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P18203 (FKB1A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A

Short name=PPIase FKBP1A
EC=5.2.1.8
Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase
Gene names
Name:FKBP1A
Synonyms:FKBP1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activity

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

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Caution

Was originally (Ref.2) thought to be protein kinase C inhibitor 2 (PKCI-2 or 12 kDa inhibitor of protein kinase C), but has since been experimentally shown not to inhibit protein kinase C (Ref.8 and Ref.10).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3 Ref.4 Ref.5
Chain2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1A
PRO_0000075288

Regions

Domain20 – 10889PPIase FKBP-type

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue91Phosphoserine By similarity
Modified residue531N6-acetyllysine; alternate By similarity
Modified residue531N6-succinyllysine; alternate By similarity

Secondary structure

...................... 108
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18203 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9CD0F1278039C5B4

FASTA10811,910
        10         20         30         40         50         60 
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFV LGKQEVIRGW 

        70         80         90        100 
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPNATLIF DVELLKLE 

« 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]"Amino acid sequence of a 12-kDa inhibitor of protein kinase C."
Mozier N.M., Zuercher-Neely H.A., Guido D.M., Mathews W.R., Heinrikson R.L., Fraser E.D., Walsh M.P., Pearson J.D.
Eur. J. Biochem. 194:19-23(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-108.
Tissue: Brain.
[3]"Complete amino acid sequence of the FK506 and rapamycin binding protein, FKBP, isolated from calf thymus."
Lane W.S., Galat A., Harding M.W., Schreiber S.L.
J. Protein Chem. 10:151-160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-108.
Tissue: Thymus.
[4]"The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase."
Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., Cryan J., Hodges P.J., Sigal N.H.
J. Biol. Chem. 265:21011-21015(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-87.
[5]"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase."
Harding M.W., Galat A., Uehling D.E., Schreiber S.L.
Nature 341:758-760(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-41.
[6]"The peptidyl-prolyl isomerase, FK506-binding protein, is most likely the 12 kd endogenous inhibitor 2 of protein kinase C."
Goebl M.G.
Cell 64:1051-1052(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTITY OF FKBP AND PKCI-2.
[7]"FK506 and protein kinase C."
Tropschug A.M., Hofmann R.
Nature 351:195-195(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTITY OF FKBP AND PKCI-2.
[8]"The peptidyl-prolyl isomerase, FK506-binding protein, is not identical to protein kinase C inhibitor 2."
Goebl M.
Cell 66:423-423(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
[9]"Retraction concerning amino acid sequence of a 12-kDa inhibitor of protein kinase C. Mistaken identity of a protein kinase C inhibitor."
Walsh M.P.
Eur. J. Biochem. 200:811-811(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
[10]"Relationship of FKBP to PKCI-2."
Albers M.W., Liu J., Schreiber S.L.
Nature 351:527-527(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
[11]"Solution structure of the major binding protein for the immunosuppressant FK506."
Moore J.M., Peattie D.A., Fitzgibbon M.J., Thomson J.A.
Nature 351:248-250(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex."
Griffith J.P., Kim J.L., Kim E.E., Sintchak M.D., Thomson J.A., Fitzgibbon M.J., Fleming M.A., Caron P.R., Hsiao K., Navia M.A.
Cell 82:507-522(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT021075 mRNA. Translation: AAX09092.1.
PIRA61431.
RefSeqNP_001030533.1. NM_001035456.1.
UniGeneBt.63982.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FKKX-ray2.20A2-107[»]
1FKLX-ray1.70A2-107[»]
1TCOX-ray2.50C2-108[»]
ProteinModelPortalP18203.
SMRP18203. Positions 2-108.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP18203.

Proteomic databases

PaxDbP18203.
PRIDEP18203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000010928; ENSBTAP00000010928; ENSBTAG00000008303.
GeneID614795.
KEGGbta:614795.

Organism-specific databases

CTD2280.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00550000074272.
HOVERGENHBG051623.
InParanoidP18203.
KOK09568.
OMAISIHYVG.
OrthoDBEOG7ZGX5T.
TreeFamTF105291.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18203.
NextBio20899293.

Entry information

Entry nameFKB1A_BOVIN
AccessionPrimary (citable) accession number: P18203
Secondary accession number(s): Q5E945
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 119 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references