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Translocase of chloroplast 132, chloroplastic (AtToc132) (EC 3.6.5.-) (132 kDa chloroplast outer envelope protein)

 TC132_ARATH             Reviewed;        1206 AA.
Q9SLF3; Q56WJ7; Q8LPK1;
14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 97.
RecName: Full=Translocase of chloroplast 132, chloroplastic;
Short=AtToc132;
EC=3.6.5.-;
AltName: Full=132 kDa chloroplast outer envelope protein;
Name=TOC132; OrderedLocusNames=At2g16640; ORFNames=T24I21.5;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 728-1206.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH THE TOC COMPLEX, AND INDUCTION BY LIGHT.
PubMed=10646606; DOI=10.1038/35003214;
Bauer J., Chen K., Hiltbunner A., Wehrli E., Eugster M., Schnell D.,
Kessler F.;
"The major protein import receptor of plastids is essential for
chloroplast biogenesis.";
Nature 403:203-207(2000).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15273297; DOI=10.1105/tpc.104.023309;
Kubis S., Patel R., Combe J., Bedard J., Kovacheva S., Lilley K.,
Biehl A., Leister D., Rios G., Koncz C., Jarvis P.;
"Functional specialization amongst the Arabidopsis Toc159 family of
chloroplast protein import receptors.";
Plant Cell 16:2059-2077(2004).
[7]
FUNCTION.
PubMed=16435266; DOI=10.1055/s-2005-873044;
Hust B., Gutensohn M.;
"Deletion of core components of the plastid protein import machinery
causes differential arrest of embryo development in Arabidopsis
thaliana.";
Plant Biol. 8:18-30(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: 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. Probably specialized in the import
of nuclear encoded non-photosynthetic preproteins from the
cytoplasm to the chloroplast. {ECO:0000269|PubMed:15273297,
ECO:0000269|PubMed:16435266}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 1 Mg(2+) ion by subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer (By similarity). 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). {ECO:0000250,
ECO:0000269|PubMed:10646606}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Cytoplasm {ECO:0000250}. Note=Cycles between the cytoplasm and
chloroplast, probably as a soluble preprotein receptor. The
anchoring to the chloroplast outer membrane required the GTPase
activity and GDP. May contain beta barrel transmembrane regions
(By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers, and
roots. {ECO:0000269|PubMed:15273297}.
-!- INDUCTION: By light conditions. {ECO:0000269|PubMed:10646606}.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase
family. TOC159 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM20511.1; Type=Erroneous termination; Positions=1203; Note=Translated as Gln.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC005825; AAD24598.1; -; Genomic_DNA.
EMBL; CP002685; AEC06521.1; -; Genomic_DNA.
EMBL; CP002685; ANM62581.1; -; Genomic_DNA.
EMBL; CP002685; ANM62582.1; -; Genomic_DNA.
EMBL; AY099660; AAM20511.1; ALT_SEQ; mRNA.
EMBL; AK222043; BAD94786.1; -; mRNA.
PIR; D84542; D84542.
RefSeq; NP_001324729.1; NM_001335482.1.
RefSeq; NP_001324730.1; NM_001335483.1.
RefSeq; NP_179255.1; NM_127216.5.
UniGene; At.21953; -.
UniGene; At.67099; -.
DisProt; DP00610; -.
ProteinModelPortal; Q9SLF3; -.
SMR; Q9SLF3; -.
BioGrid; 1522; 3.
IntAct; Q9SLF3; 5.
MINT; Q9SLF3; -.
STRING; 3702.AT2G16640.1; -.
iPTMnet; Q9SLF3; -.
PaxDb; Q9SLF3; -.
PRIDE; Q9SLF3; -.
EnsemblPlants; AT2G16640.1; AT2G16640.1; AT2G16640.
EnsemblPlants; AT2G16640.2; AT2G16640.2; AT2G16640.
EnsemblPlants; AT2G16640.3; AT2G16640.3; AT2G16640.
GeneID; 816165; -.
Gramene; AT2G16640.1; AT2G16640.1; AT2G16640.
Gramene; AT2G16640.2; AT2G16640.2; AT2G16640.
Gramene; AT2G16640.3; AT2G16640.3; AT2G16640.
KEGG; ath:AT2G16640; -.
Araport; AT2G16640; -.
TAIR; locus:2059929; AT2G16640.
eggNOG; ENOG410IJAB; Eukaryota.
eggNOG; ENOG410XR0M; LUCA.
HOGENOM; HOG000243570; -.
InParanoid; Q9SLF3; -.
OMA; AHGWDHE; -.
OrthoDB; EOG09360FPG; -.
PhylomeDB; Q9SLF3; -.
PRO; PR:Q9SLF3; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SLF3; baseline and differential.
Genevisible; Q9SLF3; AT.
GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0051117; F:ATPase binding; IPI:CAFA.
GO; GO:0051087; F:chaperone binding; IPI:CAFA.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:TAIR.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR006703; G_AIG1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR024283; TOC159_MAD.
InterPro; IPR005690; Toc86_159.
Pfam; PF04548; AIG1; 1.
Pfam; PF11886; TOC159_MAD; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00993; 3a0901s04IAP86; 1.
PROSITE; PS51720; G_AIG1; 1.
1: Evidence at protein level;
Acetylation; Chloroplast; Coiled coil; Complete proteome; Cytoplasm;
GTP-binding; Hydrolase; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Plastid; Plastid outer membrane;
Protein transport; Receptor; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 1206 Translocase of chloroplast 132,
chloroplastic.
/FTId=PRO_0000352658.
TRANSMEM 1182 1199 Helical. {ECO:0000255}.
DOMAIN 572 801 AIG1-type G.
NP_BIND 584 589 GTP. {ECO:0000250}.
NP_BIND 603 608 GTP. {ECO:0000250}.
NP_BIND 749 750 GTP. {ECO:0000250}.
REGION 603 606 Homodimerization. {ECO:0000250}.
REGION 666 671 Homodimerization. {ECO:0000250}.
COILED 13 33 {ECO:0000255}.
COMPBIAS 44 305 Glu-rich.
METAL 588 588 Magnesium. {ECO:0000250}.
BINDING 701 701 GTP; via amide nitrogen. {ECO:0000250}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:19245862}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:O81283}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:O81283}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000250|UniProtKB:O81283}.
CONFLICT 10 10 R -> G (in Ref. 3; AAM20511).
{ECO:0000305}.
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


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