Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9LDC0

- FKB42_ARATH

UniProt

Q9LDC0 - FKB42_ARATH

Protein

Peptidyl-prolyl cis-trans isomerase FKBP42

Gene

FKBP42

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity6 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. calmodulin binding Source: TAIR
    2. FK506 binding Source: RefGenome
    3. peptidyl-prolyl cis-trans isomerase activity Source: TAIR
    4. protein binding Source: IntAct

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB-KW
    2. leaf development Source: TAIR
    3. peptidyl-proline modification Source: RefGenome
    4. protein folding Source: UniProtKB-KW
    5. protein peptidyl-prolyl isomerization Source: GOC

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Keywords - Biological processi

    Auxin signaling pathway

    Keywords - Ligandi

    Calmodulin-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G21640-MONOMER.

    Protein family/group databases

    TCDBi8.A.11.1.1. the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP42 (EC:5.2.1.8)
    Short name:
    PPIase FKBP42
    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 namesi
    Name:FKBP42
    Synonyms:TWD1, UCU2
    Ordered Locus Names:At3g21640
    ORF Names:MIL23.21
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G21640.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: TAIR
    4. vacuolar membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane, Vacuole

    Pathology & Biotechi

    Disruption phenotypei

    Plants display helical rotation of several organs.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 365365Peptidyl-prolyl cis-trans isomerase FKBP42PRO_0000226087Add
    BLAST

    Proteomic databases

    PaxDbiQ9LDC0.
    PRIDEiQ9LDC0.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9LDC0.

    Interactioni

    Subunit structurei

    Interacts with calmodulin (CaM), MRP1, MRP2, MDR1/PGP1, MDR11/PGP19 and SHD/HSP90. Interacts with 1-naphthylphthalamic acid (NPA).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCB1Q9ZR722EBI-360006,EBI-366396
    ABCC1Q9C8G94EBI-360006,EBI-637633

    Protein-protein interaction databases

    BioGridi7050. 5 interactions.
    IntActiQ9LDC0. 5 interactions.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 484
    Beta strandi51 – 577
    Beta strandi69 – 7810
    Turni79 – 813
    Beta strandi84 – 874
    Turni88 – 925
    Beta strandi95 – 984
    Helixi104 – 1063
    Helixi107 – 1137
    Beta strandi121 – 1266
    Helixi128 – 1303
    Turni131 – 1355
    Beta strandi137 – 1415
    Beta strandi149 – 15911
    Turni166 – 1683
    Helixi172 – 18817
    Beta strandi191 – 1933
    Helixi196 – 20813
    Helixi211 – 2155
    Helixi219 – 22911
    Helixi231 – 24111
    Turni242 – 2443
    Helixi247 – 25913
    Helixi264 – 27512
    Turni276 – 2783
    Helixi280 – 28910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2F4EX-ray2.32A/B1-180[»]
    2IF4X-ray2.85A1-338[»]
    ProteinModelPortaliQ9LDC0.
    SMRiQ9LDC0. Positions 35-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9LDC0.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei339 – 35719Helical; Anchor for type IV membrane proteinAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini67 – 15993PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST
    Repeati179 – 21234TPR 1Add
    BLAST
    Repeati230 – 26334TPR 2Add
    BLAST
    Repeati264 – 29734TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 163163Interaction with MDR1/PGP1Add
    BLAST
    Regioni163 – 337175Interaction with MRP1Add
    BLAST
    Regioni310 – 32617Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FKBP-type PPIase family.Curated
    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0545.
    HOGENOMiHOG000006189.
    InParanoidiQ9LDC0.
    OMAiHSDKEGT.
    PhylomeDBiQ9LDC0.

    Family and domain databases

    Gene3Di1.10.150.160. 1 hit.
    1.25.40.10. 1 hit.
    InterProiIPR023114. Elongated_TPR_rpt_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    PF13181. TPR_8. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 3 hits.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9LDC0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDESLEHQTQ THDQESEIVT EGSAVVHSEP SQEGNVPPKV DSEAEVLDEK    50
    VSKQIIKEGH GSKPSKYSTC FLHYRAWTKN SQHKFEDTWH EQQPIELVLG 100
    KEKKELAGLA IGVASMKSGE RALVHVGWEL AYGKEGNFSF PNVPPMADLL 150
    YEVEVIGFDE TKEGKARSDM TVEERIGAAD RRKMDGNSLF KEEKLEEAMQ 200
    QYEMAIAYMG DDFMFQLYGK YQDMALAVKN PCHLNIAACL IKLKRYDEAI 250
    GHCNIVLTEE EKNPKALFRR GKAKAELGQM DSARDDFRKA QKYAPDDKAI 300
    RRELRALAEQ EKALYQKQKE MYKGIFKGKD EGGAKSKSLF WLIVLWQWFV 350
    SLFSRIFRRH RVKAD 365
    Length:365
    Mass (Da):41,806
    Last modified:October 1, 2000 - v1
    Checksum:iC939B75EEC79EA87
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071A → P in AAM13008. (PubMed:14593172)Curated
    Sequence conflicti107 – 1071A → P in AAN65079. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_188801.2. NM_113059.2.
    UniGeneiAt.5664.

    Genome annotation databases

    EnsemblPlantsiAT3G21640.1; AT3G21640.1; AT3G21640.
    GeneIDi821718.
    KEGGiath:AT3G21640.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_188801.2. NM_113059.2.
    UniGenei At.5664.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2F4E X-ray 2.32 A/B 1-180 [» ]
    2IF4 X-ray 2.85 A 1-338 [» ]
    ProteinModelPortali Q9LDC0.
    SMRi Q9LDC0. Positions 35-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 7050. 5 interactions.
    IntActi Q9LDC0. 5 interactions.

    Protein family/group databases

    TCDBi 8.A.11.1.1. the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.

    Proteomic databases

    PaxDbi Q9LDC0.
    PRIDEi Q9LDC0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G21640.1 ; AT3G21640.1 ; AT3G21640 .
    GeneIDi 821718.
    KEGGi ath:AT3G21640.

    Organism-specific databases

    TAIRi AT3G21640.

    Phylogenomic databases

    eggNOGi COG0545.
    HOGENOMi HOG000006189.
    InParanoidi Q9LDC0.
    OMAi HSDKEGT.
    PhylomeDBi Q9LDC0.

    Enzyme and pathway databases

    BioCyci ARA:AT3G21640-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9LDC0.
    PROi Q9LDC0.

    Gene expression databases

    Genevestigatori Q9LDC0.

    Family and domain databases

    Gene3Di 1.10.150.160. 1 hit.
    1.25.40.10. 1 hit.
    InterProi IPR023114. Elongated_TPR_rpt_dom.
    IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    PF13181. TPR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 3 hits.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    PS50005. TPR. 2 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiFKB42_ARATH
    AccessioniPrimary (citable) accession number: Q9LDC0
    Secondary accession number(s): Q8RWM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 105 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3