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P18203

- FKB1A_BOVIN

UniProt

P18203 - FKB1A_BOVIN

Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

FKBP1A

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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 activityi

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

    Enzyme regulationi

    Inhibited by both FK506 and rapamycin.

    GO - Molecular functioni

    1. calcium channel inhibitor activity Source: RefGenome
    2. FK506 binding Source: RefGenome
    3. peptidyl-prolyl cis-trans isomerase activity Source: BHF-UCL

    GO - Biological processi

    1. chaperone-mediated protein folding Source: RefGenome
    2. negative regulation of release of sequestered calcium ion into cytosol Source: RefGenome
    3. protein peptidyl-prolyl isomerization Source: GOC
    4. T cell activation Source: BHF-UCL

    Keywords - Molecular functioni

    Isomerase, Rotamase

    Enzyme and pathway databases

    ReactomeiREACT_211897. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_217890. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_220430. TGF-beta receptor signaling activates SMADs.
    REACT_220643. TGFBR1 LBD Mutants in Cancer.
    REACT_223905. TGFBR1 KD Mutants in Cancer.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
    Short name:
    PPIase FKBP1A
    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 namesi
    Name:FKBP1A
    Synonyms:FKBP1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 13

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: BHF-UCL
    2. endoplasmic reticulum membrane Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1APRO_0000075288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylglycineBy similarity
    Modified residuei9 – 91PhosphoserineBy similarity
    Modified residuei53 – 531N6-acetyllysine; alternateBy similarity
    Modified residuei53 – 531N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP18203.
    PRIDEiP18203.

    Interactioni

    Subunit structurei

    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.By similarity

    Structurei

    Secondary structure

    1
    108
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 97
    Beta strandi22 – 3110
    Beta strandi36 – 405
    Turni41 – 444
    Beta strandi47 – 504
    Beta strandi53 – 564
    Helixi58 – 658
    Beta strandi72 – 776
    Helixi79 – 813
    Turni82 – 865
    Turni89 – 913
    Beta strandi98 – 10811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FKKX-ray2.20A2-108[»]
    1FKLX-ray1.70A2-108[»]
    1TCOX-ray2.50C2-108[»]
    ProteinModelPortaliP18203.
    SMRiP18203. Positions 2-108.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP18203.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10889PPIase FKBP-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0545.
    GeneTreeiENSGT00550000074272.
    HOVERGENiHBG051623.
    InParanoidiP18203.
    KOiK09568.
    OMAiSPQKGDT.
    OrthoDBiEOG7ZGX5T.
    TreeFamiTF105291.

    Family and domain databases

    InterProiIPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view]
    PANTHERiPTHR10516. PTHR10516. 1 hit.
    PfamiPF00254. FKBP_C. 1 hit.
    [Graphical view]
    PROSITEiPS50059. FKBP_PPIASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P18203-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFV    50
    LGKQEVIRGW EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPNATLIF 100
    DVELLKLE 108
    Length:108
    Mass (Da):11,910
    Last modified:January 23, 2007 - v2
    Checksum:i9CD0F1278039C5B4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021075 mRNA. Translation: AAX09092.1.
    PIRiA61431.
    RefSeqiNP_001030533.1. NM_001035456.1.
    UniGeneiBt.63982.

    Genome annotation databases

    EnsembliENSBTAT00000010928; ENSBTAP00000010928; ENSBTAG00000008303.
    GeneIDi614795.
    KEGGibta:614795.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021075 mRNA. Translation: AAX09092.1 .
    PIRi A61431.
    RefSeqi NP_001030533.1. NM_001035456.1.
    UniGenei Bt.63982.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FKK X-ray 2.20 A 2-108 [» ]
    1FKL X-ray 1.70 A 2-108 [» ]
    1TCO X-ray 2.50 C 2-108 [» ]
    ProteinModelPortali P18203.
    SMRi P18203. Positions 2-108.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P18203.

    Proteomic databases

    PaxDbi P18203.
    PRIDEi P18203.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000010928 ; ENSBTAP00000010928 ; ENSBTAG00000008303 .
    GeneIDi 614795.
    KEGGi bta:614795.

    Organism-specific databases

    CTDi 2280.

    Phylogenomic databases

    eggNOGi COG0545.
    GeneTreei ENSGT00550000074272.
    HOVERGENi HBG051623.
    InParanoidi P18203.
    KOi K09568.
    OMAi SPQKGDT.
    OrthoDBi EOG7ZGX5T.
    TreeFami TF105291.

    Enzyme and pathway databases

    Reactomei REACT_211897. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_217890. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_220430. TGF-beta receptor signaling activates SMADs.
    REACT_220643. TGFBR1 LBD Mutants in Cancer.
    REACT_223905. TGFBR1 KD Mutants in Cancer.

    Miscellaneous databases

    EvolutionaryTracei P18203.
    NextBioi 20899293.

    Family and domain databases

    InterProi IPR023566. PPIase_FKBP.
    IPR001179. PPIase_FKBP_dom.
    [Graphical view ]
    PANTHERi PTHR10516. PTHR10516. 1 hit.
    Pfami PF00254. FKBP_C. 1 hit.
    [Graphical view ]
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. 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. 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. 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.

    Entry informationi

    Entry nameiFKB1A_BOVIN
    AccessioniPrimary (citable) accession number: P18203
    Secondary accession number(s): Q5E945
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally 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 (PubMed:1868545 and PubMed:1710782).1 Publication

    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