TOC90_ARATH
ID TOC90_ARATH Reviewed; 793 AA.
AC Q6S5G3; Q2V361;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translocase of chloroplast 90, chloroplastic;
DE Short=AtToc90;
DE EC=3.6.5.-;
DE AltName: Full=90 kDa chloroplast outer envelope protein;
DE AltName: Full=Plastid protein import 4;
GN Name=TOC90; Synonyms=PPI4; OrderedLocusNames=At5g20300; ORFNames=F5O24.190;
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], FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY
RP LIGHT, AND INTERACTION WITH TOC33 AND TOC75.
RC STRAIN=cv. Columbia;
RX PubMed=15284497; DOI=10.1023/b:plan.0000036374.92546.51;
RA Hiltbrunner A., Gruenig K., Alvarez-Huerta M., Infanger S., Bauer J.,
RA Kessler F.;
RT "AtToc90, a new GTP-binding component of the Arabidopsis chloroplast
RT protein import machinery.";
RL Plant Mol. Biol. 54:427-440(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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).
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 photosynthetic preproteins from the cytoplasm to the
CC chloroplast. {ECO:0000269|PubMed:15284497}.
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). Interacts with TOC33 and TOC75.
CC {ECO:0000250, ECO:0000269|PubMed:15284497}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:15284497}; Single-pass membrane protein
CC {ECO:0000269|PubMed:15284497}. Cytoplasm {ECO:0000269|PubMed:15284497}.
CC Note=Cycles between the cytoplasm and chloroplast, probably as a
CC soluble preprotein receptor. The anchoring to the chloroplast outer
CC membrane required the GTPase activity and GDP. May contain beta barrel
CC transmembrane regions (Probable). {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q6S5G3-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, flowers, and roots.
CC {ECO:0000269|PubMed:15273297}.
CC -!- INDUCTION: By light conditions. {ECO:0000269|PubMed:15284497}.
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; AY465351; AAS38569.1; -; mRNA.
DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92826.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92827.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68175.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68176.1; -; Genomic_DNA.
DR RefSeq; NP_001031911.1; NM_001036834.1. [Q6S5G3-1]
DR RefSeq; NP_001318609.1; NM_001343650.1. [Q6S5G3-1]
DR RefSeq; NP_001329949.1; NM_001343651.1. [Q6S5G3-1]
DR RefSeq; NP_197530.2; NM_122037.4. [Q6S5G3-1]
DR AlphaFoldDB; Q6S5G3; -.
DR SMR; Q6S5G3; -.
DR STRING; 3702.AT5G20300.2; -.
DR PaxDb; Q6S5G3; -.
DR PRIDE; Q6S5G3; -.
DR ProteomicsDB; 234334; -. [Q6S5G3-1]
DR EnsemblPlants; AT5G20300.1; AT5G20300.1; AT5G20300. [Q6S5G3-1]
DR EnsemblPlants; AT5G20300.2; AT5G20300.2; AT5G20300. [Q6S5G3-1]
DR EnsemblPlants; AT5G20300.4; AT5G20300.4; AT5G20300. [Q6S5G3-1]
DR EnsemblPlants; AT5G20300.5; AT5G20300.5; AT5G20300. [Q6S5G3-1]
DR GeneID; 832152; -.
DR Gramene; AT5G20300.1; AT5G20300.1; AT5G20300. [Q6S5G3-1]
DR Gramene; AT5G20300.2; AT5G20300.2; AT5G20300. [Q6S5G3-1]
DR Gramene; AT5G20300.4; AT5G20300.4; AT5G20300. [Q6S5G3-1]
DR Gramene; AT5G20300.5; AT5G20300.5; AT5G20300. [Q6S5G3-1]
DR KEGG; ath:AT5G20300; -.
DR Araport; AT5G20300; -.
DR TAIR; locus:2149204; AT5G20300.
DR eggNOG; ENOG502QR60; Eukaryota.
DR InParanoid; Q6S5G3; -.
DR OMA; PEVVHMS; -.
DR OrthoDB; 252618at2759; -.
DR PhylomeDB; Q6S5G3; -.
DR PRO; PR:Q6S5G3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6S5G3; baseline and differential.
DR Genevisible; Q6S5G3; AT.
DR GO; GO:0009707; C:chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045036; P:protein targeting to chloroplast; IMP: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 PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR Pfam; PF11886; TOC159_MAD; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Cytoplasm; GTP-binding;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Plastid;
KW Plastid outer membrane; Protein transport; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..793
FT /note="Translocase of chloroplast 90, chloroplastic"
FT /id="PRO_0000352656"
FT TRANSMEM 279..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 164..394
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 22..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..180
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 195..198
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 199..203
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 220..223
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 259..264
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 293..296
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 341..343
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT COILED 130..157
FT /evidence="ECO:0000255"
FT COILED 410..442
FT /evidence="ECO:0000255"
FT COILED 477..503
FT /evidence="ECO:0000255"
FT COMPBIAS 37..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 195..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 341..342
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 793 AA; 89329 MW; 4371ED5C5BACB2B2 CRC64;
MKGFKDWVFA LSNSMASSRP LLGSDPFFRD PHQEQDNHSQ APAAPQPVTL SEPPCSTSSD
LEILPPLSQQ QVPLESLYQS SIDLNGKKHN PLAKIGGLQV QFLRLVQRFG QSQNNILVSK
VLYRVHLAML IRAEESELKN VKLRQDRAKA LAREQESSGI PELDFSLRIL VLGKTGVGKS
ATINSIFGQP KSETDAFRPG TDRIEEVMGT VSGVKVTFID TPGFHPLSSS STRKNRKILL
SIKRYVKKRP PDVVLYLDRL DMIDMRYSDF SLLQLITEIF GAAIWLNTIL VMTHSAATTE
GRNGQSVNYE SYVGQRMDVV QHYIHQAVSD TKLENPVLLV ENHPSCKKNL AGEYVLPNGV
VWKPQFMFLC VCTKVLGDVQ SLLRFRDSIG LGQPSSTRTA SLPHLLSVFL RRRLSSGADE
TEKEIDKLLN LDLEEEDEYD QLPTIRILGK SRFEKLSKSQ KKEYLDELDY RETLYLKKQL
KEECRRRRDE KLVEEENLED TEQRDQAAVP LPDMAGPDSF DSDFPAHRYR CVSAGDQWLV
RPVYDPQGWD RDVGFDGINI ETAAKINRNL FASATGQVSR DKQRFTIQSE TNAAYTRNFR
EQTFSVAVDL QSSGEDLVYS FQGGTKLQTF KHNTTDVGVG LTSFGGKYYV GGKLEDTLLV
GKRVKLTANA GQMRGSGQTA NGGSFEACIR GRDYPVRNEQ IGLTMTALSF KRELVLNYGL
QTQFRPARGT NIDVNINMNN RKMGKINVKL NSSEHWEIAL ISALTMFKAL VRRSKTEMTE
ENEEEKIVNF LVS
