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Q9TRY0

- FKBP4_BOVIN

UniProt

Q9TRY0 - FKBP4_BOVIN

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Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene
FKBP4
Organism
Bos taurus (Bovine)
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. 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 activityi

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

Enzyme regulationi

Inhibited by FK506 By similarity.

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  2. protein binding Source: IntAct

GO - Biological processi

  1. chaperone-mediated protein folding Source: UniProtKB
  2. negative regulation of microtubule polymerization or depolymerization Source: UniProtKB
  3. negative regulation of neuron projection development Source: UniProtKB
  4. protein peptidyl-prolyl isomerization Source: GOC
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
FK506-binding protein 4
Short name:
FKBP-4
HSP-binding immunophilin
Short name:
HBI
Immunophilin FKBP52
Rotamase
Cleaved into the following chain:
Gene namesi
Name:FKBP4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

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.

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 – 459459Peptidyl-prolyl cis-trans isomerase FKBP4PRO_0000391467Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 459458Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processedPRO_0000075317Add
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 similarity
Modified residuei282 – 2821N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9TRY0.
PRIDEiQ9TRY0.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
S100A1P026392EBI-6477371,EBI-6477285

Protein-protein interaction databases

IntActiQ9TRY0. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9TRY0.
SMRiQ9TRY0. Positions 16-425.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 13889PPIase FKBP-type 1Add
BLAST
Domaini167 – 25387PPIase FKBP-type 2Add
BLAST
Repeati270 – 30334TPR 1Add
BLAST
Repeati319 – 35234TPR 2Add
BLAST
Repeati354 – 38633TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 400134Interaction with tubulin By similarityAdd
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 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 similaritiesi

Contains 3 TPR repeats.

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiQ9TRY0.
KOiK09571.

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.

Q9TRY0-1 [UniParc]FASTAAdd to Basket

« Hide

MTAEETKAAE SGAQSAPLRL EGVDISPKQD EGVLKVIKRE GTGTETPMIG    50
DRVFVHYTGW LLDGTKFDSS LDRKDRFSFD LGKGEVIKAW DIAVATMKVG 100
EVCHITCKPE YAYGLAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI 150
IRRIRTRGEG YAKPNEGALV EVALEGYFKD QVFDRRELRF EVGEGESMDL 200
PCGLEKAIQR MEKGEHSIVY LKPRYAFGSA GKEKFQIPPN AELKYEIHLK 250
SFEKAKESWE MSSEEKLEQS TIVKERGTVY FKEGKYKQAV LQYKKIVSWL 300
EYESSFSDED AEKAQALRLA SHLNLAMCHL KLQAFSAAIE NCNKALELDS 350
NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK AQLVVCQQRI 400
RKQLEKEKKL YANMFERLAE EETKAKATVA AGDQPADAEM RDEPKNDVAG 450
GQPQVEAEA 459
Length:459
Mass (Da):51,529
Last modified:January 23, 2007 - v4
Checksum:i2A0A25B737BC9A7B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti428 – 4281T → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT030531 mRNA. Translation: ABQ12971.1.
BC102456 mRNA. Translation: AAI02457.1.
PIRiA42576.
B42576.
RefSeqiNP_001029494.1. NM_001034322.2.
UniGeneiBt.4797.

Genome annotation databases

GeneIDi508535.
KEGGibta:508535.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT030531 mRNA. Translation: ABQ12971.1 .
BC102456 mRNA. Translation: AAI02457.1 .
PIRi A42576.
B42576.
RefSeqi NP_001029494.1. NM_001034322.2.
UniGenei Bt.4797.

3D structure databases

ProteinModelPortali Q9TRY0.
SMRi Q9TRY0. Positions 16-425.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9TRY0. 1 interaction.

Proteomic databases

PaxDbi Q9TRY0.
PRIDEi Q9TRY0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 508535.
KEGGi bta:508535.

Organism-specific databases

CTDi 2288.

Phylogenomic databases

eggNOGi COG0545.
HOGENOMi HOG000256916.
HOVERGENi HBG051624.
InParanoidi Q9TRY0.
KOi K09571.

Miscellaneous databases

NextBioi 20868562.

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

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiFKBP4_BOVIN
AccessioniPrimary (citable) accession number: Q9TRY0
Secondary accession number(s): A5D9B2, Q3T0C4, Q9TRX9
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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