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FZO_DROME
ID   FZO_DROME               Reviewed;         718 AA.
AC   O18412; Q4V3Y6; Q9VCP7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Transmembrane GTPase fzo;
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:Q8IWA4};
DE   AltName: Full=Protein fuzzy onions;
GN   Name=fzo; ORFNames=CG4568;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF LYS-99 AND ARG-249.
RC   TISSUE=Testis;
RX   PubMed=9230308; DOI=10.1016/s0092-8674(00)80319-0;
RA   Hales K.G., Fuller M.T.;
RT   "Developmentally regulated mitochondrial fusion mediated by a conserved,
RT   novel, predicted GTPase.";
RL   Cell 90:121-129(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12128227; DOI=10.1016/s0925-4773(02)00141-7;
RA   Hwa J.J., Hiller M.A., Fuller M.T., Santel A.;
RT   "Differential expression of the Drosophila mitofusin genes fuzzy onions
RT   (fzo) and dmfn.";
RL   Mech. Dev. 116:213-216(2002).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18799731; DOI=10.1073/pnas.0803998105;
RA   Deng H., Dodson M.W., Huang H., Guo M.;
RT   "The Parkinson's disease genes pink1 and parkin promote mitochondrial
RT   fission and/or inhibit fusion in Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14503-14508(2008).
CC   -!- FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial
CC       fusion during spermatogenesis (PubMed:9230308, PubMed:18799731). In
CC       early spermatocytes, fusion of mitochondria give rise to two organelles
CC       named Nebenkern and constitutes an important step in mitochondria
CC       morphology, which is balanced between fusion and fission
CC       (PubMed:9230308, PubMed:18799731). Essential for fertility
CC       (PubMed:9230308). {ECO:0000269|PubMed:18799731,
CC       ECO:0000269|PubMed:9230308}.
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:0000269|PubMed:9230308}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:9230308}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in male germ cells, in
CC       spermatocytes and early spermatids. Not expressed in other tissues.
CC       {ECO:0000269|PubMed:12128227, ECO:0000269|PubMed:9230308}.
CC   -!- DEVELOPMENTAL STAGE: Associated with mitochondria in spermatids during
CC       a narrow developmental window. Mitochondria align on the spindle
CC       equator throughout meiotic divisions, but it is not expressed on
CC       mitochondria until the last of meiosis II. In postmeiotic haploid
CC       spermatids, it is associated with aggregating mitochondria and highly
CC       expressed on onion stage Nebenkerns. Expressed at lower levels
CC       associated with early elongation stage mitochondrial derivatives. Not
CC       detected on more elongated mitochondria.
CC   -!- DISRUPTION PHENOTYPE: Defective mitochondrial fusion in spermatids
CC       results in onion-staged nebenkerns with irregular borders that contain
CC       many small mitochondria (PubMed:18799731). At the leaf-blade stage
CC       nebenkerns contain many small mitochondria instead of the two
CC       mitochondria derivatives seen in wild-type spermatids
CC       (PubMed:18799731). {ECO:0000269|PubMed:18799731}.
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; U95821; AAC24457.1; -; mRNA.
DR   EMBL; AE014297; AAF56110.2; -; Genomic_DNA.
DR   EMBL; BT023200; AAY55616.1; -; mRNA.
DR   EMBL; BT023220; AAY55636.1; -; mRNA.
DR   EMBL; BT023232; AAY55648.1; -; mRNA.
DR   RefSeq; NP_732840.1; NM_170060.2.
DR   AlphaFoldDB; O18412; -.
DR   SMR; O18412; -.
DR   BioGRID; 67689; 15.
DR   IntAct; O18412; 1.
DR   STRING; 7227.FBpp0083791; -.
DR   PaxDb; O18412; -.
DR   DNASU; 42745; -.
DR   EnsemblMetazoa; FBtr0084399; FBpp0083791; FBgn0011596.
DR   GeneID; 42745; -.
DR   KEGG; dme:Dmel_CG4568; -.
DR   CTD; 42745; -.
DR   FlyBase; FBgn0011596; fzo.
DR   VEuPathDB; VectorBase:FBgn0011596; -.
DR   eggNOG; KOG0448; Eukaryota.
DR   GeneTree; ENSGT00390000013727; -.
DR   HOGENOM; CLU_021212_1_0_1; -.
DR   InParanoid; O18412; -.
DR   OMA; WDMASSQ; -.
DR   OrthoDB; 216494at2759; -.
DR   PhylomeDB; O18412; -.
DR   Reactome; R-DME-5205685; PINK1-PRKN Mediated Mitophagy.
DR   Reactome; R-DME-9013419; RHOT2 GTPase cycle.
DR   Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR   BioGRID-ORCS; 42745; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42745; -.
DR   PRO; PR:O18412; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0011596; Expressed in testis and 12 other tissues.
DR   Genevisible; O18412; DM.
DR   GO; GO:0016021; C:integral component of membrane; TAS:FlyBase.
DR   GO; GO:0031306; C:intrinsic component of mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0005740; C:mitochondrial envelope; IDA:FlyBase.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IMP:UniProtKB.
DR   GO; GO:0008053; P:mitochondrial fusion; IMP:FlyBase.
DR   GO; GO:0051646; P:mitochondrion localization; IBA:GO_Central.
DR   GO; GO:0007287; P:Nebenkern assembly; IMP:FlyBase.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:UniProtKB.
DR   GO; GO:0030382; P:sperm mitochondrion organization; IMP:FlyBase.
DR   GO; GO:0007283; P:spermatogenesis; TAS:FlyBase.
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   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Differentiation; GTP-binding;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Reference proteome; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..718
FT                   /note="Transmembrane GTPase fzo"
FT                   /id="PRO_0000127680"
FT   TOPO_DOM        1..575
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        576..588
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        589..591
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        592..614
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        615..718
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          83..364
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          93..100
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          119..120
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          189..192
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          248..251
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   REGION          283..286
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT   COILED          366..402
FT                   /evidence="ECO:0000255"
FT   COILED          664..687
FT                   /evidence="ECO:0000255"
FT   BINDING         96..101
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   BINDING         248..251
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   BINDING         297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT   MUTAGEN         99
FT                   /note="K->T: Induces male infertility."
FT                   /evidence="ECO:0000269|PubMed:9230308"
FT   MUTAGEN         249
FT                   /note="R->L: Induces male infertility."
FT                   /evidence="ECO:0000269|PubMed:9230308"
SQ   SEQUENCE   718 AA;  81565 MW;  152CF237AFB333BD CRC64;
     MAESDSGEST SSVSSFISSS SSSRLSEFVD AKTELQDIYH DLSNYLSNFL TILEETVLLK
     DRQMLEHLCA FSSRVEAIAK VLSRDRMKVA FFGRTSNGKS AVINALLHEK ILPSAMGHTT
     SCFCQVQANG SNETEHVKVE QEDEHMELSA LSQLASAHSP GALKPSTLLQ VNMAKNRCSI
     LDYDVVLMDT PGVDVTAQLD DCLDSYCMDA DVFILVLNAE STVSRVERQF FKDVASKLSR
     PNLFILNNRW DKASSLEPEM EQKVKDQHME RCVNLLVDEL GVYSTAQEAW ERIYHVSALE
     ALHIRNGQIT NPSGQTQQRY QEFLRFENDF SNCLAVSALK TKFGPHLLSA QKILNQLKST
     LICPFIEKVS RLIDENKERR ANLNAEIEDW LILMQEDREA LQYCFEELTE MTQRVGRCVL
     NDQIKTLIPS SVLSFSQPFH PEFPAQIGQY QRSLCAHLDK LLEDRVLQCL SIPLQRKILD
     IEKEIGLPIA ENSCDWQLIY GLDCQSYMSD FQPDLRFRFS LGFTALWHRL EGNLPLHASP
     FRIQKLQNGH KKCSPLPPLV NGNHWQMLES LVKSKGSLGT VLLSAMAIRS FNWPIVLILG
     GLVGSFYIYE YAAWTTAAQE RSFKSQYARL LQQRLRSDVQ QTVSGFELQL RQHLATVRNC
     WEAQSNETLN DLNVRTAELT KQIQSMEVLQ LSLKKFRDKG QLLASRLGDF QETYLTKS
 
 
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