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Protein

Peptidyl-prolyl cis-trans isomerase FKBP4

Gene

FKBP4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Enzyme regulationi

Inhibited by FK506.By similarity

GO - Molecular functioni

GO - Biological processi

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 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

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; alternateBy 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; alternateBy similarity
Modified residuei2 – 21N-acetylthreonine; in peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed; partialBy similarity
Modified residuei143 – 1431PhosphothreonineBy similarity
Modified residuei282 – 2821N6-acetyllysineBy 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).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.
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
Repeati354 – 38633TPR 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 400134Interaction with tubulinBy 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 2 PPIase FKBP-type domains.PROSITE-ProRule annotation
Contains 3 TPR repeats.PROSITE-ProRule annotation

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_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.

Q9TRY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAEETKAAE SGAQSAPLRL EGVDISPKQD EGVLKVIKRE GTGTETPMIG
60 70 80 90 100
DRVFVHYTGW LLDGTKFDSS LDRKDRFSFD LGKGEVIKAW DIAVATMKVG
110 120 130 140 150
EVCHITCKPE YAYGLAGSPP KIPPNATLVF EVELFEFKGE DLTEEEDGGI
160 170 180 190 200
IRRIRTRGEG YAKPNEGALV EVALEGYFKD QVFDRRELRF EVGEGESMDL
210 220 230 240 250
PCGLEKAIQR MEKGEHSIVY LKPRYAFGSA GKEKFQIPPN AELKYEIHLK
260 270 280 290 300
SFEKAKESWE MSSEEKLEQS TIVKERGTVY FKEGKYKQAV LQYKKIVSWL
310 320 330 340 350
EYESSFSDED AEKAQALRLA SHLNLAMCHL KLQAFSAAIE NCNKALELDS
360 370 380 390 400
NNEKGLFRRG EAHLAVNDFD LARADFQKVL QLYPSNKAAK AQLVVCQQRI
410 420 430 440 450
RKQLEKEKKL YANMFERLAE EETKAKATVA AGDQPADAEM RDEPKNDVAG

GQPQVEAEA
Length:459
Mass (Da):51,529
Last modified:January 23, 2007 - v4
Checksum:i2A0A25B737BC9A7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti428 – 4281T → L AA sequence (PubMed:1279700).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BT030531 mRNA. Translation: ABQ12971.1.
BC102456 mRNA. Translation: AAI02457.1.
PIRiA42576.
B42576.
RefSeqiNP_001029494.1. NM_001034322.2.
UniGeneiBt.4797.

3D structure databases

ProteinModelPortaliQ9TRY0.
SMRiQ9TRY0. Positions 16-425.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9TRY0. 1 interaction.

Proteomic databases

PaxDbiQ9TRY0.
PRIDEiQ9TRY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi508535.
KEGGibta:508535.

Organism-specific databases

CTDi2288.

Phylogenomic databases

eggNOGiCOG0545.
HOGENOMiHOG000256916.
HOVERGENiHBG051624.
InParanoidiQ9TRY0.
KOiK09571.

Miscellaneous databases

NextBioi20868562.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.