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P27124

- FKBP4_RABIT

UniProt

P27124 - FKBP4_RABIT

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Protein
Peptidyl-prolyl cis-trans isomerase FKBP4
Gene
FKBP4, P59
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

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
Complete GO annotation...

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
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 FKBP4
PRO_0000391470Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 458457Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed
PRO_0000075320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate By similarity
Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial By similarity
Modified residuei143 – 1431Phosphothreonine; by CK2
Modified residuei282 – 2821N6-acetyllysine By similarity
Modified residuei450 – 4501Phosphoserine By similarity
Modified residuei452 – 4521Phosphoserine By similarity

Post-translational modificationi

Phosphorylation by CK2 results in loss of HSP90 binding activity.

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.3 Publications

Protein-protein interaction databases

BioGridi1172171. 1 interaction.
STRINGi9986.ENSOCUP00000012554.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP27124.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 400134Interaction with tubulin By similarity
Add
BLAST

Domaini

The C-terminal region (AA 375-458) is required to prevent tubulin polymerization By similarity.2 Publications
The PPIase activity is mainly due to the fisrt PPIase FKBP-type domain (1-138 AA).2 Publications
The chaperone activity resides in the C-terminal region, mainly between amino acids 264 and 400.2 Publications
The TPR repeats mediate mitochondrial localization By similarity.2 Publications

Sequence similaritiesi

Contains 3 TPR repeats.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151S → H AA sequence 1 Publication
Sequence conflicti21 – 222EG → FI AA sequence 1 Publication
Sequence conflicti26 – 261S → T AA sequence 1 Publication

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: July 9, 2014
This is version 129 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

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