OE64C_ARATH
ID OE64C_ARATH Reviewed; 589 AA.
AC Q9LVH5;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Outer envelope protein 64, chloroplastic;
DE AltName: Full=Translocon at the outer membrane of chloroplasts 64-III;
GN Name=OEP64; Synonyms=TOC64-III; OrderedLocusNames=At3g17970;
GN ORFNames=MEB5.19;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14741350; DOI=10.1016/s0014-5793(03)01457-1;
RA Chew O., Lister R., Qbadou S., Heazlewood J.L., Soll J., Schleiff E.,
RA Millar A.H., Whelan J.;
RT "A plant outer mitochondrial membrane protein with high amino acid sequence
RT identity to a chloroplast protein import receptor.";
RL FEBS Lett. 557:109-114(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15179043;
RA Lee Y.J., Sohn E.J., Lee K.H., Lee D.W., Hwang I.;
RT "The transmembrane domain of AtToc64 and its C-terminal lysine-rich
RT flanking region are targeting signals to the chloroplast outer envelope
RT membrane [correction].";
RL Mol. Cells 17:281-291(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16619024; DOI=10.1038/sj.emboj.7601091;
RA Qbadou S., Becker T., Mirus O., Tews I., Soll J., Schleiff E.;
RT "The molecular chaperone Hsp90 delivers precursor proteins to the
RT chloroplast import receptor Toc64.";
RL EMBO J. 25:1836-1847(2006).
RN [6]
RP FUNCTION, AND TOPOLOGY.
RX PubMed=17306301; DOI=10.1016/j.jmb.2007.01.047;
RA Qbadou S., Becker T., Bionda T., Reger K., Ruprecht M., Soll J.,
RA Schleiff E.;
RT "Toc64--a preprotein-receptor at the outer membrane with bipartide
RT function.";
RL J. Mol. Biol. 367:1330-1346(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17655652; DOI=10.1111/j.1365-313x.2007.03207.x;
RA Aronsson H., Boij P., Patel R., Wardle A., Toepel M., Jarvis P.;
RT "Toc64/OEP64 is not essential for the efficient import of proteins into
RT chloroplasts in Arabidopsis thaliana.";
RL Plant J. 52:53-68(2007).
RN [8]
RP IDENTIFICATION.
RX PubMed=20856808; DOI=10.1371/journal.pone.0012761;
RA Prasad B.D., Goel S., Krishna P.;
RT "In silico identification of carboxylate clamp type tetratricopeptide
RT repeat proteins in Arabidopsis and rice as putative co-chaperones of
RT Hsp90/Hsp70.";
RL PLoS ONE 5:E12761-E12761(2010).
CC -!- FUNCTION: Chaperone receptor mediating Hsp90-dependent protein
CC targeting to chloroplasts. Bi-functional preprotein receptor acting on
CC both sides of the membrane. Not essential for an efficient import of
CC pre-proteins into plastids. {ECO:0000269|PubMed:16619024,
CC ECO:0000269|PubMed:17306301, ECO:0000269|PubMed:17655652}.
CC -!- SUBUNIT: Part of the Toc complex and of the intermembrane space
CC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves and flower
CC buds. {ECO:0000269|PubMed:14741350, ECO:0000269|PubMed:17655652}.
CC -!- DOMAIN: The transmembrane domain and its C-terminal lysine-rich
CC flanking region (LFR) (26-61) are both necessary and sufficient for
CC targeting to the outer envelope membrane.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16619024, ECO:0000269|PubMed:17655652}.
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DR EMBL; AB019230; BAB02718.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76030.1; -; Genomic_DNA.
DR RefSeq; NP_188424.2; NM_112678.4.
DR AlphaFoldDB; Q9LVH5; -.
DR SMR; Q9LVH5; -.
DR BioGRID; 4995; 5.
DR STRING; 3702.AT3G17970.1; -.
DR SwissPalm; Q9LVH5; -.
DR PaxDb; Q9LVH5; -.
DR PRIDE; Q9LVH5; -.
DR ProteomicsDB; 238920; -.
DR EnsemblPlants; AT3G17970.1; AT3G17970.1; AT3G17970.
DR GeneID; 819660; -.
DR Gramene; AT3G17970.1; AT3G17970.1; AT3G17970.
DR KEGG; ath:AT3G17970; -.
DR Araport; AT3G17970; -.
DR TAIR; locus:2088600; AT3G17970.
DR eggNOG; KOG1124; Eukaryota.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_009600_17_1_1; -.
DR InParanoid; Q9LVH5; -.
DR OrthoDB; 447457at2759; -.
DR PhylomeDB; Q9LVH5; -.
DR BioCyc; ARA:AT3G17970-MON; -.
DR PRO; PR:Q9LVH5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LVH5; baseline and differential.
DR Genevisible; Q9LVH5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF01425; Amidase; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Plastid outer membrane; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..589
FT /note="Outer envelope protein 64, chloroplastic"
FT /id="PRO_0000414022"
FT TOPO_DOM 1
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..398
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REPEAT 474..507
FT /note="TPR 1"
FT REPEAT 508..541
FT /note="TPR 2"
FT REPEAT 542..575
FT /note="TPR 3"
SQ SEQUENCE 589 AA; 64025 MW; 08B4AE12CC6B9B63 CRC64;
MASQAANLWV LLGLGLAGIL MLTKKLKKTV REDFGAFIDK LMLLPPPQPA PPKAPHPLTG
LTFAVSDVFD ITGYVTGFGH PDWVRTHEAA SSTSPVVSTL VEGGATCVGK TVVDEFAFSI
SGENKHYDSP TNPAAPTRIP GGACSGAAVA VATNAVDFAL GIDTVGGVRV PAGYCGVLGF
KSSYGAISNT GIIPVSSSLD SVGWFARDPN TLRRVGHVLL QLPFATQRNP RQIILADDCF
QLLKIPVDRI TQVVTKSAEK LFGRQLLKHQ NLETYFETKV PSLKEFARTK AIANTKVSTS
RLLANVMQLL QRHEFLQNHG DWINTVKPAI DPVILSQVCE NPELTNEETE NLNAIRNETR
VAIGSLLKDD GILVIPTLPA VPPKLGSKEI TSEDYQNRAS SLLSIASISG CCQVTVPLGH
HEKCPISVSF IGRHGGDRFL LDTVQTMYPS LQEYSSIVTD PKSSKKAITK EESAEIAKEK
GNQAFKEKLW QKAIGLYSEA IKLSDNNATY YSNRAAAYLE LGGFLQAEED CTKAITLDKK
NVKAYLRRGT AREMLGDCKG AIEDFRYALV LEPNNKRASL SAERLRKFQ
