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)

P27124

- FKBP4_RABIT

UniProt

P27124 - FKBP4_RABIT

Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene

FKBP4

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by FK506.By similarity

    GO - Molecular functioni

    1. ATP binding Source: Ensembl
    2. GTP binding Source: Ensembl
    3. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. tau protein binding Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: Ensembl
    2. chaperone-mediated protein folding Source: UniProtKB
    3. embryo implantation Source: Ensembl
    4. male sex differentiation Source: Ensembl
    5. negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
    6. negative regulation of neuron projection development Source: UniProtKB
    7. prostate gland development Source: Ensembl
    8. protein complex localization Source: Ensembl
    9. protein peptidyl-prolyl isomerization Source: GOC
    10. steroid hormone receptor complex assembly Source: Ensembl

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP4 (EC:5.2.1.8)
    Short name:
    PPIase FKBP4
    Alternative name(s):
    52 kDa FK506-binding protein
    Short name:
    52 kDa FKBP
    Short name:
    FKBP-52
    59 kDa immunophilin
    Short name:
    p59
    FK506-binding protein 4
    Short name:
    FKBP-4
    FKBP59
    HSP-binding immunophilin
    Short name:
    HBI
    Immunophilin FKBP52
    Rotamase
    Cleaved into the following chain:
    Gene namesi
    Name:FKBP4
    Synonyms:P59
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Chromosome 8

    Subcellular locationi

    Cytoplasmcytosol By similarity. Mitochondrion By similarity. Nucleus. Cytoplasmcytoskeleton By similarity
    Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor.By similarity

    GO - Cellular componenti

    1. axonal growth cone Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. microtubule Source: UniProtKB-KW
    4. mitochondrion Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Peptidyl-prolyl cis-trans isomerase FKBP4PRO_0000391470Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 458457Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075320Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternateBy similarity
    Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partialBy similarity
    Modified residuei143 – 1431Phosphothreonine; by CK21 Publication
    Modified residuei282 – 2821N6-acetyllysineBy similarity
    Modified residuei450 – 4501PhosphoserineBy similarity
    Modified residuei452 – 4521PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation by CK2 results in loss of HSP90 binding activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP27124.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Associates with HSP90AA1 and HSP70 in steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein. Interacts with HSF1 in the HSP90 complex. Associates with tubulin. Interacts with MAPT/TAU. Interacts (via TPR domain) with S100A1, S100A2 and S100A6; the interaction is Ca2+ dependent. Interaction with S100A1 and S100A2 (but not with S100A6) leads to inhibition of FKBP4-HSP90 interaction. Interacts with dynein; causes partially NR3C1 transport to the nucleus.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi1172171. 1 interaction.
    STRINGi9986.ENSOCUP00000012554.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 263
    Turni27 – 293
    Beta strandi33 – 397
    Beta strandi52 – 6110
    Turni62 – 643
    Beta strandi65 – 695
    Helixi70 – 734
    Beta strandi77 – 804
    Turni81 – 833
    Helixi88 – 958
    Beta strandi102 – 1076
    Helixi109 – 1113
    Turni112 – 1165
    Turni119 – 1213
    Beta strandi128 – 1369

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ROTNMR-A4-148[»]
    1ROUNMR-A4-148[»]
    ProteinModelPortaliP27124.
    SMRiP27124. Positions 21-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27124.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 13889PPIase FKBP-type 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini167 – 25387PPIase FKBP-type 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati270 – 30334TPR 1Add
    BLAST
    Repeati319 – 35234TPR 2Add
    BLAST
    Repeati353 – 38634TPR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 400134Interaction with tubulinBy similarityAdd
    BLAST

    Domaini

    The C-terminal region (AA 375-458) is required to prevent tubulin polymerization.By similarity
    The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA).
    The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400.
    The TPR repeats mediate mitochondrial localization.By similarity

    Sequence similaritiesi

    Contains 2 PPIase FKBP-type domains.PROSITE-ProRule annotation
    Contains 3 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00550000074272.
    HOGENOMiHOG000256916.
    HOVERGENiHBG051624.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 2 hits.
    PF00515. TPR_1. 3 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 3 hits.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 2 hits.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P27124-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAEEMKAAE SGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETPMIG    50
    DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG 100
    ELCRITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTDDEDGGI 150
    IRRIRTRGEG YARPNDGAIV EVALEGYYKD RLFDQRELRF EVGEGESLDL 200
    PCGLEKAIQR MEKGEHSILY LKPSYAFGNA GKEKFQIPPY AELKYEVHLK 250
    SFEKAKESWE MSSEEKLEQS AIVKERGTVY FKEGKYKQAL LQYKKIVSWL 300
    EYESSFSSEE VQKAQALRLA SHLNLAMCHL KLQAFSAAVE SCNKALELDS 350
    NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK AQLAVCQQRI 400
    RKQIAREKKL YANMFERLAE EENKAKAEVA AGDHPMDTEM KDERNDVAGS 450
    QSQVETEA 458
    Length:458
    Mass (Da):51,475
    Last modified:January 23, 2007 - v3
    Checksum:i2EE25D561391DFF0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151S → H AA sequence (PubMed:8579355)Curated
    Sequence conflicti21 – 222EG → FI AA sequence (PubMed:8579355)Curated
    Sequence conflicti26 – 261S → T AA sequence (PubMed:8579355)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84474 mRNA. Translation: AAA31438.1.
    M84988 mRNA. Translation: AAA31439.1.
    PIRiA42386.
    RefSeqiNP_001075779.1. NM_001082310.1.
    UniGeneiOcu.1944.

    Genome annotation databases

    EnsembliENSOCUT00000014603; ENSOCUP00000012554; ENSOCUG00000014603.
    GeneIDi100009148.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M84474 mRNA. Translation: AAA31438.1 .
    M84988 mRNA. Translation: AAA31439.1 .
    PIRi A42386.
    RefSeqi NP_001075779.1. NM_001082310.1.
    UniGenei Ocu.1944.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ROT NMR - A 4-148 [» ]
    1ROU NMR - A 4-148 [» ]
    ProteinModelPortali P27124.
    SMRi P27124. Positions 21-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1172171. 1 interaction.
    STRINGi 9986.ENSOCUP00000012554.

    Proteomic databases

    PRIDEi P27124.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSOCUT00000014603 ; ENSOCUP00000012554 ; ENSOCUG00000014603 .
    GeneIDi 100009148.

    Organism-specific databases

    CTDi 2288.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00550000074272.
    HOGENOMi HOG000256916.
    HOVERGENi HBG051624.

    Miscellaneous databases

    EvolutionaryTracei P27124.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 2 hits.
    PF00515. TPR_1. 3 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 3 hits.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 2 hits.
    PS50005. TPR. 3 hits.
    PS50293. TPR_REGION. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "P59, an hsp 90-binding protein. Cloning and sequencing of its cDNA and preparation of a peptide-directed polyclonal antibody."
      Lebeau M.-C., Massol N., Herrick J., Faber L.E., Renoir J.-M., Radanyi C., Baulieu E.-E.
      J. Biol. Chem. 267:4281-4284(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Cloning and characterization of cDNA encoding the rabbit tRNA-guanine transglycosylase 60-kilodalton subunit."
      Deshpande K.L., Seubert P.H., Tillman D.M., Farkas W.R., Katze J.R.
      Arch. Biochem. Biophys. 326:1-7(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.
      Strain: New Zealand white.
      Tissue: Liver.
    3. "An immunophilin that binds M(r) 90,000 heat shock protein: main structural features of a mammalian p59 protein."
      Callebaut I., Renoir J.-M., Lebeau M.-C., Massol N., Burny A., Baulieu E.-E., Mornon J.-P.
      Proc. Natl. Acad. Sci. U.S.A. 89:6270-6274(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAINS.
    4. "Overexpression of p59-HBI (FKBP59), full length and domains, and characterization of PPlase activity."
      Chambraud B., Rouviere-Fourmy N., Radanyi C., Hsiao K., Peattie D.A., Livingston D.J., Baulieu E.E.
      Biochem. Biophys. Res. Commun. 196:160-166(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PPIASE ACTIVITY.
    5. "Protein phosphatase 5 is a major component of glucocorticoid receptor.hsp90 complexes with properties of an FK506-binding immunophilin."
      Silverstein A.M., Galigniana M.D., Chen M.S., Owens-Grillo J.K., Chinkers M., Pratt W.B.
      J. Biol. Chem. 272:16224-16230(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NR3C1 AND HSP90AA1.
    6. "Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52."
      Miyata Y., Chambraud B., Radanyi C., Leclerc J., Lebeau M.-C., Renoir J.-M., Shirai R., Catelli M.-G., Yahara I., Baulieu E.-E.
      Proc. Natl. Acad. Sci. U.S.A. 94:14500-14505(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CK2.
    7. "Different regions of the immunophilin FKBP52 determine its association with the glucocorticoid receptor, hsp90, and cytoplasmic dynein."
      Silverstein A.M., Galigniana M.D., Kanelakis K.C., Radanyi C., Renoir J.-M., Pratt W.B.
      J. Biol. Chem. 274:36980-36986(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1; DYNEIN AND HSP90.
    8. "Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-CoA alpha-hydroxylase is a new FKBP-associated protein."
      Chambraud B., Radanyi C., Camonis J.H., Rajkowski K., Schumacher M., Baulieu E.-E.
      Proc. Natl. Acad. Sci. U.S.A. 96:2104-2109(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHYH.
    9. Cited for: FUNCTION AS A CO-CHAPERONE, DOMAINS.
    10. "Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution."
      Craescu C.T., Rouviere N., Popescu A., Cerpolini E., Lebeau M.-C., Baulieu E.-E., Mispelter J.
      Biochemistry 35:11045-11052(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-149.

    Entry informationi

    Entry nameiFKBP4_RABIT
    AccessioniPrimary (citable) accession number: P27124
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3