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Q9TRY0 (FKBP4_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP4

Short name=PPIase FKBP4
EC=5.2.1.8
Alternative name(s):
52 kDa FK506-binding protein
Short name=52 kDa FKBP
Short name=FKBP-52
FK506-binding protein 4
Short name=FKBP-4
HSP-binding immunophilin
Short name=HBI
Immunophilin FKBP52
Rotamase
Gene names
Name:FKBP4
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments By similarity. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening By similarity. 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.

Catalytic activity

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

Enzyme regulation

Inhibited by FK506 By similarity.

Subunit structure

Homodimer By similarity. Associates with HSP90 and HSP70 in unactivated steroid hormone receptor complexes. Also interacts with peroxisomal phytanoyl-CoA alpha-hydroxylase (PHYH). Interacts with NR3C1 and dynein By similarity. Interacts with HSF1 in the HSP90 complex By similarity. Associates with tubulin By similarity. Interacts with MAPT/TAU By similarity. 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.

Subcellular location

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

Domain

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 By similarity.

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 similarities

Contains 2 PPIase FKBP-type domains.

Contains 3 TPR repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

S100A1P026392EBI-6477371,EBI-6477285

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Peptidyl-prolyl cis-trans isomerase FKBP4
PRO_0000391467
Initiator methionine11Removed; alternate By similarity
Chain2 – 459458Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed
PRO_0000075317

Regions

Domain50 – 13889PPIase FKBP-type 1
Domain167 – 25387PPIase FKBP-type 2
Repeat270 – 30334TPR 1
Repeat319 – 35234TPR 2
Repeat354 – 38633TPR 3
Region267 – 400134Interaction with tubulin By similarity

Amino acid modifications

Modified residue11N-acetylmethionine; in peptidyl-prolyl cis-trans isomerase FKBP4; alternate By similarity
Modified residue21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partial By similarity
Modified residue1431Phosphothreonine By similarity
Modified residue2821N6-acetyllysine By similarity

Experimental info

Sequence conflict4281T → L AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9TRY0 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 2A0A25B737BC9A7B

FASTA45951,529
        10         20         30         40         50         60 
MTAEETKAAE SGAQSAPLRL EGVDISPKQD EGVLKVIKRE GTGTETPMIG DRVFVHYTGW 

        70         80         90        100        110        120 
LLDGTKFDSS LDRKDRFSFD LGKGEVIKAW DIAVATMKVG EVCHITCKPE YAYGLAGSPP 

       130        140        150        160        170        180 
KIPPNATLVF EVELFEFKGE DLTEEEDGGI IRRIRTRGEG YAKPNEGALV EVALEGYFKD 

       190        200        210        220        230        240 
QVFDRRELRF EVGEGESMDL PCGLEKAIQR MEKGEHSIVY LKPRYAFGSA GKEKFQIPPN 

       250        260        270        280        290        300 
AELKYEIHLK SFEKAKESWE MSSEEKLEQS TIVKERGTVY FKEGKYKQAV LQYKKIVSWL 

       310        320        330        340        350        360 
EYESSFSDED AEKAQALRLA SHLNLAMCHL KLQAFSAAIE NCNKALELDS NNEKGLFRRG 

       370        380        390        400        410        420 
EAHLAVNDFD LARADFQKVL QLYPSNKAAK AQLVVCQQRI RKQLEKEKKL YANMFERLAE 

       430        440        450 
EETKAKATVA AGDQPADAEM RDEPKNDVAG GQPQVEAEA 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes."
Peattie D.A., Harding M.W., Fleming M.A., Decenzo M.T., Lippke J.A., Livingston D.J., Benasutti M.
Proc. Natl. Acad. Sci. U.S.A. 89:10974-10978(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-28; 75-83; 89-98; 122-137; 164-175; 214-222; 245-250; 277-282; 345-354; 410-424 AND 427-440.
Tissue: Thymus.
[4]"The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13."
Yem A.W., Tomasselli A.G., Heinrikson R.L., Zurcher-Neely H., Ruff V.A., Johnson R.A., Deibel M.R. Jr.
J. Biol. Chem. 267:2868-2871(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18 AND 121-137.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT030531 mRNA. Translation: ABQ12971.1.
BC102456 mRNA. Translation: AAI02457.1.
PIRA42576.
B42576.
RefSeqNP_001029494.1. NM_001034322.2.
UniGeneBt.4797.

3D structure databases

ProteinModelPortalQ9TRY0.
SMRQ9TRY0. Positions 16-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9TRY0. 1 interaction.

Proteomic databases

PaxDbQ9TRY0.
PRIDEQ9TRY0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID508535.
KEGGbta:508535.

Organism-specific databases

CTD2288.

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000256916.
HOVERGENHBG051624.
InParanoidQ9TRY0.
KOK09571.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 2 hits.
PF00515. TPR_1. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 2 hits.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20868562.

Entry information

Entry nameFKBP4_BOVIN
AccessionPrimary (citable) accession number: Q9TRY0
Secondary accession number(s): A5D9B2, Q3T0C4, Q9TRX9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families