TOC34_CHLRE
ID TOC34_CHLRE Reviewed; 397 AA.
AC A8HYJ1;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translocase of chloroplast 34 homolog, chloroplastic {ECO:0000305};
DE Short=Cr-TOC34 {ECO:0000303|PubMed:23167510};
DE Short=TOC34p {ECO:0000303|PubMed:20395508};
DE EC=3.6.5.- {ECO:0000305};
GN Name=TOC34 {ECO:0000303|PubMed:23167510};
GN ORFNames=CHLREDRAFT_187290 {ECO:0000312|EMBL:EDP08621.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=20395508; DOI=10.1126/science.1186222;
RA Ferris P., Olson B.J., De Hoff P.L., Douglass S., Casero D., Prochnik S.,
RA Geng S., Rai R., Grimwood J., Schmutz J., Nishii I., Hamaji T., Nozaki H.,
RA Pellegrini M., Umen J.G.;
RT "Evolution of an expanded sex-determining locus in Volvox.";
RL Science 328:351-354(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP FUNCTION, AND INTERACTION WITH ARSA1.
RX PubMed=23167510; DOI=10.1111/tpj.12077;
RA Formighieri C., Cazzaniga S., Kuras R., Bassi R.;
RT "Biogenesis of photosynthetic complexes in the chloroplast of Chlamydomonas
RT reinhardtii requires ARSA1, a homolog of prokaryotic arsenite transporter
RT and eukaryotic TRC40 for guided entry of tail-anchored proteins.";
RL Plant J. 73:850-861(2013).
RN [4]
RP INTERACTION WITH ARSA1.
RX PubMed=28382961; DOI=10.1038/srep46022;
RA Maestre-Reyna M., Wu S.M., Chang Y.C., Chen C.C., Maestre-Reyna A.,
RA Wang A.H., Chang H.Y.;
RT "In search of tail-anchored protein machinery in plants: reevaluating the
RT role of arsenite transporters.";
RL Sci. Rep. 7:46022-46022(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 (By similarity). Functions as an essential
CC component of the outer chloroplast membrane translocon (TOC) complex,
CC which, in turn, catalyzes the import of nucleus-encoded precursor
CC polypeptides from the cytoplasm to the chloroplast (PubMed:23167510).
CC {ECO:0000250|UniProtKB:Q38906, ECO:0000269|PubMed:23167510}.
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, heterodimer with other TOC proteins, and monomer.
CC Part of the TOC core complex that includes 1 protein for the specific
CC recognition of transit peptides surrounded by a ring composed of four
CC proteins forming translocation channels, and four to five GTP-binding
CC proteins providing energy. This core complex can interact with
CC components of the TIC complex to form a larger import complex (By
CC similarity). Interacts with ARSA1 (PubMed:28382961).
CC {ECO:0000250|UniProtKB:Q38906, ECO:0000269|PubMed:28382961}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000250|UniProtKB:Q38906}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC TOC34 subfamily. {ECO:0000305}.
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DR EMBL; GU814014; ADF43133.1; -; Genomic_DNA.
DR EMBL; DS496110; EDP08621.1; -; Genomic_DNA.
DR RefSeq; XP_001696644.1; XM_001696592.1.
DR AlphaFoldDB; A8HYJ1; -.
DR SMR; A8HYJ1; -.
DR STRING; 3055.EDP08621; -.
DR PaxDb; A8HYJ1; -.
DR EnsemblPlants; PNW81571; PNW81571; CHLRE_06g252200v5.
DR GeneID; 5722177; -.
DR Gramene; PNW81571; PNW81571; CHLRE_06g252200v5.
DR KEGG; cre:CHLRE_06g252200v5; -.
DR eggNOG; ENOG502QSV2; Eukaryota.
DR HOGENOM; CLU_695140_0_0_1; -.
DR InParanoid; A8HYJ1; -.
DR OMA; WIKNDIS; -.
DR OrthoDB; 1108753at2759; -.
DR GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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 PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; GTP-binding; Hydrolase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Plastid outer membrane; Protein transport;
KW Receptor; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..397
FT /note="Translocase of chloroplast 34 homolog,
FT chloroplastic"
FT /id="PRO_0000442532"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 90..321
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..106
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 121..124
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 126..130
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 155..158
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 193..198
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT REGION 227..230
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 271..273
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT MOTIF 350..358
FT /note="AKR2A-binding sequence (ABS) required for
FT chloroplast outer envelope membrane targeting"
FT /evidence="ECO:0000250|UniProtKB:Q38906"
FT COMPBIAS 11..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 121..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 271..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 397 AA; 44542 MW; 2A4AD399A5939A3C CRC64;
MAQPPRPAEE YDDDVQEDED ELKEGELDDD ESHEAASEGG EAAAGDEEAE DDEQDEEDGD
EDSQPWAGLN RLPERDDMLD ILNELRAEGR KQLTVLLLGK SSVGKSSLIN SLLGEAVVRV
QAFKLQADTD ITTTVVRQVA VGNSEVDGFR LKLIDTCGLE DPEAGDTVNL GALSKIAEDV
RGVGIDVVLY CDRLDLYRVD PLDKAIIDAI SSTFGRGIWR RTVVALTHAN LVQTPPGTDY
DSFVNGRVRL IRGAVRGPLF FRPSLPVALV ENSETCPVSS ESGFRVLPDG EPWLVALVSQ
LVDMAAARRR PYKYHPRLSS KPSHRFRWLL PVAIAAEVLF YRRFLHPRLD DNQRRVEREE
ERVWALRGQQ RRALGLHRPH RPDKDAAWRL EQMYDDD
