OEP61_ARATH
ID OEP61_ARATH Reviewed; 554 AA.
AC B7ZWR6; Q8GWM6; Q9C588;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Outer envelope protein 61;
DE AltName: Full=Tetratricopeptide repeat domain-containing protein 7;
GN Name=OEP61; Synonyms=TPR7; OrderedLocusNames=At5g21990; ORFNames=T6G21.100;
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=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 [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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP FUNCTION, MUTAGENESIS OF ARG-185, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND INTERACTION WITH HSP70-1 AND HSP90-2.
RX PubMed=21612577; DOI=10.1042/bj20110448;
RA von Loeffelholz O., Kriechbaumer V., Ewan R.A., Jonczyk R., Lehmann S.,
RA Young J.C., Abell B.M.;
RT "OEP61 is a chaperone receptor at the plastid outer envelope.";
RL Biochem. J. 438:143-153(2011).
RN [7]
RP FUNCTION, INTERACTION WITH HSP70-1; HSP90-1; HSP90-2; HSP90-3; HSP90-4;
RP ERDJ2A AND ERDJ2B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-181.
RX PubMed=22899711; DOI=10.1242/jcs.111054;
RA Schweiger R., Muller N.C., Schmitt M.J., Soll J., Schwenkert S.;
RT "AtTPR7 is a chaperone-docking protein of the Sec translocon in
RT Arabidopsis.";
RL J. Cell Sci. 125:5196-5207(2012).
CC -!- FUNCTION: Plays a role in protein import into the endoplasmic reticulum
CC (ER). May function as chaperone docking protein during post-
CC translational protein translocation into the ER. Chaperone receptor
CC mediating Hsp70-dependent protein targeting to chloroplasts. Interacts
CC specifically with some chloroplast precursors, but not with
CC mitochondrial precursors. Able to select precursors for delivery to the
CC chloroplast translocase independently of Hsp70.
CC {ECO:0000269|PubMed:21612577, ECO:0000269|PubMed:22899711}.
CC -!- SUBUNIT: Interacts (via TPR region) with HSP70-1, but not with HSP90-2.
CC Interacts with ERDJ2A and ERDJ2B. In the ER membrane, associates with
CC ERDJ2 in membrane complexes of 140 and 200 kDa and specifically
CC interacts with the HSP70 and HSP90 chaperones via its TPR domain.
CC {ECO:0000269|PubMed:21612577, ECO:0000269|PubMed:22899711}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Plastid, chloroplast outer
CC membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC Note=Resides most likely exclusively in the ER membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in leaves and lowest
CC in roots. {ECO:0000269|PubMed:21612577}.
CC -!- DOMAIN: The TPR region (103-213) is necessary for interaction with
CC HSP70-1 while the linker domain (214-530) facilitates selective
CC recognition of chloroplast precursor complexes.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC34492.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL589883; CAC34492.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED92964.1; -; Genomic_DNA.
DR EMBL; AK118755; BAC43348.1; -; mRNA.
DR EMBL; BT053758; ACL13985.1; -; mRNA.
DR RefSeq; NP_680187.2; NM_147882.3.
DR AlphaFoldDB; B7ZWR6; -.
DR SMR; B7ZWR6; -.
DR BioGRID; 17534; 12.
DR IntAct; B7ZWR6; 1.
DR MINT; B7ZWR6; -.
DR STRING; 3702.AT5G21990.1; -.
DR iPTMnet; B7ZWR6; -.
DR PaxDb; B7ZWR6; -.
DR PRIDE; B7ZWR6; -.
DR ProteomicsDB; 239018; -.
DR EnsemblPlants; AT5G21990.1; AT5G21990.1; AT5G21990.
DR GeneID; 832259; -.
DR Gramene; AT5G21990.1; AT5G21990.1; AT5G21990.
DR KEGG; ath:AT5G21990; -.
DR Araport; AT5G21990; -.
DR TAIR; locus:504956437; AT5G21990.
DR eggNOG; KOG0543; Eukaryota.
DR HOGENOM; CLU_024599_1_0_1; -.
DR InParanoid; B7ZWR6; -.
DR OMA; KMAKASP; -.
DR OrthoDB; 1446670at2759; -.
DR PhylomeDB; B7ZWR6; -.
DR PRO; PR:B7ZWR6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; B7ZWR6; baseline and differential.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IGI:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Endoplasmic reticulum; Membrane; Plastid;
KW Plastid outer membrane; Protein transport; Reference proteome; Repeat;
KW TPR repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Outer envelope protein 61"
FT /id="PRO_0000414021"
FT TOPO_DOM 1..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:21612577"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..554
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 103..136
FT /note="TPR 1"
FT REPEAT 180..213
FT /note="TPR 2"
FT REGION 245..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 181
FT /note="K->E: Weak binding to HSP70-1 and HSP90-2."
FT /evidence="ECO:0000269|PubMed:22899711"
FT MUTAGEN 185
FT /note="R->A: Loss of binding to HSP70-1."
FT /evidence="ECO:0000269|PubMed:21612577"
FT CONFLICT 248
FT /note="N -> K (in Ref. 3; BAC43348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 60757 MW; A72209F5DF86C3E4 CRC64;
MFNGLMDPEM IRLAQDQMSR MTPADFARIQ QQMMSNPDLM NMATESMKNM RPEDLKQAAE
QLKHTRPEDM AEISEKMAKA SPEDIAAMRA HADAQFTYQI NAAQMLKKQG NELHSRGNFS
DAAEKYLRAK NNLKEIPSSK GGAILLACSL NLMSCYLKTN QHEECIKEGS EVLGYDARNV
KALYRRGQAY RDLGLFEDAV SDLSKAHEVS PEDETIADVL RDVKERLAVE GPGKASRGVV
IEDITEENNV TSGENKKPSK EANGHAQGVK TDVDGLQALR DNPEAIRTFQ NFISKTDPDT
LAALSGGKAG DMSPDMFKTA SSMIGKMSPE EIQKMVQTAS SFKGDNPFAP TAPSTENGFT
PTPDMLKLAS DMMGKMSPEE RERMFNMASS LKANAPASTS YGNAEASEPR ESLGASGSSS
GNSFVAPRSG FEPSIPSAPP ADLQEQMRNQ MKDPAMRQMF TSMIKNMNPE MMASMSEQFG
MKLSQEDAAK AQQAMASLSP DALEKMMRWA DRAQTGMEKA KKAKKWLFGK GGLIFAILML
VLAMVLHRLG YIGN
