TOC34_ARATH
ID TOC34_ARATH Reviewed; 313 AA.
AC Q38906; Q0WNL4; Q8L9G5; Q9FF74; Q9GDD2;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Translocase of chloroplast 34, chloroplastic;
DE Short=AtToc34;
DE EC=3.6.5.-;
DE AltName: Full=34 kDa chloroplast outer envelope protein;
DE AltName: Full=GTP-binding protein OEP34;
DE AltName: Full=Plastid protein import 3;
GN Name=TOC34; Synonyms=OEP34, PPI3; OrderedLocusNames=At5g05000;
GN ORFNames=MUG13.14;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Chen L.-J., Li H.-M.;
RT "Arabidopsis homologue of OEP34, a component of the pea chloroplast protein
RT import apparatus.";
RL (er) Plant Gene Register PGR95-140(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH TOC75.
RC STRAIN=cv. Columbia;
RX PubMed=10998188; DOI=10.1046/j.1365-313x.2000.00849.x;
RA Gutensohn M., Schulz B.I., Nicolay P., Fluegge U.-I.;
RT "Functional analysis of the two Arabidopsis homologues of Toc34, a
RT component of the chloroplast protein import apparatus.";
RL Plant J. 23:771-783(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DIMERIZATION WITH TOC33.
RX PubMed=12741849; DOI=10.1021/bi034001q;
RA Jelic M., Soll J., Schleiff E.;
RT "Two Toc34 homologues with different properties.";
RL Biochemistry 42:5906-5916(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND DEVELOPMENTAL STAGE.
RX PubMed=12897258; DOI=10.1105/tpc.012955;
RA Kubis S., Baldwin A., Patel R., Razzaq A., Dupree P., Lilley K., Kurth J.,
RA Leister D., Jarvis P.;
RT "The Arabidopsis ppi1 mutant is specifically defective in the expression,
RT chloroplast import, and accumulation of photosynthetic proteins.";
RL Plant Cell 15:1859-1871(2003).
RN [9]
RP FUNCTION.
RX PubMed=15053763; DOI=10.1111/j.1365-313x.2004.02024.x;
RA Constan D., Patel R., Keegstra K., Jarvis P.;
RT "An outer envelope membrane component of the plastid protein import
RT apparatus plays an essential role in Arabidopsis.";
RL Plant J. 38:93-106(2004).
RN [10]
RP FUNCTION.
RX PubMed=16435266; DOI=10.1055/s-2005-873044;
RA Hust B., Gutensohn M.;
RT "Deletion of core components of the plastid protein import machinery causes
RT differential arrest of embryo development in Arabidopsis thaliana.";
RL Plant Biol. 8:18-30(2006).
RN [11]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17261588; DOI=10.1074/jbc.m609491200;
RA Reddick L.E., Vaughn M.D., Wright S.J., Campbell I.M., Bruce B.D.;
RT "In vitro comparative kinetic analysis of the chloroplast Toc GTPases.";
RL J. Biol. Chem. 282:11410-11426(2007).
RN [12]
RP INTERACTION WITH AKR2A AND AKR2B.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [13]
RP AKR2A-BINDING SEQUENCE, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: GTPase involved in protein precursor import into
CC chloroplasts. Seems to recognize chloroplast-destined precursor
CC proteins and regulate their presentation to the translocation channel
CC through GTP hydrolysis. Probably specialized in the import of nuclear
CC encoded non-photosynthetic preproteins from the cytoplasm to the
CC chloroplast. {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:12897258,
CC ECO:0000269|PubMed:15053763, ECO:0000269|PubMed:16435266}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 nM for GDP (at pH 7.4) {ECO:0000269|PubMed:12741849,
CC ECO:0000269|PubMed:17261588};
CC KM=6.3 uM for GTP (at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588};
CC Vmax=940 nmol/min/ug enzyme with GTP as substrate (at pH 7.4)
CC {ECO:0000269|PubMed:12741849, ECO:0000269|PubMed:17261588};
CC -!- SUBUNIT: Homodimer, heterodimer with TOC33, and monomer. Part of the
CC TOC core complex that includes 1 protein for the specific recognition
CC of transit peptides surrounded by a ring composed of four proteins
CC forming translocation channels, and four to five GTP-binding proteins
CC providing energy. This core complex can interact with components of the
CC TIC complex to form a larger import complex. Chloroplastic protein
CC precursor such as prSS (precursor of the RuBisCO small subunit)
CC interacts with these complexes. The TOC complex contains a specific
CC subset of polar lipids such as digalactosyldiacylglyceride (DGDG),
CC phosphatidylcholine (PC) and phosphatidylglycerol (PG). Interacts at
CC least with TOC75. Interacts with AKR2A and AKR2B (PubMed:20215589).
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:20215589}.
CC -!- INTERACTION:
CC Q38906; O81283: TOC159; NbExp=5; IntAct=EBI-1766808, EBI-639063;
CC Q38906; Q38906: TOC34; NbExp=2; IntAct=EBI-1766808, EBI-1766808;
CC Q38906; P69249: RBCS; Xeno; NbExp=6; IntAct=EBI-1766808, EBI-1766821;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:10998188}; Single-pass membrane protein
CC {ECO:0000269|PubMed:10998188}. Note=May contain beta barrel
CC transmembrane regions.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers, and, to a
CC lower extent, in seedlings, stems, and leaves.
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12897258}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a relatively uniform, low level at
CC most stages of development. Observed in cotyledons and hypocotyls of
CC young seedling. Expressed in apical meristems. Found in the whole
CC roots. Expressed in middle-aged leaves. In flowers, mostly localized in
CC meristems, but is also present in all organs.
CC {ECO:0000269|PubMed:10998188, ECO:0000269|PubMed:12897258}.
CC -!- INDUCTION: Induced in light but repressed in darkness.
CC {ECO:0000269|PubMed:12897258}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC34 subfamily. {ECO:0000305}.
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DR EMBL; U43377; AAD09203.1; -; mRNA.
DR EMBL; AJ132696; CAC17699.1; -; mRNA.
DR EMBL; AB005245; BAB11522.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90814.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90815.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90816.1; -; Genomic_DNA.
DR EMBL; AK229425; BAF01285.1; -; mRNA.
DR EMBL; AY088447; AAM65983.1; -; mRNA.
DR RefSeq; NP_196119.1; NM_120582.5.
DR RefSeq; NP_850768.1; NM_180437.2.
DR RefSeq; NP_974732.1; NM_203003.3.
DR AlphaFoldDB; Q38906; -.
DR SMR; Q38906; -.
DR BioGRID; 15661; 12.
DR DIP; DIP-29773N; -.
DR IntAct; Q38906; 5.
DR STRING; 3702.AT5G05000.3; -.
DR iPTMnet; Q38906; -.
DR SwissPalm; Q38906; -.
DR PaxDb; Q38906; -.
DR PRIDE; Q38906; -.
DR ProteomicsDB; 232462; -.
DR EnsemblPlants; AT5G05000.1; AT5G05000.1; AT5G05000.
DR EnsemblPlants; AT5G05000.2; AT5G05000.2; AT5G05000.
DR EnsemblPlants; AT5G05000.3; AT5G05000.3; AT5G05000.
DR GeneID; 830382; -.
DR Gramene; AT5G05000.1; AT5G05000.1; AT5G05000.
DR Gramene; AT5G05000.2; AT5G05000.2; AT5G05000.
DR Gramene; AT5G05000.3; AT5G05000.3; AT5G05000.
DR KEGG; ath:AT5G05000; -.
DR Araport; AT5G05000; -.
DR TAIR; locus:2175259; AT5G05000.
DR eggNOG; ENOG502QSV2; Eukaryota.
DR HOGENOM; CLU_051932_0_0_1; -.
DR InParanoid; Q38906; -.
DR OMA; QRGKLWI; -.
DR OrthoDB; 1108753at2759; -.
DR PhylomeDB; Q38906; -.
DR PRO; PR:Q38906; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38906; baseline and differential.
DR Genevisible; Q38906; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; TAS:TAIR.
DR GO; GO:0003924; F:GTPase activity; TAS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0019750; P:chloroplast localization; TAS:TAIR.
DR GO; GO:0045036; P:protein targeting to chloroplast; TAS:TAIR.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005688; Toc34.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR PIRSF; PIRSF038134; Toc34; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00991; 3a0901s02IAP34; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; GTP-binding; Hydrolase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Plastid; Plastid outer membrane;
KW Protein transport; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..313
FT /note="Translocase of chloroplast 34, chloroplastic"
FT /id="PRO_0000144792"
FT TRANSMEM 269..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 36..260
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 45..52
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 67..70
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 71..75
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 92..95
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 127..132
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 161..164
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 210..212
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT MOTIF 287..295
FT /note="AKR2A-binding sequence (ABS) required for
FT chloroplast outer envelope membrane targeting"
FT /evidence="ECO:0000269|PubMed:21057222"
FT BINDING 48..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 67..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 44
FT /note="M -> I (in Ref. 6; AAM65983)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="G -> S (in Ref. 6; AAM65983)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="P -> L (in Ref. 1; AAD09203 and 2; CAC17699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 34707 MW; 1C90E435B2EE0441 CRC64;
MAALQTLREW IGIQQFPPAT QSKLLEILGK YKEEDVSSLT VLVMGKGGVG KSSTVNSVIG
EKAAAVSTFQ SEGLRPTLVS RTRSGFTLNI IDTPGLIEGG YVNDQAINII KRFLLNMTID
VLLYVDRLDV YRVDDLDRQV VGAITDAFGK EIWKKSALVL THAQFSPPDG LNYNHFVSKR
SNALLKVIQT GAQLKKQDLQ GFSIPVILVE NSGRCHKNES DEKILPCGTS WIPNLFNKIT
EISFNGNKAI HVDKKLVEGP NPNERGKKLI PLMFAFQYLL VMKPLVRAIK SDVSRESKPA
WELRDSGLAS RRS
