 120 kDa protein, form S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
FT /id="PRO_0000417513"
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..977
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 302..578
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 312..319
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 338..341
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 415..418
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 484..487
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 518..521
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 224..271
FT /evidence="ECO:0000255"
FT COILED 911..977
FT /evidence="ECO:0000255"
FT BINDING 312..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 415..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 484..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT SITE 211..212
FT /note="Cleavage at site S1"
FT /evidence="ECO:0000250|UniProtKB:Q2TA68"
SQ SEQUENCE 977 AA; 113446 MW; 3A6395145F76C996 CRC64;
MWRTKAAAAC VICRSLAHSN YGIKRKSPLQ NLHLVSRSIH HPYHPSLKFQ RRPLRISLQQ
FSSLNRLPLR KTKLLNVKYG YQSYRNFWLA RLASRLLKIR YLILGSAVGG GYTAKKTYDQ
WEDMMPDLDE YKWIIPDFIW ELDEHIDLEK LIKALPDADD LAKLLPDFEK IGESFTSLKG
IFSPGYNLVS EVIGASDLLL LLGTPGETAF RATDQGYDSD KQYKKVSDKE KIDQLQEELL
RTQLKYQRML ERLEKENKEL RKLVLQRDDK GIHQRKLKKS LIDMYSEVLD ILSDYDASYN
TQDHLPRVVV VGDQSAGKTS VLEMIAQARI FPRGSGEMMT RSPVKVTLSE GPHHVALFKD
SSREFDLTKE EDLAALRNEI EIRMRNSVKE GCTVSTETIS LSVRGPGLQR MVLVDLPGVI
STVTSGMAPD TKETIFSISK AYMQNPNAII LCIQDGSVDA ERSIVTDLVS QMDPQGKRTI
FVLTKVDLAE KNVASPSRIQ QIIEGKLFPM KALGYFAVVT GKGNSSESIE SIKEYEEEFF
QNSKLLKTSM LKAHQVTTKN LSLAVSDCFW KMVRESVEQQ ADAFKATRFN LETEWKNNYP
RLRELDRNEL FEKAKNEILD EVISLTQVTP KHWEEILQKT LWERVSTHVI ENIYLPAAQT
MNSGTFNTTV DIKLKQWTDK QLPNKAVEVA WETLQEEFSR FMTEQKGKEH DDIFDKLKQA
VKEESIKRHK WNERAEDSLR VIQHNALEDR SISDKQQWDA AIHFMEETLQ SRLKDTESVI
EDMVGPDWKK RWLYWISRTK EQNIRNETKN ELEKLIKCNE EHAAYLANDE VTTVRKNLEA
RGITVDPCLI KDTWHQIYRR YFLKTALNHC NLCRRGFYYY QRHFVDSELE CNDIVLFWRI
QRMLAITANT LRQQLTNTEV RRLEKNVKEV LEDFAEDNEK KVKLLTGKRV QLAEDLKKVR
EIQEKLEAFI EALHQEK
