Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9QVC8

- FKBP4_RAT

UniProt

Q9QVC8 - FKBP4_RAT

(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)

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

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. poly(A) RNA binding Source: Ensembl
  7. 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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  5. microtubule Source: UniProtKB-KW
  6. mitochondrion Source: UniProtKB-KW
  7. neuronal cell body Source: RGD
  8. neuron projection Source: RGD
  9. nucleus Source: UniProtKB-KW
  10. perinuclear region of cytoplasm Source: RGD
  11. protein complex Source: RGD
Complete GO annotation...

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.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiQ9QVC8.
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_dom.
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

« Hide

        10         20         30         40         50
MTAEEMKVAE NGAQSAPLPL EGVDISPKQD EGVLKVIKRE GTGTETAMIG
60 70 80 90 100
DRVFVHYTGW LLDGTKFDSS LDRKDKFSFD LGKGEVIKAW DIAVATMKVG
110 120 130 140 150
EVCHITCKPE YAYGSAGSPP KIPPNATLVF EVELFEFKGE DLTEDEDGGI
160 170 180 190 200
IRRIRTRGEG YARPNDGAMV EVALEGYYND RLFDQRELCF EVGEGESLDL
210 220 230 240 250
PCGLEEAIQR MEKGEHSIVY LKPSYAFGSV GKERFQIPPH AELRYEVHLK
260 270 280 290 300
SFEKAKASWE MNSEEKLEQS NIVKERGTVY FKEGKYKQAL LQYKKIVSWL
310 320 330 340 350
EYESSFSGEE MQKVHALRLA SHLNLAMCHL KLQAFSAAIE SCNKALELDS
360 370 380 390 400
NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK TQLAVCQQRT
410 420 430 440 450
RRQLAREKKL YANMFERLAE EEHKAKTEVA AGDHPTDAEM KGEPNNVAGN

QAQVKTEA
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 ENSGT00760000119159.
HOGENOMi HOG000256916.
HOVERGENi HBG051624.
InParanoidi Q9QVC8.
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_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 102 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