FZL_ARATH
ID FZL_ARATH Reviewed; 912 AA.
AC Q1KPV0; Q67Z21; Q6NQ84; Q9SA53; Q9ZVR8;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable transmembrane GTPase FZO-like, chloroplastic {ECO:0000305};
DE EC=3.6.5.-;
DE Flags: Precursor;
GN Name=FZL {ECO:0000303|PubMed:16617119};
GN OrderedLocusNames=At1g03160 {ECO:0000312|Araport:AT1G03160};
GN ORFNames=F10O3.1 {ECO:0000312|EMBL:AAD25810.1},
GN F15K9.23 {ECO:0000312|EMBL:AAC72117.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:ABE96616.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF LYS-362, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=16617119; DOI=10.1073/pnas.0507287103;
RA Gao H., Sage T.L., Osteryoung K.W.;
RT "FZL, an FZO-like protein in plants, is a determinant of thylakoid and
RT chloroplast morphology.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6759-6764(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-642.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=23963675; DOI=10.1093/jxb/ert237;
RA Landoni M., De Francesco A., Bellatti S., Delledonne M., Ferrarini A.,
RA Venturini L., Pilu R., Bononi M., Tonelli C.;
RT "A mutation in the FZL gene of Arabidopsis causing alteration in
RT chloroplast morphology results in a lesion mimic phenotype.";
RL J. Exp. Bot. 64:4313-4328(2013).
CC -!- FUNCTION: Probable membrane-remodeling GTPase that plays a unique role
CC in the in the determination of thylakoid and chloroplast morphology and
CC regulates organization of the thylakoid network. Not involved in the
CC determination of mitochondrial morphology or ultrastructure.
CC {ECO:0000269|PubMed:16617119}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000269|PubMed:16617119}; Multi-pass membrane protein
CC {ECO:0000255}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:16617119}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes in a punctate pattern in chloroplasts.
CC {ECO:0000269|PubMed:16617119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1KPV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1KPV0-2; Sequence=VSP_057783, VSP_057784;
CC -!- DISRUPTION PHENOTYPE: Pale green leaves phenotype and delayed flowering
CC (PubMed:16617119). Decreased number of chloroplasts and heterogeneity
CC in size in mature mesophyll cells (PubMed:16617119, PubMed:23963675).
CC Abnormalities in chloroplast and thylakoid morphology, including
CC disorganized grana stacks and alterations in the relative proportions
CC of grana and stroma thylakoids (PubMed:16617119). Lesion mimic
CC phenotype with activation of defense response markers in the ecotype
CC Landsberg erecta (PubMed:23963675). {ECO:0000269|PubMed:16617119,
CC ECO:0000269|PubMed:23963675}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72117.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD25810.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ462573; ABE96616.1; -; mRNA.
DR EMBL; AC005278; AAC72117.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006550; AAD25810.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27537.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27538.1; -; Genomic_DNA.
DR EMBL; AK176297; BAD44060.1; -; mRNA.
DR EMBL; AK227660; BAE99647.1; -; mRNA.
DR EMBL; BT010575; AAQ65198.1; -; mRNA.
DR PIR; G86162; G86162.
DR PIR; H86162; H86162.
DR RefSeq; NP_001077452.1; NM_001083983.1. [Q1KPV0-2]
DR RefSeq; NP_171815.3; NM_100198.5. [Q1KPV0-1]
DR AlphaFoldDB; Q1KPV0; -.
DR IntAct; Q1KPV0; 7.
DR STRING; 3702.AT1G03160.1; -.
DR iPTMnet; Q1KPV0; -.
DR PaxDb; Q1KPV0; -.
DR PRIDE; Q1KPV0; -.
DR ProteomicsDB; 230051; -. [Q1KPV0-1]
DR EnsemblPlants; AT1G03160.1; AT1G03160.1; AT1G03160. [Q1KPV0-1]
DR EnsemblPlants; AT1G03160.2; AT1G03160.2; AT1G03160. [Q1KPV0-2]
DR GeneID; 839566; -.
DR Gramene; AT1G03160.1; AT1G03160.1; AT1G03160. [Q1KPV0-1]
DR Gramene; AT1G03160.2; AT1G03160.2; AT1G03160. [Q1KPV0-2]
DR KEGG; ath:AT1G03160; -.
DR Araport; AT1G03160; -.
DR TAIR; locus:2007579; AT1G03160.
DR eggNOG; KOG0448; Eukaryota.
DR HOGENOM; CLU_014646_0_0_1; -.
DR InParanoid; Q1KPV0; -.
DR OMA; HFWEDVQ; -.
DR OrthoDB; 226412at2759; -.
DR PhylomeDB; Q1KPV0; -.
DR PRO; PR:Q1KPV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q1KPV0; baseline and differential.
DR Genevisible; Q1KPV0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031969; C:chloroplast membrane; IDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:TAIR.
DR GO; GO:0034051; P:negative regulation of plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Developmental protein;
KW GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Plastid;
KW Plastid inner membrane; Reference proteome; Thylakoid; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..912
FT /note="Probable transmembrane GTPase FZO-like,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433470"
FT TOPO_DOM 55..773
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:16617119"
FT TRANSMEM 774..794
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..801
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:16617119"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..912
FT /note="Stromal"
FT /evidence="ECO:0000305|PubMed:16617119"
FT REGION 51..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 877..904
FT /evidence="ECO:0000255"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359..364
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT VAR_SEQ 698..740
FT /note="ELLGKYAEWLQSNTAREGSLSLKSFENKWPTYVNSKTQLGIDT -> VSVML
FT YSLSIGLTGDMLVIYMRNCLENMLNGYNQILPVKGVCL (in isoform 2)"
FT /id="VSP_057783"
FT VAR_SEQ 741..912
FT /note="Missing (in isoform 2)"
FT /id="VSP_057784"
FT MUTAGEN 362
FT /note="K->M: Loss of function and no detection in punctate
FT structures."
FT /evidence="ECO:0000269|PubMed:16617119"
FT CONFLICT 642
FT /note="I -> V (in Ref. 5; AAQ65198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 912 AA; 100731 MW; 6904836A55B43456 CRC64;
MRTLISHRQC VTSPFLISAA SPPFPGRCFK LSSFTPPRHR RFSSLSIRNI SHESADQTSS
SRPRTLYPGG YKRPELAVPG LLLRLDADEV MSGNREETLD LVDRALAKSV QIVVIDGGAT
AGKLYEAACL LKSLVKGRAY LLIAERVDIA SAVGASGVAL SDEGLPAIVA RNTLMGSNPD
SVLLPLVARI VKDVDSALIA SSSEGADFLI LGSGEEDTQV ADSLLKSVKI PIYVTCRGNE
EAKEELQLLK SGVSGFVISL KDLRSSRDVA LRQSLDGAYV VNNHETQNMN ELPEKKNSAG
FIKLEDKQKL IVEMEKSVLR ETIEIIHKAA PLMEEVSLLI DAVSRIDEPF LMVIVGEFNS
GKSTVINALL GKRYLKEGVV PTTNEITFLC YSDLESEEQQ RCQTHPDGQY VCYLPAPILK
DINIVDTPGT NVILQRQQRL TEEFVPRADL LVFVLSADRP LTESEVAFLR YTQQWKKKFV
FILNKSDIYR DARELEEAIS FVKENTRKLL NTENVILYPV SARSALEAKL STASLVGRDD
LEIADPGSNW RVQSFNELEK FLYSFLDSST ATGMERIRLK LETPMAIAER LLSSVEALVR
QDCLAAREDL ASADKIISRT KEYALKMEYE SISWRRQALS LIDNARLQVV DLIGTTLRLS
SLDLAISYVF KGEKSASVAA TSKVQGEILA PALTNAKELL GKYAEWLQSN TAREGSLSLK
SFENKWPTYV NSKTQLGIDT YDLLQKTDKV SLKTIQNLSA GTTSKRLEQD IREVFFVTVG
GLGAAGLSAS LLTSVLPTTL EDLLALGLCS AGGYVAIANF PYRRQAIIGK VNKVADALAQ
QLEDAMQKDL SDATSNLVNF VNIVAKPYRE EAQLRLDRLL GIQKELSDIR SKLQLLQVDI
DNLHVSRDEM RL
