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   27-MAR-2024, entry version 125.
DE   RecName: Full=Translocase of chloroplast 132, chloroplastic {ECO:0000303|PubMed:10646606};
DE            Short=AtToc132 {ECO:0000303|PubMed:10646606};
DE            EC=3.6.5.- {ECO:0000250|UniProtKB:O81283};
DE   AltName: Full=132 kDa chloroplast outer envelope protein {ECO:0000303|PubMed:10646606};
GN   Name=TOC132 {ECO:0000303|PubMed:10646606};
GN   OrderedLocusNames=At2g16640 {ECO:0000312|Araport:AT2G16640};
GN   ORFNames=T24I21.5 {ECO:0000312|EMBL:AAD24598.1};
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).
RN   [10]
RP   PHOSPHORYLATION BY KOC1.
RC   STRAIN=cv. Columbia;
RX   PubMed=28283569; DOI=10.1074/jbc.m117.776468;
RA   Zufferey M., Montandon C., Douet V., Demarsy E., Agne B., Baginsky S.,
RA   Kessler F.;
RT   "The novel chloroplast outer membrane kinase KOC1 is a required component
RT   of the plastid protein import machinery.";
RL   J. Biol. Chem. 292:6952-6964(2017).
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;
CC         Evidence={ECO:0000250|UniProtKB:O23680};
CC       Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250|UniProtKB:O23680};
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|UniProtKB:O81283,
CC       ECO:0000269|PubMed:10646606}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000250|UniProtKB:O23680}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:O23680}. Cytoplasm {ECO:0000250}. Note=Cycles
CC       between the cytoplasm and chloroplast, probably as a soluble preprotein
CC       receptor. The anchoring to the chloroplast outer membrane required the
CC       GTPase activity and GDP. May contain beta barrel transmembrane regions
CC       (By similarity). {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 by KOC1. {ECO:0000269|PubMed:28283569}.
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.Q9SLF3; -.
DR   iPTMnet; Q9SLF3; -.
DR   PaxDb; 3702-AT2G16640-1; -.
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; AT2G16640; TOC132.
DR   eggNOG; ENOG502QR60; Eukaryota.
DR   HOGENOM; CLU_003856_0_0_1; -.
DR   InParanoid; Q9SLF3; -.
DR   OMA; QDNIPGR; -.
DR   OrthoDB; 4210585at2759; -.
DR   PhylomeDB; Q9SLF3; -.
DR   PRO; PR:Q9SLF3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SLF3; baseline and differential.
DR   GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0051117; F:ATPase 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:0051087; F:protein-folding chaperone binding; IPI:CAFA.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:TAIR.
DR   GO; GO:0045036; P:protein targeting to chloroplast; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd01853; Toc34_like; 1.
DR   DisProt; DP00610; -.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00993; 3a0901s04IAP86; 1.
DR   PANTHER; PTHR10903:SF135; GTP-BINDING PROTEIN A; 1.
DR   PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR   Pfam; PF04548; AIG1; 1.
DR   Pfam; PF11886; TOC159_MAD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51720; G_AIG1; 1.
DR   Genevisible; Q9SLF3; AT.
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|UniProtKB:O23680"
FT   BINDING         588
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O23680"
FT   BINDING         603..608
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O23680"
FT   BINDING         701
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O23680"
FT   BINDING         749..750
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O23680"
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
//