FZO1_SCHPO
ID FZO1_SCHPO Reviewed; 758 AA.
AC Q9USY7; Q8WZK6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transmembrane GTPase fzo1;
DE EC=3.6.5.-;
GN Name=fzo1; ORFNames=SPBC1706.03, SPBC839.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Probable transmembrane GTPase, which mediates mitochondrial
CC fusion. Fusion of mitochondria occurs in many cell types and
CC constitutes an important step in mitochondrial morphology, which is
CC balanced between fusion and fission (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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; CU329671; CAA19004.1; -; Genomic_DNA.
DR PIR; T39628; T39628.
DR RefSeq; NP_595241.1; NM_001021147.2.
DR AlphaFoldDB; Q9USY7; -.
DR BioGRID; 276406; 3.
DR STRING; 4896.SPBC1706.03.1; -.
DR MaxQB; Q9USY7; -.
DR PaxDb; Q9USY7; -.
DR EnsemblFungi; SPBC1706.03.1; SPBC1706.03.1:pep; SPBC1706.03.
DR GeneID; 2539859; -.
DR KEGG; spo:SPBC1706.03; -.
DR PomBase; SPBC1706.03; fzo1.
DR VEuPathDB; FungiDB:SPBC1706.03; -.
DR eggNOG; KOG0448; Eukaryota.
DR HOGENOM; CLU_011752_0_0_1; -.
DR InParanoid; Q9USY7; -.
DR OMA; AHEKAYI; -.
DR PhylomeDB; Q9USY7; -.
DR Reactome; R-SPO-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q9USY7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0061791; F:GTPase motor activity; ISM:PomBase.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR Pfam; PF00350; Dynamin_N; 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..758
FT /note="Transmembrane GTPase fzo1"
FT /id="PRO_0000127683"
FT TOPO_DOM 1..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..635
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 151..426
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..168
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 187..191
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 270..273
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 327..330
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 364..367
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 27..70
FT /evidence="ECO:0000255"
FT COMPBIAS 7..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 164..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 327..330
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
SQ SEQUENCE 758 AA; 87102 MW; 30868CA8171F85A1 CRC64;
MEKSARQLSV AEQNGESGRL NNGYTSNNIQ QYKDETNRHQ FEYNQNRNQL LRSIHIIQNL
LNELDNYVDR SDCLFHSVWR TDKEKSKFSG NYYPFSPSKM NVITIDLSLR SSSTADEKLI
SQLGEEAHES LLKVHIEKAN KHLFSLFSRV EDTSSKILIT GDLNAGKSTL CNALVHKDIL
PEDQQPCTEV FCEVHDAELN DGKDCVHAIP HGLTYSHTDS STYKVFPIED LKRLVYETEN
WSMLIVYVND GRPAHESLLH NGITDIALID APGLNTDSMK TTSVFACQEE IDVVVFVVNA
ENHFTLSATD FLRNASTEKS HIFIIVNKFD NIRDKERCKR LILEQIHTLS PGTFADAKDL
VHFVSCRVAR DPNNREDALY SSFFQMENSL RSFILENRSK SKLAPVRRYL SGLVGDILNI
CEYNIKLIDF DINHLQQRLT DLSPKFRKVK HEQQFTYQKN ESLVEATVQS ISQHTHSELE
DAIDSLGSFA SVKYSGFFFA YQYAISVRDA MQQYLEEKLL ESEDYARKRT EEAVLCIQKD
VKDNFDSAVL PVFHANQMFI KKHRLQLQKH FRFELGLLDF IDLDLTERLG TWSASLSTIL
LVLGKTTPSF TTLGAFTGNL GYPIFKYFQN NSLQHLLVPV LGLASICVFG YVIYDIPRAL
PLKVAEKIKK SLRETDFCHN ASIWIGTESR KVLNIPLNDL RRMFHQQWDK QRETISVAEN
DLRICQKARK FFGEIESRTR EAKKKIMMVQ LEGCDINY
