FZO1_CAEEL
ID FZO1_CAEEL Reviewed; 774 AA.
AC Q23424;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane GTPase fzo-1;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:Q8IWA4};
GN Name=fzo-1 {ECO:0000312|WormBase:ZK1248.14};
GN ORFNames=ZK1248.14 {ECO:0000312|WormBase:ZK1248.14};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21248201; DOI=10.1091/mbc.e10-07-0600;
RA Head B.P., Zulaika M., Ryazantsev S., van der Bliek A.M.;
RT "A novel mitochondrial outer membrane protein, MOMA-1, that affects cristae
RT morphology in Caenorhabditis elegans.";
RL Mol. Biol. Cell 22:831-841(2011).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25190516; DOI=10.15252/embj.201489039;
RA Ackema K.B., Hench J., Boeckler S., Wang S.C., Sauder U., Mergentaler H.,
RA Westermann B., Bard F., Frank S., Spang A.;
RT "The small GTPase Arf1 modulates mitochondrial morphology and function.";
RL EMBO J. 33:2659-2675(2014).
CC -!- FUNCTION: Probable transmembrane GTPase (By similarity). Mediates
CC mitochondrial fusion (PubMed:21248201, PubMed:25190516). Fusion of
CC mitochondria occurs in many cell types and constitutes an important
CC step in mitochondria morphology, which is balanced between fusion and
CC fission (By similarity). {ECO:0000250|UniProtKB:P38297,
CC ECO:0000269|PubMed:21248201, ECO:0000269|PubMed:25190516}.
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:Q8IWA4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8IWA4}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in fragmented
CC mitochondria, most likely due to lack of fusion activity
CC (PubMed:25190516). RNAi-mediated knockdown in a moma-1 mutant
CC background results in mitochondrial fragmentation.
CC {ECO:0000269|PubMed:21248201, ECO:0000269|PubMed:25190516}.
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; BX284602; CCD72511.1; -; Genomic_DNA.
DR PIR; T34496; T34496.
DR RefSeq; NP_495161.1; NM_062760.5.
DR AlphaFoldDB; Q23424; -.
DR SMR; Q23424; -.
DR BioGRID; 39331; 2.
DR STRING; 6239.ZK1248.14; -.
DR iPTMnet; Q23424; -.
DR EPD; Q23424; -.
DR PaxDb; Q23424; -.
DR PeptideAtlas; Q23424; -.
DR EnsemblMetazoa; ZK1248.14.1; ZK1248.14.1; WBGene00001509.
DR GeneID; 173990; -.
DR KEGG; cel:CELE_ZK1248.14; -.
DR UCSC; ZK1248.14; c. elegans.
DR CTD; 173990; -.
DR WormBase; ZK1248.14; CE02898; WBGene00001509; fzo-1.
DR eggNOG; KOG0448; Eukaryota.
DR GeneTree; ENSGT00390000013727; -.
DR HOGENOM; CLU_021212_1_0_1; -.
DR InParanoid; Q23424; -.
DR OMA; LEFRFSF; -.
DR OrthoDB; 216494at2759; -.
DR PhylomeDB; Q23424; -.
DR Reactome; R-CEL-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-CEL-9013419; RHOT2 GTPase cycle.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q23424; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001509; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031306; C:intrinsic component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:WormBase.
DR GO; GO:0051646; P:mitochondrion localization; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR006884; Fzo/mitofusin_HR2.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027088; Mitofusin-1.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR PANTHER; PTHR10465:SF2; PTHR10465:SF2; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF04799; Fzo_mitofusin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil; GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..774
FT /note="Transmembrane GTPase fzo-1"
FT /id="PRO_0000127678"
FT TOPO_DOM 1..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..640
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..774
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 97..352
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..114
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 133..134
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 211..214
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 270..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 300
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 51..71
FT /evidence="ECO:0000255"
FT COILED 385..415
FT /evidence="ECO:0000255"
FT BINDING 110..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
SQ SEQUENCE 774 AA; 87462 MW; 1A8AB21F77F2877A CRC64;
MSGTASLVHT LPASGDSNHR GLHSLKNSRR AADNEPLLRF REAKKVLGDV YGELKDNVAE
LEGVYKDIKE NDFVSSEQRE EIEAIGDSIK TIMDTFQRDN MKVVFFGRTS NGKSTTINAM
LHEKVLPQGM GHTTCCFLQV EGSEGEVGHL QLDDNPQKID MKMLGKIGHA LSDENSDLPA
MGQDSLLKVF HPKKSESGEC RLLQNDVVIL DSPGVDLSPE FDSWIDKHCL DADVFVLVSN
AESTLTQAEK NFFLRVAKKL SKPNVFILNN RWDASAAETE NIEDVKKQHL TRFRQFLVDE
LEVCSEREVN DRIFFVSSRE VLESRLKARG LVQKAYQAEG HGTRALEFQN FERHFEHCIS
RSAIHTKFEA HNRRAHEMIG KMRLNLNSVL TSAAEQRSKL QNNLNESTRT FNECRVNFTQ
FEKAYREQTE QLRAEVHLKV SADFFEEIAR LDAIIDRFEQ PFDGSSSGMT KYKEDLAIFV
DKCLSSDLEA RCTGGLMSRI WNLENDMFQY VTKILAEPYQ NKLEEVWRYR APFKFSICVD
VPALVNDFHE DLEFRFTFGL HAIIRRIIAY RSGQPVTAIN TNLLTPLSLK QQSEKNSVRD
AEASAASEEQ AMMTQMVLTS AAFLANGSLG VLVVGGIVYK AVGWRVIAVG GAAYAGLYAW
ERMRWNSGAK EQHLKEQFRS HLAARMQQVS TAHTHHCETQ AIREMDQVFD GLKATVGGVH
REMKNDLDVQ KTQIDAVDST IRTLGTIKGK AVFLLRNLEQ FASSYLRSDS PPTP
