FKBP1A

From Wikipedia, the free encyclopedia
FK506 binding protein 1A, 12kDa

PDB rendering based on 1a7x.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsFKBP1A; FKBP-12; FKBP-1A; FKBP1; FKBP12; PKC12; PKCI2; PPIASE
External IDsOMIM: 186945 MGI: 95541 HomoloGene: 105139 ChEMBL: 1902 GeneCards: FKBP1A Gene
EC number5.2.1.8
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez228014225
EnsemblENSG00000088832ENSMUSG00000032966
UniProtP62942P26883
RefSeq (mRNA)NM_000801NM_008019
RefSeq (protein)NP_000792NP_032045
Location (UCSC)Chr 20:
1.35 – 1.37 Mb		Chr 2:
151.54 – 151.56 Mb
PubMed search
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Peptidyl-prolyl cis-trans isomerase FKBP1A is an enzyme that in humans is encoded by the FKBP1A gene.[1]

The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin (sirolimus). It interacts with several intracellular signal transduction proteins including type I TGF-beta receptor. It also interacts with multiple intracellular calcium release channels including the tetrameric skeletal muscle ryanodine receptor. In mouse, deletion of this homologous gene causes congenital heart disorder known as noncompaction of left ventricular myocardium. There is evidence of multiple alternatively spliced transcript variants for this gene, but the full length nature of some variants has not been determined.[2]

Interactions

FKBP1A has been shown to interact with RYR1,[3][4][5] Mammalian target of rapamycin,[6][7][8][9][10][11] TGF beta receptor 1,[12][13] GLMN,[14][15] ITPR1[16][17] and KIAA1303.[6][7]

References

  1. ↑ DiLella AG (Nov 1991). "Chromosomal assignment of the human immunophilin FKBP-12 gene". Biochem Biophys Res Commun 179 (3): 1427–33. doi:10.1016/0006-291X(91)91732-R. PMID 1930186. 
  2. ↑ "Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa". 
  3. ↑ Avila, Guillermo; Lee Eun Hui, Perez Claudio F, Allen P D, Dirksen Robert T (Jun 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". J. Biol. Chem. (United States) 278 (25): 22600–8. doi:10.1074/jbc.M205866200. ISSN 0021-9258. PMID 12704193. 
  4. ↑ Bultynck, G; De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys J B (Mar 2001). "Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor". Biochem. J. (England) 354 (Pt 2): 413–22. doi:10.1042/0264-6021:3540413. ISSN 0264-6021. PMC 1221670. PMID 11171121. 
  5. ↑ Gaburjakova, M; Gaburjakova J, Reiken S, Huang F, Marx S O, Rosemblit N, Marks A R (May 2001). "FKBP12 binding modulates ryanodine receptor channel gating". J. Biol. Chem. (United States) 276 (20): 16931–5. doi:10.1074/jbc.M100856200. ISSN 0021-9258. PMID 11279144. 
  6. ↑ 6.0 6.1 Jacinto, Estela; Loewith Robbie, Schmidt Anja, Lin Shuo, Rüegg Markus A, Hall Alan, Hall Michael N (Nov 2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive". Nat. Cell Biol. (England) 6 (11): 1122–8. doi:10.1038/ncb1183. ISSN 1465-7392. PMID 15467718. 
  7. ↑ 7.0 7.1 Sarbassov, D D; Ali Siraj M, Kim Do-Hyung, Guertin David A, Latek Robert R, Erdjument-Bromage Hediye, Tempst Paul, Sabatini David M (Jul 2004). "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton". Curr. Biol. (England) 14 (14): 1296–302. doi:10.1016/j.cub.2004.06.054. ISSN 0960-9822. PMID 15268862. 
  8. ↑ Choi, J; Chen J, Schreiber S L, Clardy J (Jul 1996). "Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP". Science (UNITED STATES) 273 (5272): 239–42. doi:10.1126/science.273.5272.239. ISSN 0036-8075. PMID 8662507. 
  9. ↑ Luker, Kathryn E; Smith Matthew C P, Luker Gary D, Gammon Seth T, Piwnica-Worms Helen, Piwnica-Worms David (Aug 2004). "Kinetics of regulated protein–protein interactions revealed with firefly luciferase complementation imaging in cells and living animals". Proc. Natl. Acad. Sci. U.S.A. (United States) 101 (33): 12288–93. doi:10.1073/pnas.0404041101. ISSN 0027-8424. PMC 514471. PMID 15284440. 
  10. ↑ Banaszynski, Laura A; Liu Corey W, Wandless Thomas J (Apr 2005). "Characterization of the FKBP.rapamycin.FRB ternary complex". J. Am. Chem. Soc. (United States) 127 (13): 4715–21. doi:10.1021/ja043277y. ISSN 0002-7863. PMID 15796538. 
  11. ↑ Sabers, C J; Martin M M, Brunn G J, Williams J M, Dumont F J, Wiederrecht G, Abraham R T (Jan 1995). "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells". J. Biol. Chem. (UNITED STATES) 270 (2): 815–22. doi:10.1074/jbc.270.2.815. ISSN 0021-9258. PMID 7822316. 
  12. ↑ Wang, T; Donahoe P K, Zervos A S (Jul 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science (UNITED STATES) 265 (5172): 674–6. doi:10.1126/science.7518616. ISSN 0036-8075. PMID 7518616. 
  13. ↑ Liu, F; Ventura F, Doody J, Massagué J (Jul 1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Mol. Cell. Biol. (UNITED STATES) 15 (7): 3479–86. ISSN 0270-7306. PMC 230584. PMID 7791754. 
  14. ↑ Chambraud, B; Radanyi C, Camonis J H, Shazand K, Rajkowski K, Baulieu E E (Dec 1996). "FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin". J. Biol. Chem. (UNITED STATES) 271 (51): 32923–9. doi:10.1074/jbc.271.51.32923. ISSN 0021-9258. PMID 8955134. 
  15. ↑ Neye, H (Mar 2001). "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52". Regul. Pept. (Netherlands) 97 (2–3): 147–52. doi:10.1016/S0167-0115(00)00206-8. ISSN 0167-0115. PMID 11164950. 
  16. ↑ MacMillan, Debbi; Currie Susan, Bradley Karen N, Muir Thomas C, McCarron John G (Dec 2005). "In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin". J. Cell. Sci. (England) 118 (Pt 23): 5443–51. doi:10.1242/jcs.02657. ISSN 0021-9533. PMID 16278292. 
  17. ↑ Cameron, A M; Nucifora F C, Fung E T, Livingston D J, Aldape R A, Ross C A, Snyder S H (Oct 1997). "FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain". J. Biol. Chem. (UNITED STATES) 272 (44): 27582–8. doi:10.1074/jbc.272.44.27582. ISSN 0021-9258. PMID 9346894. 

Further reading

  • Schiene-Fischer C, Yu C (2001). "Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases". FEBS Lett. 495 (1–2): 1–6. doi:10.1016/S0014-5793(01)02326-2. PMID 11322937. 
  • DiLella AG, Hawkins A, Craig RJ, et al. (1993). "Chromosomal band assignments of the genes encoding human FKBP12 and FKBP13". Biochem. Biophys. Res. Commun. 189 (2): 819–23. doi:10.1016/0006-291X(92)92276-4. PMID 1281998. 
  • Jayaraman T, Brillantes AM, Timerman AP, et al. (1992). "FK506 binding protein associated with the calcium release channel (ryanodine receptor)". J. Biol. Chem. 267 (14): 9474–7. PMID 1374404. 
  • Lepre CA, Thomson JA, Moore JM (1992). "Solution structure of FK506 bound to FKBP-12". FEBS Lett. 302 (1): 89–96. doi:10.1016/0014-5793(92)80292-O. PMID 1375171. 
  • Maki N, Sekiguchi F, Nishimaki J, et al. (1990). "Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin". Proc. Natl. Acad. Sci. U.S.A. 87 (14): 5440–3. doi:10.1073/pnas.87.14.5440. PMC 54340. PMID 1695378. 
  • Standaert RF, Galat A, Verdine GL, Schreiber SL (1990). "Molecular cloning and overexpression of the human FK506-binding protein FKBP". Nature 346 (6285): 671–4. doi:10.1038/346671a0. PMID 1696686. 
  • Siekierka JJ, Wiederrecht G, Greulich H, et al. (1991). "The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase". J. Biol. Chem. 265 (34): 21011–5. PMID 1701173. 
  • Michnick SW, Rosen MK, Wandless TJ, et al. (1991). "Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin". Science 252 (5007): 836–9. doi:10.1126/science.1709301. PMID 1709301. 
  • Van Duyne GD, Standaert RF, Karplus PA, et al. (1991). "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex". Science 252 (5007): 839–42. doi:10.1126/science.1709302. PMID 1709302. 
  • Rosen MK, Michnick SW, Karplus M, Schreiber SL (1991). "Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein". Biochemistry 30 (19): 4774–89. doi:10.1021/bi00233a020. PMID 1709363. 
  • Jin YJ, Albers MW, Lane WS, et al. (1991). "Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13". Proc. Natl. Acad. Sci. U.S.A. 88 (15): 6677–81. doi:10.1073/pnas.88.15.6677. PMC 52151. PMID 1713687. 
  • DiLella AG, Craig RJ (1991). "Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains". Biochemistry 30 (35): 8512–7. doi:10.1021/bi00099a002. PMID 1716149. 
  • Harding MW, Galat A, Uehling DE, Schreiber SL (1989). "A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase". Nature 341 (6244): 758–60. doi:10.1038/341758a0. PMID 2477715. 
  • Wang T, Donahoe PK, Zervos AS (1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science 265 (5172): 674–6. doi:10.1126/science.7518616. PMID 7518616. 
  • Peattie DA, Hsiao K, Benasutti M, Lippke JA (1995). "Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12". Gene 150 (2): 251–7. doi:10.1016/0378-1119(94)90434-0. PMID 7529739. 
  • Yang WM, Inouye CJ, Seto E (1995). "Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity". J. Biol. Chem. 270 (25): 15187–93. doi:10.1074/jbc.270.25.15187. PMID 7541038. 
  • Kawamura A, Su MS (1995). "Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain". J. Biol. Chem. 270 (26): 15463–6. doi:10.1074/jbc.270.26.15463. PMID 7541044. 
  • Griffith JP, Kim JL, Kim EE, et al. (1995). "X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex". Cell 82 (3): 507–22. doi:10.1016/0092-8674(95)90439-5. PMID 7543369. 
  • Van Duyne GD, Standaert RF, Karplus PA, et al. (1993). "Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin". J. Mol. Biol. 229 (1): 105–24. doi:10.1006/jmbi.1993.1012. PMID 7678431. 
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