ID FKB1A_HUMAN Reviewed; 108 AA. AC P62942; D3DVW6; P20071; Q4VC47; Q6FGD9; Q6LEU3; Q9H103; Q9H566; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 194. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A; DE Short=PPIase FKBP1A; DE EC=5.2.1.8 {ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173}; DE AltName: Full=12 kDa FK506-binding protein; DE Short=12 kDa FKBP; DE Short=FKBP-12; DE AltName: Full=Calstabin-1; DE AltName: Full=FK506-binding protein 1A; DE Short=FKBP-1A; DE AltName: Full=Immunophilin FKBP12; DE AltName: Full=Rotamase; GN Name=FKBP1A; Synonyms=FKBP1, FKBP12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1695378; DOI=10.1073/pnas.87.14.5440; RA Maki N., Sekiguchi F., Nishimaki J., Miwa K., Hayano T., Takahashi N., RA Suzuki M.; RT "Complementary DNA encoding the human T-cell FK506-binding protein, a RT peptidylprolyl cis-trans isomerase distinct from cyclophilin."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5440-5443(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=1696686; DOI=10.1038/346671a0; RA Standaert R.F., Galat A., Verdine G.L., Schreiber S.L.; RT "Molecular cloning and overexpression of the human FK506-binding protein RT FKBP."; RL Nature 346:671-674(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1716149; DOI=10.1021/bi00099a002; RA Dilella A.G., Craig R.J.; RT "Exon organization of the human FKBP-12 gene: correlation with structural RT and functional protein domains."; RL Biochemistry 30:8512-8517(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Placenta; RX PubMed=7529739; DOI=10.1016/0378-1119(94)90434-0; RA Peattie D.A., Hsiao K., Benasutti M., Lippke J.A.; RT "Three distinct messenger RNAs can encode the human immunosuppressant- RT binding protein FKBP12."; RL Gene 150:251-257(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 2-52, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=1701173; DOI=10.1016/s0021-9258(17)45319-1; RA Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y., RA Cryan J., Hodges P.J., Sigal N.H.; RT "The cytosolic-binding protein for the immunosuppressant FK-506 is both a RT ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase."; RL J. Biol. Chem. 265:21011-21015(1990). RN [11] RP PROTEIN SEQUENCE OF 2-17. RX PubMed=2477715; DOI=10.1038/341758a0; RA Harding M.W., Galat A., Uehling D.E., Schreiber S.L.; RT "A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl RT isomerase."; RL Nature 341:758-760(1989). RN [12] RP PROTEIN SEQUENCE OF 2-14. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [13] RP INTERACTION WITH GLMN. RX PubMed=8955134; DOI=10.1074/jbc.271.51.32923; RA Chambraud B., Radanyi C., Camonis J.H., Shazand K., Rajkowski K., RA Baulieu E.-E.; RT "FAP48, a new protein that forms specific complexes with both immunophilins RT FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and RT rapamycin."; RL J. Biol. Chem. 271:32923-32929(1996). RN [14] RP FUNCTION IN TGFBR1 INHIBITION, AND INTERACTION WITH TGFBR1. RX PubMed=9233797; DOI=10.1093/emboj/16.13.3866; RA Chen Y.G., Liu F., Massague J.; RT "Mechanism of TGFbeta receptor inhibition by FKBP12."; RL EMBO J. 16:3866-3876(1997). RN [15] RP INTERACTION WITH RYR3. RX PubMed=10358090; DOI=10.1074/jbc.274.24.17297; RA Murayama T., Oba T., Katayama E., Oyamada H., Oguchi K., Kobayashi M., RA Otsuka K., Ogawa Y.; RT "Further characterization of the type 3 ryanodine receptor (RyR3) purified RT from rabbit diaphragm."; RL J. Biol. Chem. 274:17297-17308(1999). RN [16] RP INTERACTION WITH ACVR1B AND SMAD7, AND FUNCTION. RX PubMed=16720724; DOI=10.1677/jme.1.01966; RA Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.; RT "FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type RT I receptor."; RL J. Mol. Endocrinol. 36:569-579(2006). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP INTERACTION WITH RYR3. RX PubMed=22100703; DOI=10.1016/j.abb.2011.11.004; RA Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.; RT "Characterization of the binding sites for the interactions between FKBP12 RT and intracellular calcium release channels."; RL Arch. Biochem. Biophys. 517:37-42(2012). RN [19] RP STRUCTURE BY NMR. RX PubMed=1709363; DOI=10.1021/bi00233a020; RA Rosen M.K., Michnick S.W., Karplus M., Schreiber S.L.; RT "Proton and nitrogen sequential assignments and secondary structure RT determination of the human FK506 and rapamycin binding protein."; RL Biochemistry 30:4774-4789(1991). RN [20] RP STRUCTURE BY NMR. RX PubMed=1709301; DOI=10.1126/science.1709301; RA Michnick S.W., Rosen M.K., Wandless T.J., Karplus M., Schreiber S.L.; RT "Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and RT rapamycin."; RL Science 252:836-839(1991). RN [21] RP STRUCTURE BY NMR. RX PubMed=1375171; DOI=10.1016/0014-5793(92)80292-o; RA Lepre C.A., Thomson J.A., Moore J.M.; RT "Solution structure of FK506 bound to FKBP-12."; RL FEBS Lett. 302:89-96(1992). RN [22] RP STRUCTURE BY NMR OF COMPLEX WITH ASCOMYCIN. RX PubMed=7682113; DOI=10.1002/bip.360330404; RA Xu R.X., Nettesheim D., Olejniczak E.T., Meadows R., Gemmecker G., RA Fesik S.W.; RT "1H, 13C, and 15N assignments and secondary structure of the FK506 binding RT protein when bound to ascomycin."; RL Biopolymers 33:535-550(1993). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=1709302; DOI=10.1126/science.1709302; RA van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.; RT "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant RT complex."; RL Science 252:839-842(1991). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RA van Duyne G.D., Standaert R.F., Schreiber S.L., Clardy J.; RT "Atomic structure of the rapamycin human immunophilin FKBP-12 complex."; RL J. Am. Chem. Soc. 113:7433-7434(1991). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). RX PubMed=7678431; DOI=10.1006/jmbi.1993.1012; RA van Duyne G.D., Standaert R.F., Karplus P.A., Schreiber S.L., Clardy J.; RT "Atomic structures of the human immunophilin FKBP-12 complexes with FK506 RT and rapamycin."; RL J. Mol. Biol. 229:105-124(1993). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-107 IN COMPLEX WITH TGFBR1. RX PubMed=10025408; DOI=10.1016/s0092-8674(00)80555-3; RA Huse M., Chen Y.-G., Massague J., Kuriyan J.; RT "Crystal structure of the cytoplasmic domain of the type I TGF beta RT receptor in complex with FKBP12."; RL Cell 96:425-436(1999). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX PubMed=10656803; DOI=10.1006/jmbi.1999.3411; RA Burkhard P., Taylor P., Walkinshaw M.D.; RT "X-ray structures of small ligand-FKBP complexes provide an estimate for RT hydrophobic interaction energies."; RL J. Mol. Biol. 295:953-962(2000). CC -!- FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I CC serine/threonine kinase receptor, preventing TGF-beta receptor CC activation in absence of ligand. Recruits SMAD7 to ACVR1B which CC prevents the association of SMAD2 and SMAD3 with the activin receptor CC complex, thereby blocking the activin signal. May modulate the RYR1 CC calcium channel activity. PPIases accelerate the folding of proteins. CC It catalyzes the cis-trans isomerization of proline imidic peptide CC bonds in oligopeptides. {ECO:0000269|PubMed:16720724, CC ECO:0000269|PubMed:1696686, ECO:0000269|PubMed:1701173, CC ECO:0000269|PubMed:9233797}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:1696686, CC ECO:0000269|PubMed:1701173}; CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin. CC -!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by CC TGFBR2 and stabilizes it in the inactive conformation (PubMed:9233797). CC Interacts with ACVR1B and SMAD7 (PubMed:16720724). Identified in a CC complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 CC (PP1) (By similarity). Interacts directly with RYR2 and RYR3 CC (PubMed:10358090, PubMed:22100703). Interacts with GLMN; rapamycin and CC FK506 abolish the interaction with GLMN in a dose dependent manner CC (PubMed:8955134). Interacts directly with RYR1 (By similarity). CC {ECO:0000250|UniProtKB:P26883, ECO:0000250|UniProtKB:P62943, CC ECO:0000269|PubMed:10025408, ECO:0000269|PubMed:10358090, CC ECO:0000269|PubMed:16720724, ECO:0000269|PubMed:22100703, CC ECO:0000269|PubMed:8955134, ECO:0000269|PubMed:9233797}. CC -!- INTERACTION: CC P62942; P36896: ACVR1B; NbExp=2; IntAct=EBI-1027571, EBI-1384128; CC P62942; Q9NZD4: AHSP; NbExp=3; IntAct=EBI-1027571, EBI-720250; CC P62942; P05067: APP; NbExp=3; IntAct=EBI-1027571, EBI-77613; CC P62942; P42345: MTOR; NbExp=5; IntAct=EBI-1027571, EBI-359260; CC P62942; Q92736: RYR2; NbExp=2; IntAct=EBI-1027571, EBI-1170425; CC P62942; O15105: SMAD7; NbExp=3; IntAct=EBI-1027571, EBI-3861591; CC P62942; P36897: TGFBR1; NbExp=2; IntAct=EBI-1027571, EBI-1027557; CC P62942; PRO_0000037309 [P0C6X7]: rep; Xeno; NbExp=4; IntAct=EBI-1027571, EBI-25475797; CC P62942; PRO_0000037312 [P0C6X7]: rep; Xeno; NbExp=2; IntAct=EBI-1027571, EBI-25487250; CC P62942; P11716: RYR1; Xeno; NbExp=2; IntAct=EBI-1027571, EBI-6477441; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1701173}. CC Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic CC side {ECO:0000250|UniProtKB:P62943}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M34539; AAA35844.1; -; mRNA. DR EMBL; M92423; AAA58476.1; -; Genomic_DNA. DR EMBL; M92422; AAA58476.1; JOINED; Genomic_DNA. DR EMBL; M93060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X55741; CAA39272.1; -; Genomic_DNA. DR EMBL; M80199; AAA58472.1; -; Genomic_DNA. DR EMBL; X52220; CAA36462.1; -; mRNA. DR EMBL; BT007066; AAP35729.1; -; mRNA. DR EMBL; CR407613; CAG28541.1; -; mRNA. DR EMBL; CR542168; CAG46965.1; -; mRNA. DR EMBL; AL136531; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL109658; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10633.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10634.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10635.1; -; Genomic_DNA. DR EMBL; BC001925; AAH01925.3; -; mRNA. DR EMBL; BC005147; AAH05147.1; -; mRNA. DR CCDS; CCDS13014.1; -. DR PIR; I65284; A35780. DR RefSeq; NP_000792.1; NM_000801.4. DR RefSeq; NP_463460.1; NM_054014.3. DR PDB; 1A7X; X-ray; 2.00 A; A/B=2-108. DR PDB; 1B6C; X-ray; 2.60 A; A/C/E/G=2-108. DR PDB; 1BKF; X-ray; 1.60 A; A=2-108. DR PDB; 1BL4; X-ray; 1.90 A; A/B=2-108. DR PDB; 1D6O; X-ray; 1.85 A; A/B=2-108. DR PDB; 1D7H; X-ray; 1.90 A; A/B=2-108. DR PDB; 1D7I; X-ray; 1.90 A; A/B=2-108. DR PDB; 1D7J; X-ray; 1.85 A; A/B=2-108. DR PDB; 1EYM; X-ray; 2.00 A; A/B=2-108. DR PDB; 1F40; NMR; -; A=2-108. DR PDB; 1FAP; X-ray; 2.70 A; A=2-108. DR PDB; 1FKB; X-ray; 1.70 A; A=2-108. DR PDB; 1FKD; X-ray; 1.72 A; A=2-108. DR PDB; 1FKF; X-ray; 1.70 A; A=2-108. DR PDB; 1FKG; X-ray; 2.00 A; A=2-108. DR PDB; 1FKH; X-ray; 1.95 A; A=2-108. DR PDB; 1FKI; X-ray; 2.20 A; A/B=2-108. DR PDB; 1FKJ; X-ray; 1.70 A; A=2-108. DR PDB; 1FKR; NMR; -; A=2-108. DR PDB; 1FKS; NMR; -; A=2-108. DR PDB; 1FKT; NMR; -; A=2-108. DR PDB; 1J4H; X-ray; 1.80 A; A=2-108. DR PDB; 1J4I; X-ray; 1.80 A; A=2-108. DR PDB; 1J4R; X-ray; 1.80 A; A/B/D=2-108. DR PDB; 1NSG; X-ray; 2.20 A; A=2-108. DR PDB; 1QPF; X-ray; 2.50 A; A/D=2-108. DR PDB; 1QPL; X-ray; 2.90 A; A/C=2-108. DR PDB; 2DG3; X-ray; 1.70 A; A=2-108. DR PDB; 2DG4; X-ray; 1.70 A; A=2-108. DR PDB; 2DG9; X-ray; 1.70 A; A=2-108. DR PDB; 2FAP; X-ray; 2.20 A; A=2-108. DR PDB; 2FKE; X-ray; 1.72 A; A=2-108. DR PDB; 2ND5; NMR; -; A=1-108. DR PDB; 2PPN; X-ray; 0.92 A; A=2-108. DR PDB; 2PPO; X-ray; 1.29 A; A=2-108. DR PDB; 2PPP; X-ray; 0.94 A; A=2-108. DR PDB; 2RSE; NMR; -; A=2-108. DR PDB; 3FAP; X-ray; 1.85 A; A=2-108. DR PDB; 3H9R; X-ray; 2.35 A; B=1-108. DR PDB; 3MDY; X-ray; 2.05 A; B/D=1-108. DR PDB; 4DH0; X-ray; 2.10 A; A=2-108. DR PDB; 4FAP; X-ray; 2.80 A; A=2-108. DR PDB; 4IPX; X-ray; 1.70 A; A=2-108. DR PDB; 4N19; X-ray; 1.20 A; A=2-108. DR PDB; 4ODP; X-ray; 1.75 A; A=85-97. DR PDB; 4ODQ; X-ray; 2.00 A; A=85-97. DR PDB; 4ODR; X-ray; 1.93 A; A/B=85-97. DR PDB; 5I7P; X-ray; 2.00 A; A=2-84, A=98-108. DR PDB; 5I7Q; X-ray; 1.90 A; A=2-84, A=97-108. DR PDB; 6I1S; X-ray; 1.52 A; B=1-108. DR PDB; 6M4U; X-ray; 2.20 A; A/E=1-108. DR PDB; 6OQA; X-ray; 2.20 A; A/B/E/F=1-108. DR PDB; 6VCU; X-ray; 1.69 A; A/B/C/D=1-108. DR PDB; 6YF0; X-ray; 1.55 A; A=2-108. DR PDB; 6YF1; X-ray; 1.12 A; A=2-108. DR PDB; 6YF2; X-ray; 1.03 A; A=2-108. DR PDB; 6YF3; X-ray; 1.00 A; A=2-108. DR PDB; 7EPD; EM; 3.90 A; A=2-108. DR PDB; 7U0T; X-ray; 2.45 A; B=2-108. DR PDB; 7U8D; X-ray; 1.39 A; A/B=2-108. DR PDB; 8CHI; X-ray; 1.70 A; A/B=2-108. DR PDB; 8CHJ; X-ray; 1.70 A; A/B/C/D=2-108. DR PDB; 8CHK; X-ray; 1.55 A; A/B/C=2-108. DR PDB; 8CHL; X-ray; 1.40 A; A/B=2-108. DR PDB; 8CHM; X-ray; 1.12 A; A=2-108. DR PDB; 8ER6; X-ray; 2.81 A; A/C/E=2-108. DR PDB; 8ER7; X-ray; 3.07 A; A/C/E=2-108. DR PDB; 8ERA; EM; 2.86 A; B=2-108. DR PDB; 8JCU; EM; 2.80 A; 2=2-108. DR PDB; 8JCV; EM; 3.40 A; 2=18-108. DR PDB; 8JCW; EM; 3.00 A; 2=2-108. DR PDB; 8JCX; EM; 3.00 A; 2=2-108. DR PDB; 8JCY; EM; 2.90 A; 2=2-108. DR PDB; 8JCZ; EM; 3.00 A; 2=2-108. DR PDB; 8JD0; EM; 3.30 A; 2=2-108. DR PDB; 8JD1; EM; 3.70 A; 2=2-108. DR PDB; 8JD2; EM; 2.80 A; 2=2-108. DR PDB; 8JD4; EM; 2.90 A; 2=2-108. DR PDB; 8PDF; X-ray; 1.20 A; A=2-108. DR PDB; 8PPZ; X-ray; 1.85 A; A=2-108. DR PDBsum; 1A7X; -. DR PDBsum; 1B6C; -. DR PDBsum; 1BKF; -. DR PDBsum; 1BL4; -. DR PDBsum; 1D6O; -. DR PDBsum; 1D7H; -. DR PDBsum; 1D7I; -. DR PDBsum; 1D7J; -. DR PDBsum; 1EYM; -. DR PDBsum; 1F40; -. DR PDBsum; 1FAP; -. DR PDBsum; 1FKB; -. DR PDBsum; 1FKD; -. DR PDBsum; 1FKF; -. DR PDBsum; 1FKG; -. DR PDBsum; 1FKH; -. DR PDBsum; 1FKI; -. DR PDBsum; 1FKJ; -. DR PDBsum; 1FKR; -. DR PDBsum; 1FKS; -. DR PDBsum; 1FKT; -. DR PDBsum; 1J4H; -. DR PDBsum; 1J4I; -. DR PDBsum; 1J4R; -. DR PDBsum; 1NSG; -. DR PDBsum; 1QPF; -. DR PDBsum; 1QPL; -. DR PDBsum; 2DG3; -. DR PDBsum; 2DG4; -. DR PDBsum; 2DG9; -. DR PDBsum; 2FAP; -. DR PDBsum; 2FKE; -. DR PDBsum; 2ND5; -. DR PDBsum; 2PPN; -. DR PDBsum; 2PPO; -. DR PDBsum; 2PPP; -. DR PDBsum; 2RSE; -. DR PDBsum; 3FAP; -. DR PDBsum; 3H9R; -. DR PDBsum; 3MDY; -. DR PDBsum; 4DH0; -. DR PDBsum; 4FAP; -. DR PDBsum; 4IPX; -. DR PDBsum; 4N19; -. DR PDBsum; 4ODP; -. DR PDBsum; 4ODQ; -. DR PDBsum; 4ODR; -. DR PDBsum; 5I7P; -. DR PDBsum; 5I7Q; -. DR PDBsum; 6I1S; -. DR PDBsum; 6M4U; -. DR PDBsum; 6OQA; -. DR PDBsum; 6VCU; -. DR PDBsum; 6YF0; -. DR PDBsum; 6YF1; -. DR PDBsum; 6YF2; -. DR PDBsum; 6YF3; -. DR PDBsum; 7EPD; -. DR PDBsum; 7U0T; -. DR PDBsum; 7U8D; -. DR PDBsum; 8CHI; -. DR PDBsum; 8CHJ; -. DR PDBsum; 8CHK; -. DR PDBsum; 8CHL; -. DR PDBsum; 8CHM; -. DR PDBsum; 8ER6; -. DR PDBsum; 8ER7; -. DR PDBsum; 8ERA; -. DR PDBsum; 8JCU; -. DR PDBsum; 8JCV; -. DR PDBsum; 8JCW; -. DR PDBsum; 8JCX; -. DR PDBsum; 8JCY; -. DR PDBsum; 8JCZ; -. DR PDBsum; 8JD0; -. DR PDBsum; 8JD1; -. DR PDBsum; 8JD2; -. DR PDBsum; 8JD4; -. DR PDBsum; 8PDF; -. DR PDBsum; 8PPZ; -. DR AlphaFoldDB; P62942; -. DR BMRB; P62942; -. DR EMDB; EMD-28551; -. DR EMDB; EMD-36165; -. DR EMDB; EMD-36166; -. DR EMDB; EMD-36167; -. DR EMDB; EMD-36168; -. DR EMDB; EMD-36169; -. DR EMDB; EMD-36170; -. DR EMDB; EMD-36171; -. DR EMDB; EMD-36172; -. DR EMDB; EMD-36173; -. DR EMDB; EMD-36175; -. DR SMR; P62942; -. DR BioGRID; 108570; 108. DR CORUM; P62942; -. DR DIP; DIP-29710N; -. DR IntAct; P62942; 30. DR MINT; P62942; -. DR STRING; 9606.ENSP00000383003; -. DR BindingDB; P62942; -. DR ChEMBL; CHEMBL1902; -. DR DrugBank; DB08520; (21S)-1AZA-4,4-DIMETHYL-6,19-DIOXA-2,3,7,20-TETRAOXOBICYCLO[19.4.0] PENTACOSANE. DR DrugBank; DB04012; (3r)-4-(P-Toluenesulfonyl)-1,4-Thiazane-3-Carboxylicacid-L-Leucine. DR DrugBank; DB01712; (3R)-4-(p-toluenesulfonyl)-1,4-thiazane-3-carboxylicacid-L-phenylalanine ethyl ester. DR DrugBank; DB04094; 4-hydroxybutan-2-one. DR DrugBank; DB08597; Dorsomorphin. DR DrugBank; DB02888; FKB-001. DR DrugBank; DB01951; Gpi-1046. DR DrugBank; DB05814; GPI-1485. DR DrugBank; DB03338; Heptyl glucoside. DR DrugBank; DB03621; L-709,587. DR DrugBank; DB02311; Methyl Methylsulfinylmethyl Sulfide. DR DrugBank; DB08231; Myristic acid. DR DrugBank; DB00337; Pimecrolimus. DR DrugBank; DB00864; Tacrolimus. DR DrugBank; DB01723; {3-[3-(3,4-Dimethoxy-Phenyl)-1-(1-{1-[2-(3,4,5-Trimethoxy-Phenyl)-Butyryl]-Piperidin-2yl}-Vinyloxy)-Propyl]-Phenoxy}-Acetic Acid. DR DrugCentral; P62942; -. DR GuidetoPHARMACOLOGY; 2609; -. DR TCDB; 8.A.11.1.2; the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family. DR GlyGen; P62942; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62942; -. DR MetOSite; P62942; -. DR PhosphoSitePlus; P62942; -. DR SwissPalm; P62942; -. DR BioMuta; FKBP1A; -. DR EPD; P62942; -. DR jPOST; P62942; -. DR MassIVE; P62942; -. DR MaxQB; P62942; -. DR PaxDb; 9606-ENSP00000383003; -. DR PeptideAtlas; P62942; -. DR ProteomicsDB; 57456; -. DR Pumba; P62942; -. DR TopDownProteomics; P62942; -. DR Antibodypedia; 23072; 472 antibodies from 39 providers. DR DNASU; 2280; -. DR Ensembl; ENST00000381719.8; ENSP00000371138.3; ENSG00000088832.18. DR Ensembl; ENST00000381724.8; ENSP00000371143.4; ENSG00000088832.18. DR Ensembl; ENST00000400137.9; ENSP00000383003.4; ENSG00000088832.18. DR Ensembl; ENST00000677335.1; ENSP00000503033.1; ENSG00000088832.18. DR Ensembl; ENST00000678408.1; ENSP00000503152.1; ENSG00000088832.18. DR GeneID; 2280; -. DR KEGG; hsa:2280; -. DR MANE-Select; ENST00000400137.9; ENSP00000383003.4; NM_000801.5; NP_000792.1. DR UCSC; uc002wey.4; human. DR AGR; HGNC:3711; -. DR CTD; 2280; -. DR DisGeNET; 2280; -. DR GeneCards; FKBP1A; -. DR HGNC; HGNC:3711; FKBP1A. DR HPA; ENSG00000088832; Low tissue specificity. DR MIM; 186945; gene. DR neXtProt; NX_P62942; -. DR OpenTargets; ENSG00000088832; -. DR PharmGKB; PA28153; -. DR VEuPathDB; HostDB:ENSG00000088832; -. DR eggNOG; KOG0544; Eukaryota. DR GeneTree; ENSGT00940000153311; -. DR HOGENOM; CLU_013615_12_1_1; -. DR InParanoid; P62942; -. DR OMA; FTSMNNQ; -. DR OrthoDB; 25281at2759; -. DR PhylomeDB; P62942; -. DR TreeFam; TF105291; -. DR BRENDA; 5.2.1.8; 2681. DR PathwayCommons; P62942; -. DR Reactome; R-HSA-166208; mTORC1-mediated signalling. DR Reactome; R-HSA-2025928; Calcineurin activates NFAT. DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition). DR Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SignaLink; P62942; -. DR SIGNOR; P62942; -. DR BioGRID-ORCS; 2280; 244 hits in 1072 CRISPR screens. DR ChiTaRS; FKBP1A; human. DR EvolutionaryTrace; P62942; -. DR GeneWiki; FKBP1A; -. DR GenomeRNAi; 2280; -. DR Pharos; P62942; Tclin. DR PRO; PR:P62942; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P62942; Protein. DR Bgee; ENSG00000088832; Expressed in right lung and 205 other cell types or tissues. DR ExpressionAtlas; P62942; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0016020; C:membrane; IDA:BHF-UCL. DR GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB. DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0014802; C:terminal cisterna; ISS:BHF-UCL. DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL. DR GO; GO:0070697; F:activin receptor binding; IPI:BHF-UCL. DR GO; GO:0005528; F:FK506 binding; IDA:BHF-UCL. DR GO; GO:0070411; F:I-SMAD binding; IPI:BHF-UCL. DR GO; GO:0005527; F:macrolide binding; NAS:BHF-UCL. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL. DR GO; GO:0030547; F:signaling receptor inhibitor activity; IDA:BHF-UCL. DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; ISS:BHF-UCL. DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IPI:FlyBase. DR GO; GO:0006458; P:'de novo' protein folding; TAS:BHF-UCL. DR GO; GO:1990000; P:amyloid fibril formation; IDA:BHF-UCL. DR GO; GO:0070588; P:calcium ion transmembrane transport; NAS:BHF-UCL. DR GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL. DR GO; GO:0060347; P:heart trabecula formation; ISS:BHF-UCL. DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:FlyBase. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL. DR GO; GO:0006457; P:protein folding; NAS:UniProtKB. DR GO; GO:0022417; P:protein maturation by protein folding; TAS:BHF-UCL. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:BHF-UCL. DR GO; GO:0042026; P:protein refolding; TAS:BHF-UCL. DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IGI:ParkinsonsUK-UCL. DR GO; GO:0050776; P:regulation of immune response; IMP:BHF-UCL. DR GO; GO:0032880; P:regulation of protein localization; IGI:ParkinsonsUK-UCL. DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL. DR GO; GO:0097435; P:supramolecular fiber organization; IDA:BHF-UCL. DR GO; GO:0042110; P:T cell activation; NAS:BHF-UCL. DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL. DR Gene3D; 3.10.50.40; -; 1. DR InterPro; IPR046357; PPIase_dom_sf. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR10516:SF301; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP1A-RELATED; 1. DR Pfam; PF00254; FKBP_C; 1. DR SUPFAM; SSF54534; FKBP-like; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. DR Genevisible; P62942; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Isomerase; KW Membrane; Reference proteome; Rotamase; Sarcoplasmic reticulum. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0000269|PubMed:1701173, ECO:0000269|PubMed:2477715" FT CHAIN 2..108 FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1A" FT /id="PRO_0000075289" FT DOMAIN 20..108 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277" FT MOD_RES 53 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26883" FT MOD_RES 53 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26883" FT CONFLICT 60 FT /note="W -> R (in Ref. 6; CAG28541)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="I -> V (in Ref. 6; CAG28541)" FT /evidence="ECO:0000305" FT STRAND 3..9 FT /evidence="ECO:0007829|PDB:2PPN" FT STRAND 22..31 FT /evidence="ECO:0007829|PDB:2PPN" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:8ER7" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:2PPN" FT HELIX 40..43 FT /evidence="ECO:0007829|PDB:2PPN" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:2PPN" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:7U8D" FT HELIX 58..64 FT /evidence="ECO:0007829|PDB:2PPN" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:2PPN" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2PPN" FT TURN 82..86 FT /evidence="ECO:0007829|PDB:2PPN" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:2PPN" FT STRAND 98..108 FT /evidence="ECO:0007829|PDB:2PPN" SQ SEQUENCE 108 AA; 11951 MW; 9CC8493C802540B4 CRC64; MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFM LGKQEVIRGW EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPHATLVF DVELLKLE //