TC132_ARATH
ID TC132_ARATH Reviewed; 1206 AA.
AC Q9SLF3; Q56WJ7; Q8LPK1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Translocase of chloroplast 132, chloroplastic;
DE Short=AtToc132;
DE EC=3.6.5.-;
DE AltName: Full=132 kDa chloroplast outer envelope protein;
GN Name=TOC132; OrderedLocusNames=At2g16640; ORFNames=T24I21.5;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 728-1206.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH THE TOC COMPLEX, AND INDUCTION 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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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:15273297,
CC 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 -!- 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, leaves, flowers, and roots.
CC {ECO:0000269|PubMed:15273297}.
CC -!- INDUCTION: By light conditions. {ECO:0000269|PubMed:10646606}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20511.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005825; AAD24598.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06521.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62581.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62582.1; -; Genomic_DNA.
DR EMBL; AY099660; AAM20511.1; ALT_SEQ; mRNA.
DR EMBL; AK222043; BAD94786.1; -; mRNA.
DR PIR; D84542; D84542.
DR RefSeq; NP_001324729.1; NM_001335482.1.
DR RefSeq; NP_001324730.1; NM_001335483.1.
DR RefSeq; NP_179255.1; NM_127216.5.
DR AlphaFoldDB; Q9SLF3; -.
DR SMR; Q9SLF3; -.
DR BioGRID; 1522; 64.
DR IntAct; Q9SLF3; 5.
DR MINT; Q9SLF3; -.
DR STRING; 3702.AT2G16640.1; -.
DR iPTMnet; Q9SLF3; -.
DR PaxDb; Q9SLF3; -.
DR PRIDE; Q9SLF3; -.
DR ProteomicsDB; 234164; -.
DR EnsemblPlants; AT2G16640.1; AT2G16640.1; AT2G16640.
DR EnsemblPlants; AT2G16640.2; AT2G16640.2; AT2G16640.
DR EnsemblPlants; AT2G16640.3; AT2G16640.3; AT2G16640.
DR GeneID; 816165; -.
DR Gramene; AT2G16640.1; AT2G16640.1; AT2G16640.
DR Gramene; AT2G16640.2; AT2G16640.2; AT2G16640.
DR Gramene; AT2G16640.3; AT2G16640.3; AT2G16640.
DR KEGG; ath:AT2G16640; -.
DR Araport; AT2G16640; -.
DR TAIR; locus:2059929; AT2G16640.
DR eggNOG; ENOG502QR60; Eukaryota.
DR HOGENOM; CLU_003856_0_0_1; -.
DR InParanoid; Q9SLF3; -.
DR OMA; IASKWFR; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9SLF3; -.
DR PRO; PR:Q9SLF3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SLF3; baseline and differential.
DR Genevisible; Q9SLF3; 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:0051117; F:ATPase binding; IPI:CAFA.
DR GO; GO:0051087; F:chaperone binding; IPI:CAFA.
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:0004888; F:transmembrane signaling receptor activity; ISS:TAIR.
DR GO; GO:0045036; P:protein targeting to chloroplast; IBA:GO_Central.
DR DisProt; DP00610; -.
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:0007744|PubMed:22223895"
FT CHAIN 2..1206
FT /note="Translocase of chloroplast 132, chloroplastic"
FT /id="PRO_0000352658"
FT TRANSMEM 1182..1199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 572..801
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 33..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..588
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 603..606
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 607..611
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 628..631
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 666..671
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 700..703
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 749..751
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 824..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..33
FT /evidence="ECO:0000255"
FT COMPBIAS 42..68
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..852
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 584..589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 603..608
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 701
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 749..750
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81283"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81283"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O81283"
FT CONFLICT 10
FT /note="R -> G (in Ref. 3; AAM20511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1206 AA; 132277 MW; FEFB80CFC83655B5 CRC64;
MGDGTEFVVR SDREDKKLAE DRISDEQVVK NELVRSDEVR DDNEDEVFEE AIGSENDEQE
EEEDPKRELF ESDDLPLVET LKSSMVEHEV EDFEEAVGDL DETSSNEGGV KDFTAVGESH
GAGEAEFDVL ATKMNGDKGE GGGGGSYDKV ESSLDVVDTT ENATSTNTNG SNLAAEHVGI
ENGKTHSFLG NGIASPKNKE VVAEVIPKDD GIEEPWNDGI EVDNWEERVD GIQTEQEVEE
GEGTTENQFE KRTEEEVVEG EGTSKNLFEK QTEQDVVEGE GTSKDLFENG SVCMDSESEA
ERNGETGAAY TSNIVTNASG DNEVSSAVTS SPLEESSSGE KGETEGDSTC LKPEQHLASS
PHSYPESTEV HSNSGSPGVT SREHKPVQSA NGGHDVQSPQ PNKELEKQQS SRVHVDPEIT
ENSHVETEPE VVSSVSPTES RSNPAALPPA RPAGLGRASP LLEPASRAPQ QSRVNGNGSH
NQFQQAEDST TTEADEHDET REKLQLIRVK FLRLAHRLGQ TPHNVVVAQV LYRLGLAEQL
RGRNGSRVGA FSFDRASAMA EQLEAAGQDP LDFSCTIMVL GKSGVGKSAT INSIFDEVKF
CTDAFQMGTK RVQDVEGLVQ GIKVRVIDTP GLLPSWSDQA KNEKILNSVK AFIKKNPPDI
VLYLDRLDMQ SRDSGDMPLL RTISDVFGPS IWFNAIVGLT HAASVPPDGP NGTASSYDMF
VTQRSHVIQQ AIRQAAGDMR LMNPVSLVEN HSACRTNRAG QRVLPNGQVW KPHLLLLSFA
SKILAEANAL LKLQDNIPGR PFAARSKAPP LPFLLSSLLQ SRPQPKLPEQ QYGDEEDEDD
LEESSDSDEE SEYDQLPPFK SLTKAQMATL SKSQKKQYLD EMEYREKLLM KKQMKEERKR
RKMFKKFAAE IKDLPDGYSE NVEEESGGPA SVPVPMPDLS LPASFDSDNP THRYRYLDSS
NQWLVRPVLE THGWDHDIGY EGVNAERLFV VKEKIPISVS GQVTKDKKDA NVQLEMASSV
KHGEGKSTSL GFDMQTVGKE LAYTLRSETR FNNFRRNKAA AGLSVTHLGD SVSAGLKVED
KFIASKWFRI VMSGGAMTSR GDFAYGGTLE AQLRDKDYPL GRFLTTLGLS VMDWHGDLAI
GGNIQSQVPI GRSSNLIARA NLNNRGAGQV SVRVNSSEQL QLAMVAIVPL FKKLLSYYYP
QTQYGQ
