Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9SLF3

- TC132_ARATH

UniProt

Q9SLF3 - TC132_ARATH

(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)

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

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

Mg2+By similarityNote: Binds 1 Mg(2+) 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
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 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

Topology

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

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
Complete GO annotation...

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...

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

        10         20         30         40         50
MGDGTEFVVR SDREDKKLAE DRISDEQVVK NELVRSDEVR DDNEDEVFEE
60 70 80 90 100
AIGSENDEQE EEEDPKRELF ESDDLPLVET LKSSMVEHEV EDFEEAVGDL
110 120 130 140 150
DETSSNEGGV KDFTAVGESH GAGEAEFDVL ATKMNGDKGE GGGGGSYDKV
160 170 180 190 200
ESSLDVVDTT ENATSTNTNG SNLAAEHVGI ENGKTHSFLG NGIASPKNKE
210 220 230 240 250
VVAEVIPKDD GIEEPWNDGI EVDNWEERVD GIQTEQEVEE GEGTTENQFE
260 270 280 290 300
KRTEEEVVEG EGTSKNLFEK QTEQDVVEGE GTSKDLFENG SVCMDSESEA
310 320 330 340 350
ERNGETGAAY TSNIVTNASG DNEVSSAVTS SPLEESSSGE KGETEGDSTC
360 370 380 390 400
LKPEQHLASS PHSYPESTEV HSNSGSPGVT SREHKPVQSA NGGHDVQSPQ
410 420 430 440 450
PNKELEKQQS SRVHVDPEIT ENSHVETEPE VVSSVSPTES RSNPAALPPA
460 470 480 490 500
RPAGLGRASP LLEPASRAPQ QSRVNGNGSH NQFQQAEDST TTEADEHDET
510 520 530 540 550
REKLQLIRVK FLRLAHRLGQ TPHNVVVAQV LYRLGLAEQL RGRNGSRVGA
560 570 580 590 600
FSFDRASAMA EQLEAAGQDP LDFSCTIMVL GKSGVGKSAT INSIFDEVKF
610 620 630 640 650
CTDAFQMGTK RVQDVEGLVQ GIKVRVIDTP GLLPSWSDQA KNEKILNSVK
660 670 680 690 700
AFIKKNPPDI VLYLDRLDMQ SRDSGDMPLL RTISDVFGPS IWFNAIVGLT
710 720 730 740 750
HAASVPPDGP NGTASSYDMF VTQRSHVIQQ AIRQAAGDMR LMNPVSLVEN
760 770 780 790 800
HSACRTNRAG QRVLPNGQVW KPHLLLLSFA SKILAEANAL LKLQDNIPGR
810 820 830 840 850
PFAARSKAPP LPFLLSSLLQ SRPQPKLPEQ QYGDEEDEDD LEESSDSDEE
860 870 880 890 900
SEYDQLPPFK SLTKAQMATL SKSQKKQYLD EMEYREKLLM KKQMKEERKR
910 920 930 940 950
RKMFKKFAAE IKDLPDGYSE NVEEESGGPA SVPVPMPDLS LPASFDSDNP
960 970 980 990 1000
THRYRYLDSS NQWLVRPVLE THGWDHDIGY EGVNAERLFV VKEKIPISVS
1010 1020 1030 1040 1050
GQVTKDKKDA NVQLEMASSV KHGEGKSTSL GFDMQTVGKE LAYTLRSETR
1060 1070 1080 1090 1100
FNNFRRNKAA AGLSVTHLGD SVSAGLKVED KFIASKWFRI VMSGGAMTSR
1110 1120 1130 1140 1150
GDFAYGGTLE AQLRDKDYPL GRFLTTLGLS VMDWHGDLAI GGNIQSQVPI
1160 1170 1180 1190 1200
GRSSNLIARA NLNNRGAGQV SVRVNSSEQL QLAMVAIVPL FKKLLSYYYP

QTQYGQ
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.Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 72 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