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Q9LDC0 (FKB42_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP42

Short name=PPIase FKBP42
EC=5.2.1.8
Alternative name(s):
42 kDa peptidyl-prolyl isomerase
FK506-binding protein 42
Short name=AtFKBP42
Immunophilin FKBP42
Protein TWISTED DWARF 1
Protein ULTRACURVATA 2
Rotamase
Gene names
Name:FKBP42
Synonyms:TWD1, UCU2
Ordered Locus Names:At3g21640
ORF Names:MIL23.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
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. Modulates the uptake of MRP substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E217betaG) uptake. Regulates cell elongation and orientation. Functions as a positive regulator of PGP1-mediated auxin transport. Confers drug modulation of PGP1 efflux activity as interaction with NPA or flavonol quercetin prevents its physical and functional interaction with PGP1. Required for the proper localization of auxin-related ABCB transporters. Plays a role in brassinosteroid (BR) signaling pathway. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12

Catalytic activity

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

Subunit structure

Interacts with calmodulin (CaM), MRP1, MRP2, MDR1/PGP1, MDR11/PGP19 and SHD/HSP90. Interacts with 1-naphthylphthalamic acid (NPA). Ref.5 Ref.6 Ref.7 Ref.11

Subcellular location

Cell membrane; Single-pass type IV membrane protein. Vacuole membrane; Single-pass type IV membrane protein. Endoplasmic reticulum Ref.5 Ref.6 Ref.7 Ref.12.

Disruption phenotype

Plants display helical rotation of several organs. Ref.5

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Contains 3 TPR repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCB1Q9ZR722EBI-360006,EBI-366396
ABCC1Q9C8G94EBI-360006,EBI-637633

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Peptidyl-prolyl cis-trans isomerase FKBP42
PRO_0000226087

Regions

Transmembrane339 – 35719Helical; Anchor for type IV membrane protein
Domain67 – 15993PPIase FKBP-type
Repeat179 – 21234TPR 1
Repeat230 – 26334TPR 2
Repeat264 – 29734TPR 3
Region1 – 163163Interaction with MDR1/PGP1
Region163 – 337175Interaction with MRP1
Region310 – 32617Calmodulin-binding Potential

Experimental info

Sequence conflict1071A → P in AAM13008. Ref.4
Sequence conflict1071A → P in AAN65079. Ref.4

Secondary structure

............................................... 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9LDC0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C939B75EEC79EA87

FASTA36541,806
        10         20         30         40         50         60 
MDESLEHQTQ THDQESEIVT EGSAVVHSEP SQEGNVPPKV DSEAEVLDEK VSKQIIKEGH 

        70         80         90        100        110        120 
GSKPSKYSTC FLHYRAWTKN SQHKFEDTWH EQQPIELVLG KEKKELAGLA IGVASMKSGE 

       130        140        150        160        170        180 
RALVHVGWEL AYGKEGNFSF PNVPPMADLL YEVEVIGFDE TKEGKARSDM TVEERIGAAD 

       190        200        210        220        230        240 
RRKMDGNSLF KEEKLEEAMQ QYEMAIAYMG DDFMFQLYGK YQDMALAVKN PCHLNIAACL 

       250        260        270        280        290        300 
IKLKRYDEAI GHCNIVLTEE EKNPKALFRR GKAKAELGQM DSARDDFRKA QKYAPDDKAI 

       310        320        330        340        350        360 
RRELRALAEQ EKALYQKQKE MYKGIFKGKD EGGAKSKSLF WLIVLWQWFV SLFSRIFRRH 


RVKAD 

« Hide

References

« Hide 'large scale' references
[1]"Structure and evolution of FKBP-like genes in Arabidopsis."
Kolukisaoglu U., Berger J., Eckhoff A., Moeller A., Saal B., Bellini C., Schulz B.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-bound and interacts with Hsp90."
Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.
Plant J. 32:263-276(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CALMODULIN AND SHD/HSP90, DISRUPTION PHENOTYPE.
[6]"TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19."
Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J., Saal B., Frangne N., Koncz-Kalman Z., Koncz C., Dudler R., Blakeslee J.J., Murphy A.S., Martinoia E., Schulz B.
Mol. Biol. Cell 14:4238-4249(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MDR1/PGP1 AND MDR11/PGP19.
[7]"Arabidopsis immunophilin-like TWD1 functionally interacts with vacuolar ABC transporters."
Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N., Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B., Martinoia E.
Mol. Biol. Cell 15:3393-3405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MRP1 AND MRP2.
[8]"The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding protein involved in auxin and brassinosteroid signaling."
Perez-Perez J.M., Ponce M.R., Micol J.L.
Plant Physiol. 134:101-117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis."
He Z., Li L., Luan S.
Plant Physiol. 134:1248-1267(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[10]"Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of Arabidopsis P-glycoproteins."
Bouchard R., Bailly A., Blakeslee J.J., Oehring S.C., Vincenzetti V., Lee O.R., Paponov I., Palme K., Mancuso S., Murphy A.S., Schulz B., Geisler M.
J. Biol. Chem. 281:30603-30612(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Modulation of P-glycoproteins by auxin transport inhibitors is mediated by interaction with immunophilins."
Bailly A., Sovero V., Vincenzetti V., Santelia D., Bartnik D., Koenig B.W., Mancuso S., Martinoia E., Geisler M.
J. Biol. Chem. 283:21817-21826(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NPA.
[12]"The ER-localized TWD1 immunophilin is necessary for localization of multidrug resistance-like proteins required for polar auxin transport in Arabidopsis roots."
Wu G., Otegui M.S., Spalding E.P.
Plant Cell 22:3295-3304(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"Crystal structure of a plant immunophilin domain involved in regulation of MDR-type ABC transporters."
Weiergraeber O.H., Eckhoff A., Granzin J.
FEBS Lett. 580:251-255(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-180.
[14]"Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana: a paradigm for regulation of plant ABC transporters."
Granzin J., Eckhoff A., Weiergraber O.H.
J. Mol. Biol. 364:799-809(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-338.
[15]"Solid-state NMR characterization of the putative membrane anchor of TWD1 from Arabidopsis thaliana."
Scheidt H.A., Vogel A., Eckhoff A., Koenig B.W., Huster D.
Eur. Biophys. J. 36:393-404(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 335-365, MEMBRANE ANCHOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ224640 mRNA. Translation: CAC00654.1.
AB019232 Genomic DNA. Translation: BAB02359.1.
CP002686 Genomic DNA. Translation: AEE76533.1.
AY093009 mRNA. Translation: AAM13008.1.
BT001192 mRNA. Translation: AAN65079.1.
RefSeqNP_188801.2. NM_113059.2.
UniGeneAt.5664.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F4EX-ray2.32A/B1-180[»]
2IF4X-ray2.85A1-338[»]
ProteinModelPortalQ9LDC0.
SMRQ9LDC0. Positions 35-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid7050. 5 interactions.
IntActQ9LDC0. 5 interactions.

Protein family/group databases

TCDB8.A.11.1.1. the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.

Proteomic databases

PaxDbQ9LDC0.
PRIDEQ9LDC0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G21640.1; AT3G21640.1; AT3G21640.
GeneID821718.
KEGGath:AT3G21640.

Organism-specific databases

TAIRAT3G21640.

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000006189.
InParanoidQ9LDC0.
OMAHSDKEGT.
PhylomeDBQ9LDC0.
ProtClustDBCLSN2680044.

Enzyme and pathway databases

BioCycARA:AT3G21640-MONOMER.

Gene expression databases

GenevestigatorQ9LDC0.

Family and domain databases

Gene3D1.10.150.160. 1 hit.
1.25.40.10. 1 hit.
InterProIPR023114. Elongated_TPR_rpt_dom.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
PS50005. TPR. 2 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9LDC0.
PROQ9LDC0.

Entry information

Entry nameFKB42_ARATH
AccessionPrimary (citable) accession number: Q9LDC0
Secondary accession number(s): Q8RWM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names