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Q9QVC8

- FKBP4_RAT

UniProt

Q9QVC8 - FKBP4_RAT

Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene

Fkbp4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 3 (13 Oct 2009)
      Previous versions | rss
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    Functioni

    Immunophilin protein with PPIase and co-chaperone activities By similarity. Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90) By similarity. Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. May have a protective role against oxidative stress in mitochondria By similarity. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. The PPIase activity controls neuronal growth cones via regulation of TRPC1 channel opening.By similarity2 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by FK506.By similarity

    GO - Molecular functioni

    1. ATP binding Source: Ensembl
    2. copper-dependent protein binding Source: RGD
    3. FK506 binding Source: RefGenome
    4. GTP binding Source: Ensembl
    5. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
    6. tau protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_206546. Attenuation phase.

    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:Fkbp52
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 4

    Organism-specific databases

    RGDi628729. Fkbp4.

    Subcellular locationi

    Cytoplasmcytosol 2 Publications. Mitochondrion By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity
    Note: Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor By similarity. Colocalized with MAPT/TAU in the distal part of the primary cortical neurons.By similarity

    GO - Cellular componenti

    1. axonal growth cone Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum membrane Source: RefGenome
    4. microtubule Source: UniProtKB-KW
    5. mitochondrion Source: UniProtKB-SubCell
    6. neuronal cell body Source: RGD
    7. neuron projection Source: RGD
    8. nucleus Source: UniProtKB-SubCell
    9. perinuclear region of cytoplasm Source: RGD
    10. protein complex Source: RGD

    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_0000391471Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 458457Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075321Add
    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 CK2By similarity
    Modified residuei282 – 2821N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylation by CK2 results in loss of HSP90 binding activity.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9QVC8.
    PRIDEiQ9QVC8.

    PTM databases

    PhosphoSiteiQ9QVC8.

    Expressioni

    Tissue specificityi

    Widely detected in the brain (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriQ9QVC8.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-59214N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QVC8.
    ModBaseiSearch...
    MobiDBiSearch...

    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 tubulinAdd
    BLAST

    Domaini

    The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA).By similarity
    The C-terminal region (AA 375-458) is required to prevent tubulin polymerization.
    The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400.By similarity
    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.
    InParanoidiQ8K3U8.
    KOiK09571.
    OMAiNAELKYE.
    OrthoDBiEOG725DHH.
    PhylomeDBiQ9QVC8.

    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. 1 hit.
    [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.

    Q9QVC8-1 [UniParc]FASTAAdd to Basket

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    MTAEEMKVAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETAMIG    50
    DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG 100
    EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEDEDGGI 150
    IRRIRTRGEG YARPNDGAMV EVALEGYYND RLFDQRELCF EVGEGESLDL 200
    PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH AELRYEVHLK 250
    SFEKAKASWE MNSEEKLEQS NIVKERGTVY FKEGKYKQAL LQYKKIVSWL 300
    EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS 350
    NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT 400
    RRQLAREKKL YANMFERLAE EEHKAKTEVA AGDHPTDAEM KGEPNNVAGN 450
    QAQVKTEA 458
    Length:458
    Mass (Da):51,450
    Last modified:October 13, 2009 - v3
    Checksum:i5701387E5DC991C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH473964 Genomic DNA. Translation: EDM01775.1.
    AF531427 mRNA. Translation: AAM95632.1.
    RefSeqiNP_001178792.1. NM_001191863.1.
    UniGeneiRn.23741.

    Genome annotation databases

    EnsembliENSRNOT00000008737; ENSRNOP00000008737; ENSRNOG00000006444.
    GeneIDi260321.
    KEGGirno:260321.
    UCSCiRGD:628729. rat.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    A mind astray - Issue 118 of June 2010

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH473964 Genomic DNA. Translation: EDM01775.1 .
    AF531427 mRNA. Translation: AAM95632.1 .
    RefSeqi NP_001178792.1. NM_001191863.1.
    UniGenei Rn.23741.

    3D structure databases

    ProteinModelPortali Q9QVC8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59214N.

    PTM databases

    PhosphoSitei Q9QVC8.

    Proteomic databases

    PaxDbi Q9QVC8.
    PRIDEi Q9QVC8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000008737 ; ENSRNOP00000008737 ; ENSRNOG00000006444 .
    GeneIDi 260321.
    KEGGi rno:260321.
    UCSCi RGD:628729. rat.

    Organism-specific databases

    CTDi 2288.
    RGDi 628729. Fkbp4.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00550000074272.
    HOGENOMi HOG000256916.
    HOVERGENi HBG051624.
    InParanoidi Q8K3U8.
    KOi K09571.
    OMAi NAELKYE.
    OrthoDBi EOG725DHH.
    PhylomeDBi Q9QVC8.

    Enzyme and pathway databases

    Reactomei REACT_206546. Attenuation phase.

    Miscellaneous databases

    NextBioi 624351.

    Gene expression databases

    Genevestigatori Q9QVC8.

    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. 1 hit.
    [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. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex."
      Tai P.-K.K., Albers M.W., Chang H., Faber L.E., Schreiber S.L.
      Science 256:1315-1318(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25.
      Tissue: Leukemia.
    3. Desai B.J., McKinney K.Q., Meyer M.H., Bahrani-Mostafavi Z., Meyer R.A. Jr.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-458.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    4. "The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation."
      Chambraud B., Belabes H., Fontaine-Lenoir V., Fellous A., Baulieu E.E.
      FASEB J. 21:2787-2797(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBULIN.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH MAPT.
    6. Maurya D.K., Bhargava P.
      Submitted (JAN-2009) to UniProtKB
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiFKBP4_RAT
    AccessioniPrimary (citable) accession number: Q9QVC8
    Secondary accession number(s): A6IM14, Q8K3U8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 101 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3