TC120_ARATH
ID TC120_ARATH Reviewed; 1089 AA.
AC Q9LUS2;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translocase of chloroplast 120, chloroplastic;
DE Short=AtToc120;
DE EC=3.6.5.-;
DE AltName: Full=120 kDa chloroplast outer envelope protein;
GN Name=TOC120; OrderedLocusNames=At3g16620; ORFNames=MGL6.15;
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], INTERACTION WITH THE TOC COMPLEX, AND INDUCTION
RP BY LIGHT.
RX PubMed=10646606; DOI=10.1038/35003214;
RA Bauer J., Chen K., Hiltbunner A., Wehrli E., Eugster M., Schnell D.,
RA Kessler F.;
RT "The major protein import receptor of plastids is essential for chloroplast
RT biogenesis.";
RL Nature 403:203-207(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15273297; DOI=10.1105/tpc.104.023309;
RA Kubis S., Patel R., Combe J., Bedard J., Kovacheva S., Lilley K., Biehl A.,
RA Leister D., Rios G., Koncz C., Jarvis P.;
RT "Functional specialization amongst the Arabidopsis Toc159 family of
RT chloroplast protein import receptors.";
RL Plant Cell 16:2059-2077(2004).
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.
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:15273297}.
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 -!- SUBUNIT: Homodimer (By similarity). Part of the TOC core complex that
CC includes 1 protein for the specific recognition of transit peptides
CC surrounded by a ring composed of four proteins forming translocation
CC channels, and four to five GTP-binding proteins providing energy. This
CC core complex can interact with components of the TIC complex to form a
CC larger import complex. Chloroplastic protein precursor such as prSS
CC (precursor of the RuBisCO small subunit) interacts with these
CC complexes. The TOC complex contains a specific subset of polar lipids
CC such as digalactosyldiacylglyceride (DGDG), phosphatidylcholine (PC)
CC and phosphatidylglycerol (PG). {ECO:0000250,
CC ECO:0000269|PubMed:10646606}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Cycles between the cytoplasm and chloroplast,
CC probably as a soluble preprotein receptor. The anchoring to the
CC chloroplast outer membrane required the GTPase activity and GDP. May
CC contain beta barrel transmembrane regions (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, flowers, and roots.
CC {ECO:0000269|PubMed:15273297}.
CC -!- INDUCTION: By light conditions. {ECO:0000269|PubMed:10646606}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC159 subfamily. {ECO:0000305}.
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DR EMBL; AY587019; AAS97961.1; -; mRNA.
DR EMBL; AB022217; BAB02753.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75844.1; -; Genomic_DNA.
DR EMBL; AK229133; BAF01007.1; -; mRNA.
DR RefSeq; NP_188284.1; NM_112535.4.
DR AlphaFoldDB; Q9LUS2; -.
DR SMR; Q9LUS2; -.
DR BioGRID; 6247; 3.
DR IntAct; Q9LUS2; 4.
DR STRING; 3702.AT3G16620.1; -.
DR iPTMnet; Q9LUS2; -.
DR PaxDb; Q9LUS2; -.
DR PRIDE; Q9LUS2; -.
DR ProteomicsDB; 234207; -.
DR EnsemblPlants; AT3G16620.1; AT3G16620.1; AT3G16620.
DR GeneID; 820913; -.
DR Gramene; AT3G16620.1; AT3G16620.1; AT3G16620.
DR KEGG; ath:AT3G16620; -.
DR Araport; AT3G16620; -.
DR TAIR; locus:2089348; AT3G16620.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_0_0_1; -.
DR InParanoid; Q9LUS2; -.
DR OMA; QVSIRVN; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9LUS2; -.
DR PRO; PR:Q9LUS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUS2; baseline and differential.
DR Genevisible; Q9LUS2; AT.
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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045036; P:protein targeting to chloroplast; IDA: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; IPR024283; TOC159_MAD.
DR InterPro; IPR005690; Toc86_159.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR Pfam; PF11886; TOC159_MAD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00993; 3a0901s04IAP86; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chloroplast; Coiled coil; Cytoplasm; GTP-binding; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Plastid; Plastid outer membrane; Protein transport; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9SLF3"
FT CHAIN 2..1089
FT /note="Translocase of chloroplast 120, chloroplastic"
FT /id="PRO_0000352657"
FT TRANSMEM 1064..1080
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 454..683
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 158..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..470
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 485..488
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 489..493
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 510..513
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 548..553
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 582..585
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 631..633
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 710..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 767..788
FT /evidence="ECO:0000255"
FT COMPBIAS 269..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..735
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 466..471
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 485..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 631..632
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9SLF3"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SLF3"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81283"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81283"
SQ SEQUENCE 1089 AA; 119918 MW; 2ED2EAE60E409C7E CRC64;
MGDGAEIVTR LYGDEKKLAE DGRISELVGS DEVKDNEEEV FEEAIGSQEG LKPESLKTDV
LQEDFPLASN DEVCDLEETS RNERGVENLK VNYSEIGESH GEVNEQCITT KEADSDLVTL
KMNDYDHGEV ADADISYGKM ASSLDVVENS EKATSNLATE DVNLENGNTH SSSENGVVSP
DENKELVAEV ISVSACSVET GSNGIDDEKW EEEIDVSAGM VTEQRNGKTG AEFNSVKIVS
GDKSLNDSIE VAAGTLSPLE KSSSEEKGET ESQNSNGGHD IQSNKEIVKQ QDSSVNIGPE
IKESQHMERE SEVLSSVSPT ESRSDTAALP PARPAGLGRA APLLEPAPRV TQQPRVNGNV
SHNQPQQAED STTAETDEHD ETREKLQFIR VKFLRLSHRL GQTPHNVVVA QVLYRLGLAE
QLRGRNGSRV GAFSFDRASA MAEQLEAAAQ DPLDFSCTIM VLGKSGVGKS ATINSIFDEL
KISTDAFQVG TKKVQDIEGF VQGIKVRVID TPGLLPSWSD QHKNEKILKS VRAFIKKSPP
DIVLYLDRLD MQSRDSGDMP LLRTITDVFG PSIWFNAIVG LTHAASAPPD GPNGTASSYD
MFVTQRSHVI QQAIRQAAGD MRLMNPVSLV ENHSACRTNR AGQRVLPNGQ VWKPHLLLLS
FASKILAEAN ALLKLQDNIP GGQFATRSKA PPLPLLLSSL LQSRPQAKLP EQQYDDEDDE
DDLDESSDSE EESEYDELPP FKRLTKAEMT KLSKSQKKEY LDEMEYREKL FMKRQMKEER
KRRKLLKKFA AEIKDMPNGY SENVEEERSE PASVPVPMPD LSLPASFDSD NPTHRYRYLD
TSNQWLVRPV LETHGWDHDI GYEGVNAERL FVVKDKIPVS FSGQVTKDKK DAHVQLELAS
SVKHGEGRST SLGFDMQNAG KELAYTIRSE TRFNKFRKNK AAAGLSVTLL GDSVSAGLKV
EDKLIANKRF RMVMSGGAMT SRGDVAYGGT LEAQFRDKDY PLGRFLSTLG LSVMDWHGDL
AIGGNIQSQV PIGRSSNLIA RANLNNRGAG QVSIRVNSSE QLQLAVVALV PLFKKLLTYY
SPEQMQYGH
