TC159_ARATH
ID TC159_ARATH Reviewed; 1503 AA.
AC O81283; O22774; Q56W83; Q945M4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Translocase of chloroplast 159, chloroplastic;
DE Short=AtToc159;
DE EC=3.6.5.-;
DE AltName: Full=159 kDa chloroplast outer envelope protein;
DE AltName: Full=Plastid protein import 2;
DE AltName: Full=Translocase of chloroplast 160, chloroplastic;
DE Short=AtToc160;
DE AltName: Full=Translocase of chloroplast 86, chloroplastic;
DE Short=AtToc86;
GN Name=TOC159; Synonyms=PPI2, TOC160, TOC86; OrderedLocusNames=At4g02510;
GN ORFNames=T10P11.19, T14P8.24;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1004-1503.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 815-1503.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH THE TOC COMPLEX, AND INDUCTION BY LIGHT.
RX PubMed=10646606; DOI=10.1038/35003214;
RA Bauer J., Chen K., Hiltbunner A., Wehrli E., Eugster M., Schnell D.,
RA Kessler F.;
RT "The major protein import receptor of plastids is essential for chloroplast
RT biogenesis.";
RL Nature 403:203-207(2000).
RN [6]
RP INTERACTION WITH TOC33, MUTAGENESIS OF ALA-864 AND LYS-868, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12473690; DOI=10.1083/jcb.200208017;
RA Smith M.D., Hiltbrunner A., Kessler F., Schnell D.J.;
RT "The targeting of the atToc159 preprotein receptor to the chloroplast outer
RT membrane is mediated by its GTPase domain and is regulated by GTP.";
RL J. Cell Biol. 159:833-843(2002).
RN [7]
RP FUNCTION, AND DIMERIZATION WITH TOC33.
RX PubMed=12869544; DOI=10.1074/jbc.m305946200;
RA Weibel P., Hiltbrunner A., Brand L., Kessler F.;
RT "Dimerization of Toc-GTPases at the chloroplast protein import machinery.";
RL J. Biol. Chem. 278:37321-37329(2003).
RN [8]
RP FUNCTION, MUTAGENESIS OF LYS-868, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH TOC33.
RX PubMed=12951325; DOI=10.1074/jbc.m307873200;
RA Wallas T.R., Smith M.D., Sanchez-Nieto S., Schnell D.J.;
RT "The roles of Toc34 and Toc75 in targeting the Toc159 preprotein receptor
RT to chloroplasts.";
RL J. Biol. Chem. 278:44289-44297(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12766230; DOI=10.1074/mcp.m300030-mcp200;
RA Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M.,
RA Garin J., Joyard J., Rolland N.;
RT "Proteomics of the chloroplast envelope membranes from Arabidopsis
RT thaliana.";
RL Mol. Cell. Proteomics 2:325-345(2003).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15273297; DOI=10.1105/tpc.104.023309;
RA Kubis S., Patel R., Combe J., Bedard J., Kovacheva S., Lilley K., Biehl A.,
RA Leister D., Rios G., Koncz C., Jarvis P.;
RT "Functional specialization amongst the Arabidopsis Toc159 family of
RT chloroplast protein import receptors.";
RL Plant Cell 16:2059-2077(2004).
RN [11]
RP FUNCTION, INDUCTION BY LIGHT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15284497; DOI=10.1023/b:plan.0000036374.92546.51;
RA Hiltbrunner A., Gruenig K., Alvarez-Huerta M., Infanger S., Bauer J.,
RA Kessler F.;
RT "AtToc90, a new GTP-binding component of the Arabidopsis chloroplast
RT protein import machinery.";
RL Plant Mol. Biol. 54:427-440(2004).
RN [12]
RP FUNCTION.
RX PubMed=16435266; DOI=10.1055/s-2005-873044;
RA Hust B., Gutensohn M.;
RT "Deletion of core components of the plastid protein import machinery causes
RT differential arrest of embryo development in Arabidopsis thaliana.";
RL Plant Biol. 8:18-30(2006).
RN [13]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17261588; DOI=10.1074/jbc.m609491200;
RA Reddick L.E., Vaughn M.D., Wright S.J., Campbell I.M., Bruce B.D.;
RT "In vitro comparative kinetic analysis of the chloroplast Toc GTPases.";
RL J. Biol. Chem. 282:11410-11426(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-665, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-210; SER-281;
RP SER-288; SER-448; SER-589; SER-609; SER-630 AND SER-632, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [17]
RP INTERACTION WITH SP1.
RX PubMed=23118188; DOI=10.1126/science.1225053;
RA Ling Q., Huang W., Baldwin A., Jarvis P.;
RT "Chloroplast biogenesis is regulated by direct action of the ubiquitin-
RT proteasome system.";
RL Science 338:655-659(2012).
CC -!- FUNCTION: GTPase involved in protein precursor import into
CC chloroplasts. Seems to recognize chloroplast-destined precursor
CC proteins and regulate their presentation to the translocation channel
CC through GTP hydrolysis. Required for chloroplast biogenesis. Probably
CC specialized in the import of nuclear encoded photosynthetic preproteins
CC from the cytoplasm to the chloroplast. {ECO:0000269|PubMed:10646606,
CC ECO:0000269|PubMed:12869544, ECO:0000269|PubMed:12951325,
CC ECO:0000269|PubMed:15273297, ECO:0000269|PubMed:15284497,
CC ECO:0000269|PubMed:16435266}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.2 uM for GTP (at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17261588};
CC -!- SUBUNIT: Homodimer and heterodimer with TOC33. Part of the TOC core
CC complex that includes 1 protein for the specific recognition of transit
CC peptides surrounded by a ring composed of four proteins forming
CC translocation channels, and four to five GTP-binding proteins providing
CC energy. This core complex can interact with components of the TIC
CC complex to form a larger import complex. Chloroplastic protein
CC precursor such as prSS (precursor of the RuBisCO small subunit)
CC interacts with these complexes. The TOC complex contains a specific
CC subset of polar lipids such as digalactosyldiacylglyceride (DGDG),
CC phosphatidylcholine (PC) and phosphatidylglycerol (PG)
CC (PubMed:10646606, PubMed:12473690, PubMed:12951325). Interacts with SP1
CC (PubMed:23118188). {ECO:0000269|PubMed:10646606,
CC ECO:0000269|PubMed:12473690, ECO:0000269|PubMed:12951325,
CC ECO:0000269|PubMed:23118188}.
CC -!- INTERACTION:
CC O81283; Q8L7N4: SP1; NbExp=2; IntAct=EBI-639063, EBI-6559199;
CC O81283; Q38906: TOC34; NbExp=5; IntAct=EBI-639063, EBI-1766808;
CC O81283; P69249: RBCS; Xeno; NbExp=5; IntAct=EBI-639063, EBI-1766821;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane; Single-pass
CC membrane protein. Cytoplasm. Note=Cycles between the cytoplasm and
CC chloroplast, probably as a soluble preprotein receptor. The anchoring
CC to the chloroplast outer membrane required the GTPase activity and GDP,
CC and is dependent of interactions with TOC33 as well as TOC34 and TOC75.
CC May contain beta barrel transmembrane regions.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in seedlings, and, to a lower
CC extent, in leaves and flowers.
CC -!- INDUCTION: By light conditions. {ECO:0000269|PubMed:10646606,
CC ECO:0000269|PubMed:15284497}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC159 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78265.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL06516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB80744.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002330; AAC78265.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AF069298; AAC19285.1; -; Genomic_DNA.
DR EMBL; AL161494; CAB80744.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82182.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66758.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66759.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66760.1; -; Genomic_DNA.
DR EMBL; AF412063; AAL06516.1; ALT_INIT; mRNA.
DR EMBL; AY133653; AAM91483.1; -; mRNA.
DR EMBL; AK222164; BAD95269.1; -; mRNA.
DR PIR; A85032; A85032.
DR PIR; T01098; T01098.
DR RefSeq; NP_001319848.1; NM_001340383.1.
DR RefSeq; NP_001328635.1; NM_001340385.1.
DR RefSeq; NP_001328636.1; NM_001340384.1.
DR RefSeq; NP_567242.2; NM_116485.4.
DR AlphaFoldDB; O81283; -.
DR SMR; O81283; -.
DR BioGRID; 13225; 52.
DR IntAct; O81283; 15.
DR MINT; O81283; -.
DR STRING; 3702.AT4G02510.1; -.
DR iPTMnet; O81283; -.
DR MetOSite; O81283; -.
DR SwissPalm; O81283; -.
DR PaxDb; O81283; -.
DR PRIDE; O81283; -.
DR ProteomicsDB; 234226; -.
DR EnsemblPlants; AT4G02510.1; AT4G02510.1; AT4G02510.
DR EnsemblPlants; AT4G02510.2; AT4G02510.2; AT4G02510.
DR EnsemblPlants; AT4G02510.3; AT4G02510.3; AT4G02510.
DR EnsemblPlants; AT4G02510.4; AT4G02510.4; AT4G02510.
DR GeneID; 827934; -.
DR Gramene; AT4G02510.1; AT4G02510.1; AT4G02510.
DR Gramene; AT4G02510.2; AT4G02510.2; AT4G02510.
DR Gramene; AT4G02510.3; AT4G02510.3; AT4G02510.
DR Gramene; AT4G02510.4; AT4G02510.4; AT4G02510.
DR KEGG; ath:AT4G02510; -.
DR Araport; AT4G02510; -.
DR TAIR; locus:2132298; AT4G02510.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_1_0_1; -.
DR InParanoid; O81283; -.
DR OMA; EFGYPGE; -.
DR OrthoDB; 41760at2759; -.
DR PhylomeDB; O81283; -.
DR PRO; PR:O81283; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81283; baseline and differential.
DR Genevisible; O81283; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0061927; C:TOC-TIC supercomplex I; IDA:TAIR.
DR GO; GO:0051087; F:chaperone binding; IPI:CAFA.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; TAS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:TAIR.
DR GO; GO:0045037; P:protein import into chloroplast stroma; IDA:TAIR.
DR GO; GO:0045036; P:protein targeting to chloroplast; IDA:TAIR.
DR DisProt; DP00609; -.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR024283; TOC159_MAD.
DR InterPro; IPR005690; Toc86_159.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR Pfam; PF11886; TOC159_MAD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00993; 3a0901s04IAP86; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Coiled coil; Cytoplasm; GTP-binding; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Plastid;
KW Plastid outer membrane; Protein transport; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1503
FT /note="Translocase of chloroplast 159, chloroplastic"
FT /id="PRO_0000352659"
FT TRANSMEM 21..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 853..1087
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..869
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 884..887
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 889..893
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 909..912
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 947..952
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 981..984
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1035..1037
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 781..804
FT /evidence="ECO:0000255"
FT COILED 1175..1203
FT /evidence="ECO:0000255"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 865..870
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 869
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 884..889
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 982
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 1035..1036
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SLF3"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MUTAGEN 864
FT /note="A->R: Reduced GTPase activity and impaired
FT chloroplast outer membrane anchoring."
FT /evidence="ECO:0000269|PubMed:12473690"
FT MUTAGEN 868
FT /note="K->R: Loss of GTPase activity and impaired
FT chloroplast outer membrane anchoring."
FT /evidence="ECO:0000269|PubMed:12473690,
FT ECO:0000269|PubMed:12951325"
FT CONFLICT 815
FT /note="Q -> L (in Ref. 4; BAD95269)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="K -> E (in Ref. 4; BAD95269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1503 AA; 160819 MW; 04AEDE84C1BED3F6 CRC64;
MDSKSVTPEP TNPFYASSGQ SGKTYASVVA AAAAAAADKE DGGAVSSAKE LDSSSEAVSG
NSDKVGADDL SDSEKEKPNL VGDGKVSDEV DGSLKEDSTT PEATPKPEVV SGETIGVDDV
SSLSPKPEAV SDGVGVVEEN KKVKEDVEDI KDDGESKIEN GSVDVDVKQA STDGESESKV
KDVEEEDVGT KKDDEGESEL GGKVDVDDKS DNVIEEEGVE LTDKGDVIVN SSPVESVHVD
VAKPGVVVVG DAEGSEELKI NADAETLEVA NKFDQIGDDD SGEFEPVSDK AIEEVEEKFT
SESDSIADSS KLESVDTSAV EPEVVAAESG SEPKDVEKAN GLEKGMTYAE VIKAASAVAD
NGTKEEESVL GGIVDDAEEG VKLNNKGDFV VDSSAIEAVN VDVAKPGVVV VGDVEVSEVL
ETDGNIPDVH NKFDPIGQGE GGEVELESDK ATEEGGGKLV SEGDSMVDSS VVDSVDADIN
VAEPGVVVVG AAKEAVIKED DKDDEVDKTI SNIEEPDDLT AAYDGNFELA VKEISEAAKV
EPDEPKVGVE VEELPVSESL KVGSVDAEED SIPAAESQFE VRKVVEGDSA EEDENKLPVE
DIVSSREFSF GGKEVDQEPS GEGVTRVDGS ESEEETEEMI FGSSEAAKQF LAELEKASSG
IEAHSDEANI SNNMSDRIDG QIVTDSDEDV DTEDEGEEKM FDTAALAALL KAATGGGSSE
GGNFTITSQD GTKLFSMDRP AGLSSSLRPL KPAAAPRANR SNIFSNSNVT MADETEINLS
EEEKQKLEKL QSLRVKFLRL LQRLGHSAED SIAAQVLYRL ALLAGRQAGQ LFSLDAAKKK
AVESEAEGNE ELIFSLNILV LGKAGVGKSA TINSILGNQI ASIDAFGLST TSVREISGTV
NGVKITFIDT PGLKSAAMDQ STNAKMLSSV KKVMKKCPPD IVLYVDRLDT QTRDLNNLPL
LRTITASLGT SIWKNAIVTL THAASAPPDG PSGTPLSYDV FVAQCSHIVQ QSIGQAVGDL
RLMNPSLMNP VSLVENHPLC RKNREGVKVL PNGQTWRSQL LLLCYSLKVL SETNSLLRPQ
EPLDHRKVFG FRVRSPPLPY LLSWLLQSRA HPKLPGDQGG DSVDSDIEID DVSDSEQEDG
EDDEYDQLPP FKPLRKTQLA KLSNEQRKAY FEEYDYRVKL LQKKQWREEL KRMKEMKKNG
KKLGESEFGY PGEEDDPENG APAAVPVPLP DMVLPPSFDS DNSAYRYRYL EPTSQLLTRP
VLDTHGWDHD CGYDGVNAEH SLALASRFPA TATVQVTKDK KEFNIHLDSS VSAKHGENGS
TMAGFDIQNV GKQLAYVVRG ETKFKNLRKN KTTVGGSVTF LGENIATGVK LEDQIALGKR
LVLVGSTGTM RSQGDSAYGA NLEVRLREAD FPIGQDQSSF GLSLVKWRGD LALGANLQSQ
VSVGRNSKIA LRAGLNNKMS GQITVRTSSS DQLQIALTAI LPIAMSIYKS IRPEATNDKY
SMY
