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Protein

Translocase of chloroplast 159, chloroplastic

Gene

TOC159

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase involved in protein precursor import into chloroplasts. Seems to recognize chloroplast-destined precursor proteins and regulate their presentation to the translocation channel through GTP hydrolysis. Required for chloroplast biogenesis. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast.6 Publications

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion by subunit.By similarity

Kineticsi

  1. KM=21.2 µM for GTP (at pH 7.6 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi869 – 8691MagnesiumBy similarity
    Binding sitei982 – 9821GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi865 – 8706GTPBy similarity
    Nucleotide bindingi884 – 8896GTPBy similarity
    Nucleotide bindingi1035 – 10362GTPBy similarity

    GO - Molecular functioni

    • GTPase activity Source: TAIR
    • GTP binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • transmembrane signaling receptor activity Source: TAIR

    GO - Biological processi

    • metabolic process Source: GOC
    • protein targeting to chloroplast Source: TAIR
    • signal transduction Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Receptor

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translocase of chloroplast 159, chloroplastic (EC:3.6.5.-)
    Short name:
    AtToc159
    Alternative name(s):
    159 kDa chloroplast outer envelope protein
    Plastid protein import 2
    Translocase of chloroplast 160, chloroplastic
    Short name:
    AtToc160
    Translocase of chloroplast 86, chloroplastic
    Short name:
    AtToc86
    Gene namesi
    Name:TOC159
    Synonyms:PPI2, TOC160, TOC86
    Ordered Locus Names:At4g02510
    ORF Names:T10P11.19, T14P8.24
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G02510.

    Subcellular locationi

    • Plastidchloroplast outer membrane; Single-pass membrane protein
    • Cytoplasm

    • Note: Cycles between the cytoplasm and chloroplast, probably as a soluble preprotein receptor. The anchoring to the chloroplast outer membrane required the GTPase activity and GDP, and is dependent of interactions with TOC33 as well as TOC34 and TOC75. May contain beta barrel transmembrane regions.

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 3717HelicalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast envelope Source: TAIR
    • chloroplast outer membrane Source: TAIR
    • cytosol Source: TAIR
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: TAIR
    • plastid Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Cytoplasm, Membrane, Plastid, Plastid outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi864 – 8641A → R: Reduced GTPase activity and impaired chloroplast outer membrane anchoring. 1 Publication
    Mutagenesisi868 – 8681K → R: Loss of GTPase activity and impaired chloroplast outer membrane anchoring. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15031503Translocase of chloroplast 159, chloroplasticPRO_0000352659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711Phosphoserine2 Publications
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei281 – 2811Phosphoserine1 Publication
    Modified residuei288 – 2881Phosphoserine1 Publication
    Modified residuei448 – 4481Phosphoserine1 Publication
    Modified residuei461 – 4611PhosphoserineBy similarity
    Modified residuei589 – 5891Phosphoserine2 Publications
    Modified residuei609 – 6091Phosphoserine1 Publication
    Modified residuei630 – 6301Phosphoserine1 Publication
    Modified residuei632 – 6321Phosphoserine1 Publication
    Modified residuei665 – 6651Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiO81283.
    PRIDEiO81283.

    Expressioni

    Developmental stagei

    Mostly expressed in seedlings, and, to a lower extent, in leaves and flowers.

    Inductioni

    By light conditions.2 Publications

    Interactioni

    Subunit structurei

    Homodimer and heterodimer with TOC33. Part of the TOC core complex that includes 1 protein for the specific recognition of transit peptides surrounded by a ring composed of four proteins forming translocation channels, and four to five GTP-binding proteins providing energy. This core complex can interact with components of the TIC complex to form a larger import complex. Chloroplastic protein precursor such as prSS (precursor of the RuBisCO small subunit) interacts with these complexes. The TOC complex contains a specific subset of polar lipids such as digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC) and phosphatidylglycerol (PG).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    At1g63890Q8L7N42EBI-639063,EBI-6559199
    RBCSP692495EBI-639063,EBI-1766821From a different organism.
    TOC34Q389065EBI-639063,EBI-1766808

    Protein-protein interaction databases

    BioGridi13225. 7 interactions.
    IntActiO81283. 15 interactions.
    STRINGi3702.AT4G02510.1.

    Structurei

    3D structure databases

    DisProtiDP00609.
    ProteinModelPortaliO81283.
    SMRiO81283. Positions 836-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini853 – 1087235AIG1-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni884 – 8874HomodimerizationBy similarity
    Regioni947 – 9526HomodimerizationBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili781 – 80424Sequence AnalysisAdd
    BLAST
    Coiled coili1175 – 120329Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000243570.
    InParanoidiO81283.
    OMAiSDEANIS.
    PhylomeDBiO81283.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR024283. DUF3406_chlpt_translocase.
    IPR006703. G_AIG1.
    IPR027417. P-loop_NTPase.
    IPR005690. Toc86_159.
    [Graphical view]
    PfamiPF04548. AIG1. 1 hit.
    PF11886. DUF3406. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00993. 3a0901s04IAP86. 1 hit.
    PROSITEiPS51720. G_AIG1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O81283-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDSKSVTPEP TNPFYASSGQ SGKTYASVVA AAAAAAADKE DGGAVSSAKE
    60 70 80 90 100
    LDSSSEAVSG NSDKVGADDL SDSEKEKPNL VGDGKVSDEV DGSLKEDSTT
    110 120 130 140 150
    PEATPKPEVV SGETIGVDDV SSLSPKPEAV SDGVGVVEEN KKVKEDVEDI
    160 170 180 190 200
    KDDGESKIEN GSVDVDVKQA STDGESESKV KDVEEEDVGT KKDDEGESEL
    210 220 230 240 250
    GGKVDVDDKS DNVIEEEGVE LTDKGDVIVN SSPVESVHVD VAKPGVVVVG
    260 270 280 290 300
    DAEGSEELKI NADAETLEVA NKFDQIGDDD SGEFEPVSDK AIEEVEEKFT
    310 320 330 340 350
    SESDSIADSS KLESVDTSAV EPEVVAAESG SEPKDVEKAN GLEKGMTYAE
    360 370 380 390 400
    VIKAASAVAD NGTKEEESVL GGIVDDAEEG VKLNNKGDFV VDSSAIEAVN
    410 420 430 440 450
    VDVAKPGVVV VGDVEVSEVL ETDGNIPDVH NKFDPIGQGE GGEVELESDK
    460 470 480 490 500
    ATEEGGGKLV SEGDSMVDSS VVDSVDADIN VAEPGVVVVG AAKEAVIKED
    510 520 530 540 550
    DKDDEVDKTI SNIEEPDDLT AAYDGNFELA VKEISEAAKV EPDEPKVGVE
    560 570 580 590 600
    VEELPVSESL KVGSVDAEED SIPAAESQFE VRKVVEGDSA EEDENKLPVE
    610 620 630 640 650
    DIVSSREFSF GGKEVDQEPS GEGVTRVDGS ESEEETEEMI FGSSEAAKQF
    660 670 680 690 700
    LAELEKASSG IEAHSDEANI SNNMSDRIDG QIVTDSDEDV DTEDEGEEKM
    710 720 730 740 750
    FDTAALAALL KAATGGGSSE GGNFTITSQD GTKLFSMDRP AGLSSSLRPL
    760 770 780 790 800
    KPAAAPRANR SNIFSNSNVT MADETEINLS EEEKQKLEKL QSLRVKFLRL
    810 820 830 840 850
    LQRLGHSAED SIAAQVLYRL ALLAGRQAGQ LFSLDAAKKK AVESEAEGNE
    860 870 880 890 900
    ELIFSLNILV LGKAGVGKSA TINSILGNQI ASIDAFGLST TSVREISGTV
    910 920 930 940 950
    NGVKITFIDT PGLKSAAMDQ STNAKMLSSV KKVMKKCPPD IVLYVDRLDT
    960 970 980 990 1000
    QTRDLNNLPL LRTITASLGT SIWKNAIVTL THAASAPPDG PSGTPLSYDV
    1010 1020 1030 1040 1050
    FVAQCSHIVQ QSIGQAVGDL RLMNPSLMNP VSLVENHPLC RKNREGVKVL
    1060 1070 1080 1090 1100
    PNGQTWRSQL LLLCYSLKVL SETNSLLRPQ EPLDHRKVFG FRVRSPPLPY
    1110 1120 1130 1140 1150
    LLSWLLQSRA HPKLPGDQGG DSVDSDIEID DVSDSEQEDG EDDEYDQLPP
    1160 1170 1180 1190 1200
    FKPLRKTQLA KLSNEQRKAY FEEYDYRVKL LQKKQWREEL KRMKEMKKNG
    1210 1220 1230 1240 1250
    KKLGESEFGY PGEEDDPENG APAAVPVPLP DMVLPPSFDS DNSAYRYRYL
    1260 1270 1280 1290 1300
    EPTSQLLTRP VLDTHGWDHD CGYDGVNAEH SLALASRFPA TATVQVTKDK
    1310 1320 1330 1340 1350
    KEFNIHLDSS VSAKHGENGS TMAGFDIQNV GKQLAYVVRG ETKFKNLRKN
    1360 1370 1380 1390 1400
    KTTVGGSVTF LGENIATGVK LEDQIALGKR LVLVGSTGTM RSQGDSAYGA
    1410 1420 1430 1440 1450
    NLEVRLREAD FPIGQDQSSF GLSLVKWRGD LALGANLQSQ VSVGRNSKIA
    1460 1470 1480 1490 1500
    LRAGLNNKMS GQITVRTSSS DQLQIALTAI LPIAMSIYKS IRPEATNDKY

    SMY
    Length:1,503
    Mass (Da):160,819
    Last modified:November 1, 1998 - v1
    Checksum:i04AEDE84C1BED3F6
    GO

    Sequence cautioni

    The sequence AAC78265.2 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence AAL06516.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence CAB80744.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti815 – 8151Q → L in BAD95269 (Ref. 4) Curated
    Sequence conflicti914 – 9141K → E in BAD95269 (Ref. 4) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC002330 Genomic DNA. Translation: AAC78265.2. Sequence problems.
    AF069298 Genomic DNA. Translation: AAC19285.1.
    AL161494 Genomic DNA. Translation: CAB80744.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82182.1.
    AF412063 mRNA. Translation: AAL06516.1. Different initiation.
    AY133653 mRNA. Translation: AAM91483.1.
    AK222164 mRNA. Translation: BAD95269.1.
    PIRiA85032.
    T01098.
    RefSeqiNP_567242.2. NM_116485.3.
    UniGeneiAt.24962.

    Genome annotation databases

    EnsemblPlantsiAT4G02510.1; AT4G02510.1; AT4G02510.
    GeneIDi827934.
    KEGGiath:AT4G02510.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC002330 Genomic DNA. Translation: AAC78265.2. Sequence problems.
    AF069298 Genomic DNA. Translation: AAC19285.1.
    AL161494 Genomic DNA. Translation: CAB80744.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82182.1.
    AF412063 mRNA. Translation: AAL06516.1. Different initiation.
    AY133653 mRNA. Translation: AAM91483.1.
    AK222164 mRNA. Translation: BAD95269.1.
    PIRiA85032.
    T01098.
    RefSeqiNP_567242.2. NM_116485.3.
    UniGeneiAt.24962.

    3D structure databases

    DisProtiDP00609.
    ProteinModelPortaliO81283.
    SMRiO81283. Positions 836-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi13225. 7 interactions.
    IntActiO81283. 15 interactions.
    STRINGi3702.AT4G02510.1.

    Proteomic databases

    PaxDbiO81283.
    PRIDEiO81283.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G02510.1; AT4G02510.1; AT4G02510.
    GeneIDi827934.
    KEGGiath:AT4G02510.

    Organism-specific databases

    TAIRiAT4G02510.

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000243570.
    InParanoidiO81283.
    OMAiSDEANIS.
    PhylomeDBiO81283.

    Miscellaneous databases

    PROiO81283.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR024283. DUF3406_chlpt_translocase.
    IPR006703. G_AIG1.
    IPR027417. P-loop_NTPase.
    IPR005690. Toc86_159.
    [Graphical view]
    PfamiPF04548. AIG1. 1 hit.
    PF11886. DUF3406. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00993. 3a0901s04IAP86. 1 hit.
    PROSITEiPS51720. G_AIG1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1004-1503.
      Strain: cv. Columbia.
    4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 815-1503.
      Strain: cv. Columbia.
    5. "The major protein import receptor of plastids is essential for chloroplast biogenesis."
      Bauer J., Chen K., Hiltbunner A., Wehrli E., Eugster M., Schnell D., Kessler F.
      Nature 403:203-207(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH THE TOC COMPLEX, INDUCTION BY LIGHT.
    6. "The targeting of the atToc159 preprotein receptor to the chloroplast outer membrane is mediated by its GTPase domain and is regulated by GTP."
      Smith M.D., Hiltbrunner A., Kessler F., Schnell D.J.
      J. Cell Biol. 159:833-843(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOC33, MUTAGENESIS OF ALA-864 AND LYS-868, SUBCELLULAR LOCATION.
    7. "Dimerization of Toc-GTPases at the chloroplast protein import machinery."
      Weibel P., Hiltbrunner A., Brand L., Kessler F.
      J. Biol. Chem. 278:37321-37329(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DIMERIZATION WITH TOC33.
    8. "The roles of Toc34 and Toc75 in targeting the Toc159 preprotein receptor to chloroplasts."
      Wallas T.R., Smith M.D., Sanchez-Nieto S., Schnell D.J.
      J. Biol. Chem. 278:44289-44297(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-868, SUBCELLULAR LOCATION, INTERACTION WITH TOC33.
    9. "Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis."
      Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S.
      J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
      Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
      Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: cv. Wassilewskija.
    11. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
      Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
      Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors."
      Kubis S., Patel R., Combe J., Bedard J., Kovacheva S., Lilley K., Biehl A., Leister D., Rios G., Koncz C., Jarvis P.
      Plant Cell 16:2059-2077(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "AtToc90, a new GTP-binding component of the Arabidopsis chloroplast protein import machinery."
      Hiltbrunner A., Gruenig K., Alvarez-Huerta M., Infanger S., Bauer J., Kessler F.
      Plant Mol. Biol. 54:427-440(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY LIGHT, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
    14. "Deletion of core components of the plastid protein import machinery causes differential arrest of embryo development in Arabidopsis thaliana."
      Hust B., Gutensohn M.
      Plant Biol. 8:18-30(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "In vitro comparative kinetic analysis of the chloroplast Toc GTPases."
      Reddick L.E., Vaughn M.D., Wright S.J., Campbell I.M., Bruce B.D.
      J. Biol. Chem. 282:11410-11426(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Root.
    17. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
      Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
      J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-665, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    18. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-210; SER-281; SER-288; SER-448; SER-589; SER-609; SER-630 AND SER-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTC159_ARATH
    AccessioniPrimary (citable) accession number: O81283
    Secondary accession number(s): O22774, Q56W83, Q945M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2008
    Last sequence update: November 1, 1998
    Last modified: June 24, 2015
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.