FZO_DROSI
ID FZO_DROSI Reviewed; 454 AA.
AC Q9N6P4; Q9NGI3; Q9NGI4; Q9NGI5; Q9NGI6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Transmembrane GTPase fzo;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q8IWA4};
DE AltName: Full=Protein fuzzy onions;
DE Flags: Fragment;
GN Name=fzo;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=Isolate SIM1, Isolate SIM2, Isolate SIM3, Isolate SIM4,
RC Isolate SIM5, Isolate SIM6, Isolate SIM7, and Isolate SIM8;
RX PubMed=10823947; DOI=10.1073/pnas.97.11.5960;
RA Begun D.J., Whitley P.;
RT "Reduced X-linked nucleotide polymorphism in Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5960-5965(2000).
CC -!- FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial
CC fusion during spermatogenesis. In early spermatocytes, fusion of
CC mitochondria give rise to two organelles named Nebenkern and
CC constitutes an important step in mitochondria morphology, which is
CC balanced between fusion and fission. Essential for fertility (By
CC similarity). {ECO:0000250|UniProtKB:O18412}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q8IWA4};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O18412}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O18412}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01055}.
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DR EMBL; AF252672; AAF68054.1; -; Genomic_DNA.
DR EMBL; AF252673; AAF68055.1; -; Genomic_DNA.
DR EMBL; AF252674; AAF68056.1; -; Genomic_DNA.
DR EMBL; AF252675; AAF68057.1; -; Genomic_DNA.
DR EMBL; AF252676; AAF68058.1; -; Genomic_DNA.
DR EMBL; AF252677; AAF68059.1; -; Genomic_DNA.
DR EMBL; AF252678; AAF68060.1; -; Genomic_DNA.
DR EMBL; AF252679; AAF68061.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9N6P4; -.
DR SMR; Q9N6P4; -.
DR PRIDE; Q9N6P4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0007287; P:Nebenkern assembly; ISS:UniProtKB.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:EnsemblMetazoa.
DR GO; GO:0030382; P:sperm mitochondrion organization; IEA:EnsemblMetazoa.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027088; Mitofusin-1.
DR InterPro; IPR027094; Mitofusin_fam.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR PANTHER; PTHR10465:SF2; PTHR10465:SF2; 1.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; Developmental protein; Differentiation; GTP-binding;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Spermatogenesis; Transmembrane; Transmembrane helix.
FT CHAIN <1..>454
FT /note="Transmembrane GTPase fzo"
FT /id="PRO_0000127681"
FT TOPO_DOM <1..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..335
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..338
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..361
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..>454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..111
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 30..33
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 112..162
FT /evidence="ECO:0000255"
FT COILED 411..434
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT VARIANT 78
FT /note="S -> L (in strain: Isolate SIM7)"
FT VARIANT 146
FT /note="E -> D (in strain: Isolate SIM1, Isolate SIM3 and
FT Isolate SIM6)"
FT VARIANT 150
FT /note="Y -> F (in strain: Isolate SIM3 and Isolate SIM6)"
FT VARIANT 195
FT /note="G -> S (in strain: Isolate SIM3, Isolate SIM6 and
FT Isolate SIM7)"
FT VARIANT 232
FT /note="L -> M (in strain: Isolate SIM3, Isolate SIM6 and
FT Isolate SIM7)"
FT VARIANT 285
FT /note="S -> A (in strain: Isolate SIM3, Isolate SIM6 and
FT Isolate SIM7)"
FT VARIANT 304
FT /note="P -> L (in strain: Isolate SIM7)"
FT VARIANT 355
FT /note="M -> I (in strain: Isolate SIM1, Isolate SIM3 and
FT Isolate SIM6)"
FT NON_TER 1
FT NON_TER 454
SQ SEQUENCE 454 AA; 52686 MW; 2443AFFD680DBFB4 CRC64;
SSMEPEMEQK VKDQHMERCV NLLVDELGVY STAQEAWERI YHVSALEALH IRNGHIKNPS
AQTKERYQEF LRFENDFSNC LAVSALKTKF GPHLLSAQKI LNQLKSTLIS PFIEKVSRLI
DENKERRANL NAEIEEWELE MQDEREDLQY CFEELTEMTQ RLGRCVLNDQ IKTLIPSAVL
SFSHPFHPEF PAQIGQYQRS LCAHLDNLLE DRVLQCLSIP LQRKILDMEK ELGLQITEKS
CDWQLIYGLD CQSYMSDFQP DLRFRFSLGF TALWHRLEGN LPLHSSPFRT QKLRNGHKKC
LPLPPLVHGN HWQMLESLVK SKGSLGTVLL GAMAIRSFNW PIVMILGGLV GSFYMYEYAA
WTTAAQERSF KSQYSRLLQQ RLRTDVQQTV SGFELQLRQH LAKVRNCWEA QSNETLNDLN
VRTAELTKQI QSMEVLQLSL KKFRDKGQLL ASRL
