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Protein

Translocase of chloroplast 33, chloroplastic

Gene

TOC33

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. Binds GTP, GDP, XTP, but not ATP. Probably specialized in the import of nuclear encoded photosynthetic preproteins from the cytoplasm to the chloroplast, especially during early development stages.10 Publications

Cofactori

Mg2+3 PublicationsNote: Binds 1 Mg2+ ion by subunit.3 Publications

Kineticsi

  1. KM=290 nM for GDP (at pH 7.4)2 Publications
  2. KM=5.7 µM for GTP (at pH 7.6 and 25 degrees Celsius)2 Publications
  1. Vmax=1040 nmol/min/µg enzyme with GTP as substrate (at pH 7.4)2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Magnesium3 Publications1
Metal bindingi68Magnesium3 Publications1
Binding sitei160GTP; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi46 – 51GTPCombined sources1 Publication6
Nucleotide bindingi65 – 70GTP1 Publication6
Nucleotide bindingi208 – 209GTPCombined sources1 Publication2

GO - Molecular functioni

  • GTPase activity Source: TAIR
  • GTP binding Source: TAIR
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro
  • protein homodimerization activity Source: TAIR

GO - Biological processi

  • protein targeting to chloroplast Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Receptor

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciARA:AT1G02280-MONOMER.
BRENDAi3.6.5.2. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocase of chloroplast 33, chloroplastic (EC:3.6.5.-)
Short name:
AtToc33
Alternative name(s):
33 kDa chloroplast outer envelope protein
Plastid protein import 1
Gene namesi
Name:TOC33
Synonyms:PPI1
Ordered Locus Names:At1g02280
ORF Names:T7I23.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G02280.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei37 – 53HelicalSequence analysisAdd BLAST17

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Plastid outer membrane

Pathology & Biotechi

Disruption phenotypei

Plants exhibits a pale yellowish phenotype.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45 – 50GGVGKS → RGVGNR: Reduced GTPase activity and impaired interaction with TOC159. 1 Publication6
Mutagenesisi130R → A: Loss of homidimerization and heterodimerization with TOC159, reduction of GTPase activity. 3 Publications1
Mutagenesisi170S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi175S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi181S → A: Loss of phosphorylation, normal activity. 2 Publications1
Mutagenesisi181S → D or E: According to PubMed:16412428, supposed to mimic the effects of phosphoserine, but normal activity. 2 Publications1
Mutagenesisi181S → T: Phosphothreonine instead of phosphoserine. 2 Publications1
Mutagenesisi190S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi200S → A: Normal phosphorylation. 1 Publication1
Mutagenesisi208E → Q: Normal GTPase activity, but weaker nucleotide binding. 1 Publication1
Mutagenesisi217D → N: Normal GTPase activity. 1 Publication1
Mutagenesisi219D → N: Normal GTPase activity. 1 Publication1
Mutagenesisi220E → Q: Normal GTPase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003526552 – 297Translocase of chloroplast 33, chloroplasticAdd BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei181Phosphoserine3 Publications1

Post-translational modificationi

Phosphorylated by a kinase present in the outer envelope of chloroplast. When Ser-181 is phosphorylated, the binding to preprotein, GTP and GDP is inhibited, and thus, GTPase activity is repressed.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO23680.

PTM databases

iPTMnetiO23680.

Expressioni

Tissue specificityi

Mostly expressed in seedlings and flowers, and, to a lower extent, in roots, stems, and leaves.2 Publications

Developmental stagei

Mostly expressed in photosynthetic tissues undergoing rapid growth. Observed in cotyledons and vascular tissues of hypocotyls of young seedling. In roots, restricted to apical and lateral meristems, and vascular bundles. In stems, mostly detected in the upper part. Expressed in young and middle-aged leaves. In flowers, confined to sepals.2 Publications

Inductioni

Up-regulated by CIA2 in leaves. Induced in light but repressed in darkness.2 Publications

Gene expression databases

GenevisibleiO23680. AT.

Interactioni

Subunit structurei

Homodimer, heterodimer with TOC34 and TOC159, and monomer. The homodimerization and the dimerization with TOC159 require the binding of GTP on Arg-130, and a hypothetical coGAP factor. The dimeric form has a higher GTPase activity than the monomeric form. 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). Interacts at least with TOC75-3. Forms large complexes including TOC33, pPORA and OEP161 during pPORA import into plastids at the plastid envelope membrane (PubMed:10998188, PubMed:12473690, PubMed:12951325, PubMed:15773849, PubMed:17337454, PubMed:18400179, PubMed:18541539). Interacts with SP1 (PubMed:23118188).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-639377,EBI-639377
CPK11Q390164EBI-639377,EBI-979321
CPK4Q388695EBI-639377,EBI-979475
SP1Q8L7N42EBI-639377,EBI-6559199

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi24483. 8 interactors.
IntActiO23680. 8 interactors.
STRINGi3702.AT1G02280.1.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Helixi16 – 31Combined sources16
Beta strandi36 – 43Combined sources8
Helixi49 – 57Combined sources9
Beta strandi58 – 60Combined sources3
Beta strandi75 – 81Combined sources7
Beta strandi84 – 90Combined sources7
Beta strandi94 – 96Combined sources3
Beta strandi97 – 100Combined sources4
Helixi102 – 111Combined sources10
Turni112 – 114Combined sources3
Beta strandi119 – 127Combined sources9
Helixi133 – 146Combined sources14
Helixi148 – 153Combined sources6
Beta strandi154 – 159Combined sources6
Helixi171 – 190Combined sources20
Helixi191 – 193Combined sources3
Helixi194 – 200Combined sources7
Beta strandi203 – 206Combined sources4
Beta strandi224 – 228Combined sources5
Helixi229 – 241Combined sources13
Beta strandi243 – 245Combined sources3
Beta strandi248 – 250Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J3EX-ray3.20A2-250[»]
3BB3X-ray2.94A1-251[»]
3BB4X-ray2.85A1-251[»]
3DEFX-ray1.96A1-251[»]
ProteinModelPortaliO23680.
SMRiO23680.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO23680.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 259AIG1-type GAdd BLAST226

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni65 – 68Homodimerization1 Publication4
Regioni125 – 130Homodimerization1 Publication6

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IERB. Eukaryota.
ENOG410ZHTP. LUCA.
HOGENOMiHOG000264764.
InParanoidiO23680.
OMAiFPAATQE.
OrthoDBiEOG09360FPG.
PhylomeDBiO23680.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006703. G_AIG1.
IPR027417. P-loop_NTPase.
IPR005688. Toc34.
[Graphical view]
PfamiPF04548. AIG1. 1 hit.
[Graphical view]
PIRSFiPIRSF038134. Toc34. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00991. 3a0901s02IAP34. 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.

O23680-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSLVREWVG FQQFPAATQE KLIEFFGKLK QKDMNSMTVL VLGKGGVGKS
60 70 80 90 100
STVNSLIGEQ VVRVSPFQAE GLRPVMVSRT MGGFTINIID TPGLVEAGYV
110 120 130 140 150
NHQALELIKG FLVNRTIDVL LYVDRLDVYR VDELDKQVVI AITQTFGKEI
160 170 180 190 200
WCKTLLVLTH AQFSPPDELS YETFSSKRSD SLLKTIRAGS KMRKQEFEDS
210 220 230 240 250
AIAVVYAENS GRCSKNDKDE KALPNGEAWI PNLVKAITDV ATNQRKAIHV
260 270 280 290
DKKMVDGSYS DDKGKKLIPL IIGAQYLIVK MIQGAIRNDI KTSGKPL
Length:297
Mass (Da):32,925
Last modified:January 1, 1998 - v1
Checksum:iE48892E123BA412D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti147G → A in AAK68809 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010724 mRNA. Translation: CAC17698.1.
U89959 Genomic DNA. Translation: AAC24375.1.
CP002684 Genomic DNA. Translation: AEE27409.1.
CP002684 Genomic DNA. Translation: AEE27410.1.
AY042869 mRNA. Translation: AAK68809.1.
AY056448 mRNA. Translation: AAL08304.1.
BT025654 mRNA. Translation: ABF74715.1.
RefSeqiNP_001117215.1. NM_001123743.2.
NP_171730.1. NM_100108.5.
UniGeneiAt.10710.

Genome annotation databases

EnsemblPlantsiAT1G02280.1; AT1G02280.1; AT1G02280.
AT1G02280.2; AT1G02280.2; AT1G02280.
GeneIDi839248.
GrameneiAT1G02280.1; AT1G02280.1; AT1G02280.
AT1G02280.2; AT1G02280.2; AT1G02280.
KEGGiath:AT1G02280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010724 mRNA. Translation: CAC17698.1.
U89959 Genomic DNA. Translation: AAC24375.1.
CP002684 Genomic DNA. Translation: AEE27409.1.
CP002684 Genomic DNA. Translation: AEE27410.1.
AY042869 mRNA. Translation: AAK68809.1.
AY056448 mRNA. Translation: AAL08304.1.
BT025654 mRNA. Translation: ABF74715.1.
RefSeqiNP_001117215.1. NM_001123743.2.
NP_171730.1. NM_100108.5.
UniGeneiAt.10710.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J3EX-ray3.20A2-250[»]
3BB3X-ray2.94A1-251[»]
3BB4X-ray2.85A1-251[»]
3DEFX-ray1.96A1-251[»]
ProteinModelPortaliO23680.
SMRiO23680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24483. 8 interactors.
IntActiO23680. 8 interactors.
STRINGi3702.AT1G02280.1.

PTM databases

iPTMnetiO23680.

Proteomic databases

PaxDbiO23680.

Protocols and materials databases

DNASUi839248.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G02280.1; AT1G02280.1; AT1G02280.
AT1G02280.2; AT1G02280.2; AT1G02280.
GeneIDi839248.
GrameneiAT1G02280.1; AT1G02280.1; AT1G02280.
AT1G02280.2; AT1G02280.2; AT1G02280.
KEGGiath:AT1G02280.

Organism-specific databases

TAIRiAT1G02280.

Phylogenomic databases

eggNOGiENOG410IERB. Eukaryota.
ENOG410ZHTP. LUCA.
HOGENOMiHOG000264764.
InParanoidiO23680.
OMAiFPAATQE.
OrthoDBiEOG09360FPG.
PhylomeDBiO23680.

Enzyme and pathway databases

BioCyciARA:AT1G02280-MONOMER.
BRENDAi3.6.5.2. 399.

Miscellaneous databases

EvolutionaryTraceiO23680.
PROiO23680.

Gene expression databases

GenevisibleiO23680. AT.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006703. G_AIG1.
IPR027417. P-loop_NTPase.
IPR005688. Toc34.
[Graphical view]
PfamiPF04548. AIG1. 1 hit.
[Graphical view]
PIRSFiPIRSF038134. Toc34. 1 hit.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00991. 3a0901s02IAP34. 1 hit.
PROSITEiPS51720. G_AIG1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOC33_ARATH
AccessioniPrimary (citable) accession number: O23680
Secondary accession number(s): Q94B42, Q9GDD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 121 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.