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Protein

Outer envelope protein 61

Gene

OEP61

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in protein import into the endoplasmic reticulum (ER). May function as chaperone docking protein during post-translational protein translocation into the ER. Chaperone receptor mediating Hsp70-dependent protein targeting to chloroplasts. Interacts specifically with some chloroplast precursors, but not with mitochondrial precursors. Able to select precursors for delivery to the chloroplast translocase independently of Hsp70.2 Publications

GO - Molecular functioni

GO - Biological processi

  • chaperone-mediated protein folding Source: GO_Central
  • cytosol to ER transport Source: TAIR
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Outer envelope protein 61
Alternative name(s):
Tetratricopeptide repeat domain-containing protein 7
Gene namesi
Name:OEP61
Synonyms:TPR7
Ordered Locus Names:At5g21990
ORF Names:T6G21.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G21990.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 525525Cytoplasmic1 PublicationAdd
BLAST
Transmembranei526 – 54621HelicalSequence analysisAdd
BLAST
Topological domaini547 – 5548LumenalSequence analysis

GO - Cellular componenti

  • chloroplast outer membrane Source: TAIR
  • cytosol Source: TAIR
  • endoplasmic reticulum membrane Source: TAIR
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Endoplasmic reticulum, Membrane, Plastid, Plastid outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi181 – 1811K → E: Weak binding to HSP70-1 and HSP90-2. 1 Publication
Mutagenesisi185 – 1851R → A: Loss of binding to HSP70-1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 554554Outer envelope protein 61PRO_0000414021Add
BLAST

Proteomic databases

PaxDbiB7ZWR6.
PRIDEiB7ZWR6.

PTM databases

iPTMnetiB7ZWR6.

Expressioni

Tissue specificityi

Ubiquitous. Highest expression in leaves and lowest in roots.1 Publication

Interactioni

Subunit structurei

Interacts (via TPR region) with HSP70-1, but not with HSP90-2. Interacts with ERDJ2A and ERDJ2B. In the ER membrane, associates with ERDJ2 in membrane complexes of 140 and 200 kDa and specifically interacts with the HSP70 and HSP90 chaperones via its TPR domain.2 Publications

Protein-protein interaction databases

BioGridi17534. 12 interactions.
IntActiB7ZWR6. 1 interaction.
MINTiMINT-8375685.
STRINGi3702.AT5G21990.1.

Structurei

3D structure databases

ProteinModelPortaliB7ZWR6.
SMRiB7ZWR6. Positions 99-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati103 – 13634TPR 1Add
BLAST
Repeati180 – 21334TPR 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 5050Met-richAdd
BLAST
Compositional biasi447 – 48135Met-richAdd
BLAST

Domaini

The TPR region (103-213) is necessary for interaction with HSP70-1 while the linker domain (214-530) facilitates selective recognition of chloroplast precursor complexes.

Sequence similaritiesi

Contains 2 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IQSZ. Eukaryota.
ENOG410ZI5X. LUCA.
HOGENOMiHOG000240818.
InParanoidiB7ZWR6.
OMAiTYQINAA.
PhylomeDBiB7ZWR6.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR023566. PPIase_FKBP.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00515. TPR_1. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B7ZWR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNGLMDPEM IRLAQDQMSR MTPADFARIQ QQMMSNPDLM NMATESMKNM
60 70 80 90 100
RPEDLKQAAE QLKHTRPEDM AEISEKMAKA SPEDIAAMRA HADAQFTYQI
110 120 130 140 150
NAAQMLKKQG NELHSRGNFS DAAEKYLRAK NNLKEIPSSK GGAILLACSL
160 170 180 190 200
NLMSCYLKTN QHEECIKEGS EVLGYDARNV KALYRRGQAY RDLGLFEDAV
210 220 230 240 250
SDLSKAHEVS PEDETIADVL RDVKERLAVE GPGKASRGVV IEDITEENNV
260 270 280 290 300
TSGENKKPSK EANGHAQGVK TDVDGLQALR DNPEAIRTFQ NFISKTDPDT
310 320 330 340 350
LAALSGGKAG DMSPDMFKTA SSMIGKMSPE EIQKMVQTAS SFKGDNPFAP
360 370 380 390 400
TAPSTENGFT PTPDMLKLAS DMMGKMSPEE RERMFNMASS LKANAPASTS
410 420 430 440 450
YGNAEASEPR ESLGASGSSS GNSFVAPRSG FEPSIPSAPP ADLQEQMRNQ
460 470 480 490 500
MKDPAMRQMF TSMIKNMNPE MMASMSEQFG MKLSQEDAAK AQQAMASLSP
510 520 530 540 550
DALEKMMRWA DRAQTGMEKA KKAKKWLFGK GGLIFAILML VLAMVLHRLG

YIGN
Length:554
Mass (Da):60,757
Last modified:March 3, 2009 - v1
Checksum:iA72209F5DF86C3E4
GO

Sequence cautioni

The sequence CAC34492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481N → K in BAC43348 (PubMed:11910074).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL589883 Genomic DNA. Translation: CAC34492.1. Different initiation.
CP002688 Genomic DNA. Translation: AED92964.1.
AK118755 mRNA. Translation: BAC43348.1.
BT053758 mRNA. Translation: ACL13985.1.
RefSeqiNP_680187.2. NM_147882.2.
UniGeneiAt.20053.

Genome annotation databases

EnsemblPlantsiAT5G21990.1; AT5G21990.1; AT5G21990.
GeneIDi832259.
GrameneiAT5G21990.1; AT5G21990.1; AT5G21990.
KEGGiath:AT5G21990.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL589883 Genomic DNA. Translation: CAC34492.1. Different initiation.
CP002688 Genomic DNA. Translation: AED92964.1.
AK118755 mRNA. Translation: BAC43348.1.
BT053758 mRNA. Translation: ACL13985.1.
RefSeqiNP_680187.2. NM_147882.2.
UniGeneiAt.20053.

3D structure databases

ProteinModelPortaliB7ZWR6.
SMRiB7ZWR6. Positions 99-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17534. 12 interactions.
IntActiB7ZWR6. 1 interaction.
MINTiMINT-8375685.
STRINGi3702.AT5G21990.1.

PTM databases

iPTMnetiB7ZWR6.

Proteomic databases

PaxDbiB7ZWR6.
PRIDEiB7ZWR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G21990.1; AT5G21990.1; AT5G21990.
GeneIDi832259.
GrameneiAT5G21990.1; AT5G21990.1; AT5G21990.
KEGGiath:AT5G21990.

Organism-specific databases

TAIRiAT5G21990.

Phylogenomic databases

eggNOGiENOG410IQSZ. Eukaryota.
ENOG410ZI5X. LUCA.
HOGENOMiHOG000240818.
InParanoidiB7ZWR6.
OMAiTYQINAA.
PhylomeDBiB7ZWR6.

Miscellaneous databases

PROiB7ZWR6.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR023566. PPIase_FKBP.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00515. TPR_1. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 3 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50005. TPR. 2 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70."
    Prasad B.D., Goel S., Krishna P.
    PLoS ONE 5:E12761-E12761(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. Cited for: FUNCTION, MUTAGENESIS OF ARG-185, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH HSP70-1 AND HSP90-2.
  7. "AtTPR7 is a chaperone-docking protein of the Sec translocon in Arabidopsis."
    Schweiger R., Muller N.C., Schmitt M.J., Soll J., Schwenkert S.
    J. Cell Sci. 125:5196-5207(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP70-1; HSP90-1; HSP90-2; HSP90-3; HSP90-4; ERDJ2A AND ERDJ2B, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-181.

Entry informationi

Entry nameiOEP61_ARATH
AccessioniPrimary (citable) accession number: B7ZWR6
Secondary accession number(s): Q8GWM6, Q9C588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: March 3, 2009
Last modified: July 6, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.