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Reviewed, UniProtKB/Swiss-Prot O22870 (FKBP2_ARATH)

Last modified May 5, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable FKBP-type peptidyl-prolyl cis-trans isomerase 2, chloroplastic
      Short name=PPIase
      Short name=Rotamase
    EC=5.2.1.8
Gene names
Ordered Locus Names: At2g43560
ORF Names: T1O24.30
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Subcellular location

Plastidchloroplast thylakoid lumen. Ref.3

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
Thylakoid
   DomainTransit peptide
   Molecular functionIsomerase
Rotamase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processprotein folding

Non-traceable author statement. Source: UniProtKB

   Cellular componentchloroplast thylakoid lumen Ref.3

Inferred from direct assay. Source: UniProtKB

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Non-traceable author statement. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRX3Q424031EBI-449404,EBI-449157

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3636Chloroplast Potential
Transit peptide37 – 7741Thylakoid
Chain78 – 223146Probable FKBP-type peptidyl-prolyl cis-trans isomerase 2, chloroplastic
PRO_0000025525

Regions

Domain124 – 21693PPIase FKBP-type

Sequences

Sequence LengthMass (Da)Tools
O22870-1 [UniParc].

Last modified March 27, 2002. Version 2.
Checksum: BE3A48D0C1A59C38

FASTA22323,564
        10         20         30         40         50         60 
MAASSPSLLL PLGSASRNGL TTKNPNSSRY IAARVIASET REQSCKISNL SSRREAMLLV 

        70         80         90        100        110        120 
LGVSGGLSMS SLAAYAAGLP PEDKPRLCEA ECEKELENVP MVTTESGLQY KDIKVGRGPS 

       130        140        150        160        170        180 
PPVGFQVAAN YVAMVPSGQI FDSSLEKGLP YLFRVGSGQV IKGLDEGILS MKAGGKRRLY 

       190        200        210        220 
IPGPLAFPKG LVSAPGRPRV APNSPVIFDV SLEFIPGLDS EEE 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Proteome map of the chloroplast lumen of Arabidopsis thaliana."
Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P., Kieselbach T.
J. Biol. Chem. 277:8354-8365(2002) [PubMed: 11719511] [Abstract]
Cited for: PROTEIN SEQUENCE OF 77-96, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

AC002335 Genomic DNA. Translation: AAB64339.2.
AY056125 mRNA. Translation: AAL07204.1.
AY113988 mRNA. Translation: AAM45036.1.
IPIIPI00531720.
PIRF84867.
RefSeqNP_181884.1.
UniGeneAt.24392

3D structure databases

HSSPHSSP built from PDB template 1YAT based on UniProtKB P20081.
ModBaseSearch...

Protein-protein interaction databases

IntActO22870. 1 interaction.

Proteomic databases

PRIDEO22870.
ProMEXO22870.

Genome annotation databases

GeneID818958.
GenomeReviewsGene locus AT2G43560 in contig CT485783_GR.
KEGGath:AT2G43560.
NMPDRfig|3702.1.peg.11513.

Organism-specific databases

TAIRAt2g43560.

Phylogenomic databases

OMAO22870. LYIFRVG.

Enzyme and pathway databases

BRENDA5.2.1.8. 302.

Gene expression databases

ArrayExpressO22870.
GermOnlineAT2G43560. Arabidopsis thaliana.

Family and domain databases

InterProIPR001179. PPIase_FKBP.
[Graphical view]
PANTHERPTHR10516. PPIase_FKBP. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFKBP2_ARATH
AccessionPrimary (citable) accession number: O22870
Secondary accession number(s): Q940C0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: May 5, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents