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O81283 (TC159_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translocase of chloroplast 159, chloroplastic

Short name=AtToc159
EC=3.6.5.-
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 names
Name:TOC159
Synonyms:PPI2, TOC160, TOC86
Ordered Locus Names:At4g02510
ORF Names:T10P11.19, T14P8.24
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8 Ref.12 Ref.13 Ref.14

Cofactor

Binds 1 magnesium ion by subunit By similarity.

Subunit structure

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). Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13

Developmental stage

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

Induction

By light conditions. Ref.5 Ref.13

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. TOC159 subfamily.

Contains 1 AIG1-type G (guanine nucleotide-binding) domain.

Biophysicochemical properties

Kinetic parameters:

KM=21.2 µM for GTP (at pH 7.6 and 25 degrees Celsius) Ref.15

Sequence caution

The sequence AAC78265.2 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAL06516.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB80744.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentChloroplast
Cytoplasm
Membrane
Plastid
Plastid outer membrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
Receptor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Traceable author statement PubMed 18487635. Source: GOC

protein targeting to chloroplast

Inferred from direct assay Ref.5. Source: TAIR

signal transduction

Inferred from direct assay Ref.5. Source: GOC

   Cellular_componentchloroplast

Inferred from direct assay Ref.11PubMed 18431481. Source: TAIR

chloroplast envelope

Inferred from direct assay Ref.10Ref.9PubMed 20061580. Source: TAIR

chloroplast outer membrane

Inferred from direct assay Ref.5. Source: TAIR

cytosol

Inferred from direct assay Ref.16. Source: TAIR

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

plastid

Inferred from direct assay PubMed 22923678. Source: TAIR

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Traceable author statement PubMed 18487635. Source: TAIR

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 14765117PubMed 23118188. Source: IntAct

transmembrane signaling receptor activity

Inferred from direct assay Ref.5. Source: TAIR

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

At1g63890Q8L7N42EBI-639063,EBI-6559199
RBCSP692495EBI-639063,EBI-1766821From a different organism.
TOC34Q389065EBI-639063,EBI-1766808

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15031503Translocase of chloroplast 159, chloroplastic
PRO_0000352659

Regions

Transmembrane21 – 3717Helical; Potential
Domain853 – 1087235AIG1-type G
Nucleotide binding865 – 8706GTP By similarity
Nucleotide binding884 – 8896GTP By similarity
Nucleotide binding1035 – 10362GTP By similarity
Region884 – 8874Homodimerization By similarity
Region947 – 9526Homodimerization By similarity
Coiled coil781 – 80424 Potential
Coiled coil1175 – 120329 Potential

Sites

Metal binding8691Magnesium By similarity
Binding site9821GTP; via amide nitrogen By similarity

Amino acid modifications

Modified residue711Phosphoserine Ref.16 Ref.18
Modified residue2101Phosphoserine Ref.18
Modified residue2811Phosphoserine Ref.18
Modified residue2881Phosphoserine Ref.18
Modified residue4481Phosphoserine Ref.18
Modified residue4611Phosphoserine By similarity
Modified residue5891Phosphoserine Ref.17 Ref.18
Modified residue6091Phosphoserine Ref.18
Modified residue6301Phosphoserine Ref.18
Modified residue6321Phosphoserine Ref.18
Modified residue6651Phosphoserine Ref.17

Experimental info

Mutagenesis8641A → R: Reduced GTPase activity and impaired chloroplast outer membrane anchoring. Ref.6
Mutagenesis8681K → R: Loss of GTPase activity and impaired chloroplast outer membrane anchoring. Ref.6 Ref.8
Sequence conflict8151Q → L in BAD95269. Ref.4
Sequence conflict9141K → E in BAD95269. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O81283 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 04AEDE84C1BED3F6

FASTA1,503160,819
        10         20         30         40         50         60 
MDSKSVTPEP TNPFYASSGQ SGKTYASVVA AAAAAAADKE DGGAVSSAKE LDSSSEAVSG 

        70         80         90        100        110        120 
NSDKVGADDL SDSEKEKPNL VGDGKVSDEV DGSLKEDSTT PEATPKPEVV SGETIGVDDV 

       130        140        150        160        170        180 
SSLSPKPEAV SDGVGVVEEN KKVKEDVEDI KDDGESKIEN GSVDVDVKQA STDGESESKV 

       190        200        210        220        230        240 
KDVEEEDVGT KKDDEGESEL GGKVDVDDKS DNVIEEEGVE LTDKGDVIVN SSPVESVHVD 

       250        260        270        280        290        300 
VAKPGVVVVG DAEGSEELKI NADAETLEVA NKFDQIGDDD SGEFEPVSDK AIEEVEEKFT 

       310        320        330        340        350        360 
SESDSIADSS KLESVDTSAV EPEVVAAESG SEPKDVEKAN GLEKGMTYAE VIKAASAVAD 

       370        380        390        400        410        420 
NGTKEEESVL GGIVDDAEEG VKLNNKGDFV VDSSAIEAVN VDVAKPGVVV VGDVEVSEVL 

       430        440        450        460        470        480 
ETDGNIPDVH NKFDPIGQGE GGEVELESDK ATEEGGGKLV SEGDSMVDSS VVDSVDADIN 

       490        500        510        520        530        540 
VAEPGVVVVG AAKEAVIKED DKDDEVDKTI SNIEEPDDLT AAYDGNFELA VKEISEAAKV 

       550        560        570        580        590        600 
EPDEPKVGVE VEELPVSESL KVGSVDAEED SIPAAESQFE VRKVVEGDSA EEDENKLPVE 

       610        620        630        640        650        660 
DIVSSREFSF GGKEVDQEPS GEGVTRVDGS ESEEETEEMI FGSSEAAKQF LAELEKASSG 

       670        680        690        700        710        720 
IEAHSDEANI SNNMSDRIDG QIVTDSDEDV DTEDEGEEKM FDTAALAALL KAATGGGSSE 

       730        740        750        760        770        780 
GGNFTITSQD GTKLFSMDRP AGLSSSLRPL KPAAAPRANR SNIFSNSNVT MADETEINLS 

       790        800        810        820        830        840 
EEEKQKLEKL QSLRVKFLRL LQRLGHSAED SIAAQVLYRL ALLAGRQAGQ LFSLDAAKKK 

       850        860        870        880        890        900 
AVESEAEGNE ELIFSLNILV LGKAGVGKSA TINSILGNQI ASIDAFGLST TSVREISGTV 

       910        920        930        940        950        960 
NGVKITFIDT PGLKSAAMDQ STNAKMLSSV KKVMKKCPPD IVLYVDRLDT QTRDLNNLPL 

       970        980        990       1000       1010       1020 
LRTITASLGT SIWKNAIVTL THAASAPPDG PSGTPLSYDV FVAQCSHIVQ QSIGQAVGDL 

      1030       1040       1050       1060       1070       1080 
RLMNPSLMNP VSLVENHPLC RKNREGVKVL PNGQTWRSQL LLLCYSLKVL SETNSLLRPQ 

      1090       1100       1110       1120       1130       1140 
EPLDHRKVFG FRVRSPPLPY LLSWLLQSRA HPKLPGDQGG DSVDSDIEID DVSDSEQEDG 

      1150       1160       1170       1180       1190       1200 
EDDEYDQLPP FKPLRKTQLA KLSNEQRKAY FEEYDYRVKL LQKKQWREEL KRMKEMKKNG 

      1210       1220       1230       1240       1250       1260 
KKLGESEFGY PGEEDDPENG APAAVPVPLP DMVLPPSFDS DNSAYRYRYL EPTSQLLTRP 

      1270       1280       1290       1300       1310       1320 
VLDTHGWDHD CGYDGVNAEH SLALASRFPA TATVQVTKDK KEFNIHLDSS VSAKHGENGS 

      1330       1340       1350       1360       1370       1380 
TMAGFDIQNV GKQLAYVVRG ETKFKNLRKN KTTVGGSVTF LGENIATGVK LEDQIALGKR 

      1390       1400       1410       1420       1430       1440 
LVLVGSTGTM RSQGDSAYGA NLEVRLREAD FPIGQDQSSF GLSLVKWRGD LALGANLQSQ 

      1450       1460       1470       1480       1490       1500 
VSVGRNSKIA LRAGLNNKMS GQITVRTSSS DQLQIALTAI LPIAMSIYKS IRPEATNDKY 


SMY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis."
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.
J. Proteome Res. 7:2458-2470(2008) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA85032.
T01098.
RefSeqNP_567242.2. NM_116485.3.
UniGeneAt.24962.

3D structure databases

DisProtDP00609.
ProteinModelPortalO81283.
SMRO81283. Positions 836-1061.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13225. 7 interactions.
IntActO81283. 15 interactions.

Proteomic databases

PaxDbO81283.
PRIDEO81283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02510.1; AT4G02510.1; AT4G02510.
GeneID827934.
KEGGath:AT4G02510.

Organism-specific databases

TAIRAT4G02510.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000243570.
InParanoidO81283.
OMASDEANIS.
PhylomeDBO81283.

Gene expression databases

GenevestigatorO81283.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR006703. AIG1.
IPR024283. DUF3406_chlpt_translocase.
IPR027417. P-loop_NTPase.
IPR005690. Toc86_159.
[Graphical view]
PfamPF04548. AIG1. 1 hit.
PF11886. DUF3406. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00993. 3a0901s04IAP86. 1 hit.
PROSITEPS51720. G_AIG1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTC159_ARATH
AccessionPrimary (citable) accession number: O81283
Secondary accession number(s): O22774, Q56W83, Q945M4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names