Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SLF3

- TC132_ARATH

UniProt

Q9SLF3 - TC132_ARATH

Protein

Translocase of chloroplast 132, chloroplastic

Gene

TOC132

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Probably specialized in the import of nuclear encoded non-photosynthetic preproteins from the cytoplasm to the chloroplast.2 Publications

    Cofactori

    Binds 1 magnesium ion by subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi588 – 5881MagnesiumBy similarity
    Binding sitei701 – 7011GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi584 – 5896GTPBy similarity
    Nucleotide bindingi603 – 6086GTPBy similarity
    Nucleotide bindingi749 – 7502GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. hydrolase activity, acting on acid anhydrides Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. transmembrane signaling receptor activity Source: TAIR

    GO - Biological processi

    1. protein targeting to chloroplast Source: TAIR
    2. signal transduction Source: GOC

    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 132, chloroplastic (EC:3.6.5.-)
    Short name:
    AtToc132
    Alternative name(s):
    132 kDa chloroplast outer envelope protein
    Gene namesi
    Name:TOC132
    Ordered Locus Names:At2g16640
    ORF Names:T24I21.5
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G16640.

    Subcellular locationi

    Plastidchloroplast outer membrane By similarity; Single-pass membrane protein By similarity. Cytoplasm By similarity
    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. May contains beta barrel transmembrane regions By similarity.By similarity

    GO - Cellular componenti

    1. chloroplast outer membrane Source: TAIR
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: TAIR
    4. plastid Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Cytoplasm, Membrane, Plastid, Plastid outer membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 12061205Translocase of chloroplast 132, chloroplasticPRO_0000352658Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycine1 Publication
    Modified residuei195 – 1951Phosphoserine1 Publication
    Modified residuei337 – 3371PhosphoserineBy similarity
    Modified residuei363 – 3631PhosphoserineBy similarity
    Modified residuei398 – 3981PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9SLF3.
    PRIDEiQ9SLF3.

    Expressioni

    Tissue specificityi

    Expressed in seedlings, leaves, flowers, and roots.1 Publication

    Inductioni

    By light conditions.1 Publication

    Gene expression databases

    GenevestigatoriQ9SLF3.

    Interactioni

    Subunit structurei

    Homodimer By similarity. 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).By similarity1 Publication

    Protein-protein interaction databases

    BioGridi1522. 3 interactions.
    IntActiQ9SLF3. 5 interactions.

    Structurei

    3D structure databases

    DisProtiDP00610.
    ProteinModelPortaliQ9SLF3.
    SMRiQ9SLF3. Positions 543-775.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1182 – 119918HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini572 – 801230AIG1-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni603 – 6064HomodimerizationBy similarity
    Regioni666 – 6716HomodimerizationBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili13 – 3321Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi44 – 305262Glu-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG244338.
    HOGENOMiHOG000243570.
    InParanoidiQ9SLF3.
    OMAiIENGKTH.
    PhylomeDBiQ9SLF3.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR006703. AIG1.
    IPR024283. DUF3406_chlpt_translocase.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SLF3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDGTEFVVR SDREDKKLAE DRISDEQVVK NELVRSDEVR DDNEDEVFEE     50
    AIGSENDEQE EEEDPKRELF ESDDLPLVET LKSSMVEHEV EDFEEAVGDL 100
    DETSSNEGGV KDFTAVGESH GAGEAEFDVL ATKMNGDKGE GGGGGSYDKV 150
    ESSLDVVDTT ENATSTNTNG SNLAAEHVGI ENGKTHSFLG NGIASPKNKE 200
    VVAEVIPKDD GIEEPWNDGI EVDNWEERVD GIQTEQEVEE GEGTTENQFE 250
    KRTEEEVVEG EGTSKNLFEK QTEQDVVEGE GTSKDLFENG SVCMDSESEA 300
    ERNGETGAAY TSNIVTNASG DNEVSSAVTS SPLEESSSGE KGETEGDSTC 350
    LKPEQHLASS PHSYPESTEV HSNSGSPGVT SREHKPVQSA NGGHDVQSPQ 400
    PNKELEKQQS SRVHVDPEIT ENSHVETEPE VVSSVSPTES RSNPAALPPA 450
    RPAGLGRASP LLEPASRAPQ QSRVNGNGSH NQFQQAEDST TTEADEHDET 500
    REKLQLIRVK FLRLAHRLGQ TPHNVVVAQV LYRLGLAEQL RGRNGSRVGA 550
    FSFDRASAMA EQLEAAGQDP LDFSCTIMVL GKSGVGKSAT INSIFDEVKF 600
    CTDAFQMGTK RVQDVEGLVQ GIKVRVIDTP GLLPSWSDQA KNEKILNSVK 650
    AFIKKNPPDI VLYLDRLDMQ SRDSGDMPLL RTISDVFGPS IWFNAIVGLT 700
    HAASVPPDGP NGTASSYDMF VTQRSHVIQQ AIRQAAGDMR LMNPVSLVEN 750
    HSACRTNRAG QRVLPNGQVW KPHLLLLSFA SKILAEANAL LKLQDNIPGR 800
    PFAARSKAPP LPFLLSSLLQ SRPQPKLPEQ QYGDEEDEDD LEESSDSDEE 850
    SEYDQLPPFK SLTKAQMATL SKSQKKQYLD EMEYREKLLM KKQMKEERKR 900
    RKMFKKFAAE IKDLPDGYSE NVEEESGGPA SVPVPMPDLS LPASFDSDNP 950
    THRYRYLDSS NQWLVRPVLE THGWDHDIGY EGVNAERLFV VKEKIPISVS 1000
    GQVTKDKKDA NVQLEMASSV KHGEGKSTSL GFDMQTVGKE LAYTLRSETR 1050
    FNNFRRNKAA AGLSVTHLGD SVSAGLKVED KFIASKWFRI VMSGGAMTSR 1100
    GDFAYGGTLE AQLRDKDYPL GRFLTTLGLS VMDWHGDLAI GGNIQSQVPI 1150
    GRSSNLIARA NLNNRGAGQV SVRVNSSEQL QLAMVAIVPL FKKLLSYYYP 1200
    QTQYGQ 1206
    Length:1,206
    Mass (Da):132,277
    Last modified:May 1, 2000 - v1
    Checksum:iFEFB80CFC83655B5
    GO

    Sequence cautioni

    The sequence AAM20511.1 differs from that shown. Reason: Erroneous termination at position 1203. Translated as Gln.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101R → G in AAM20511. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC005825 Genomic DNA. Translation: AAD24598.1.
    CP002685 Genomic DNA. Translation: AEC06521.1.
    AY099660 mRNA. Translation: AAM20511.1. Sequence problems.
    AK222043 mRNA. Translation: BAD94786.1.
    PIRiD84542.
    RefSeqiNP_179255.1. NM_127216.4.
    UniGeneiAt.21953.
    At.67099.

    Genome annotation databases

    EnsemblPlantsiAT2G16640.1; AT2G16640.1; AT2G16640.
    GeneIDi816165.
    KEGGiath:AT2G16640.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC005825 Genomic DNA. Translation: AAD24598.1 .
    CP002685 Genomic DNA. Translation: AEC06521.1 .
    AY099660 mRNA. Translation: AAM20511.1 . Sequence problems.
    AK222043 mRNA. Translation: BAD94786.1 .
    PIRi D84542.
    RefSeqi NP_179255.1. NM_127216.4.
    UniGenei At.21953.
    At.67099.

    3D structure databases

    DisProti DP00610.
    ProteinModelPortali Q9SLF3.
    SMRi Q9SLF3. Positions 543-775.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1522. 3 interactions.
    IntActi Q9SLF3. 5 interactions.

    Proteomic databases

    PaxDbi Q9SLF3.
    PRIDEi Q9SLF3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G16640.1 ; AT2G16640.1 ; AT2G16640 .
    GeneIDi 816165.
    KEGGi ath:AT2G16640.

    Organism-specific databases

    TAIRi AT2G16640.

    Phylogenomic databases

    eggNOGi NOG244338.
    HOGENOMi HOG000243570.
    InParanoidi Q9SLF3.
    OMAi IENGKTH.
    PhylomeDBi Q9SLF3.

    Gene expression databases

    Genevestigatori Q9SLF3.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR006703. AIG1.
    IPR024283. DUF3406_chlpt_translocase.
    IPR027417. P-loop_NTPase.
    IPR005690. Toc86_159.
    [Graphical view ]
    Pfami PF04548. AIG1. 1 hit.
    PF11886. DUF3406. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00993. 3a0901s04IAP86. 1 hit.
    PROSITEi PS51720. G_AIG1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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].
      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 728-1206.
      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: INTERACTION WITH THE TOC COMPLEX, INDUCTION BY LIGHT.
    6. "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.
    7. "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.
    8. "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-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: cv. Columbia.
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTC132_ARATH
    AccessioniPrimary (citable) accession number: Q9SLF3
    Secondary accession number(s): Q56WJ7, Q8LPK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2008
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 71 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