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Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase)

 FKB1A_BOVIN             Reviewed;         108 AA.
P18203; Q5E945;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
07-JUN-2017, entry version 146.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
Short=PPIase FKBP1A;
EC=5.2.1.8 {ECO:0000250|UniProtKB:P62942};
AltName: Full=12 kDa FK506-binding protein;
Short=12 kDa FKBP;
Short=FKBP-12;
AltName: Full=Calstabin-1;
AltName: Full=FK506-binding protein 1A;
Short=FKBP-1A;
AltName: Full=Immunophilin FKBP12;
AltName: Full=Rotamase;
Name=FKBP1A; Synonyms=FKBP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
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.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
PROTEIN SEQUENCE OF 2-108.
TISSUE=Brain;
PubMed=2253615; DOI=10.1111/j.1432-1033.1990.tb19421.x;
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.;
"Amino acid sequence of a 12-kDa inhibitor of protein kinase C.";
Eur. J. Biochem. 194:19-23(1990).
[3]
PROTEIN SEQUENCE OF 2-108.
TISSUE=Thymus;
PubMed=1718307; DOI=10.1007/BF01024778;
Lane W.S., Galat A., Harding M.W., Schreiber S.L.;
"Complete amino acid sequence of the FK506 and rapamycin binding
protein, FKBP, isolated from calf thymus.";
J. Protein Chem. 10:151-160(1991).
[4]
PROTEIN SEQUENCE OF 2-87.
PubMed=1701173;
Siekierka J.J., Widerrecht G., Greulich H., Boulton D., Hung S.H.Y.,
Cryan J., Hodges P.J., Sigal N.H.;
"The cytosolic-binding protein for the immunosuppressant FK-506 is
both a ubiquitous and highly conserved peptidyl-prolyl cis-trans
isomerase.";
J. Biol. Chem. 265:21011-21015(1990).
[5]
PROTEIN SEQUENCE OF 2-41.
PubMed=2477715; DOI=10.1038/341758a0;
Harding M.W., Galat A., Uehling D.E., Schreiber S.L.;
"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-
prolyl isomerase.";
Nature 341:758-760(1989).
[6]
IDENTITY OF FKBP AND PKCI-2.
PubMed=1706222; DOI=10.1016/0092-8674(91)90258-Z;
Goebl M.G.;
"The peptidyl-prolyl isomerase, FK506-binding protein, is most likely
the 12 kd endogenous inhibitor 2 of protein kinase C.";
Cell 64:1051-1052(1991).
[7]
IDENTITY OF FKBP AND PKCI-2.
PubMed=1710319; DOI=10.1038/351195a0;
Tropschug A.M., Hofmann R.;
"FK506 and protein kinase C.";
Nature 351:195-195(1991).
[8]
SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
PubMed=1868545; DOI=10.1016/0092-8674(81)90004-0;
Goebl M.;
"The peptidyl-prolyl isomerase, FK506-binding protein, is not
identical to protein kinase C inhibitor 2.";
Cell 66:423-423(1991).
[9]
SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
PubMed=1915353; DOI=10.1111/j.1432-1033.1991.tb16249.x;
Walsh M.P.;
"Retraction concerning amino acid sequence of a 12-kDa inhibitor of
protein kinase C. Mistaken identity of a protein kinase C inhibitor.";
Eur. J. Biochem. 200:811-811(1991).
[10]
SHOWS THAT THE PROTEIN IS NOT AN INHIBITOR OF PROTEIN KINASE C.
PubMed=1710782; DOI=10.1038/351527c0;
Albers M.W., Liu J., Schreiber S.L.;
"Relationship of FKBP to PKCI-2.";
Nature 351:527-527(1991).
[11]
STRUCTURE BY NMR.
PubMed=2041572; DOI=10.1038/351248a0;
Moore J.M., Peattie D.A., Fitzgibbon M.J., Thomson J.A.;
"Solution structure of the major binding protein for the
immunosuppressant FK506.";
Nature 351:248-250(1991).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
PubMed=7543369; DOI=10.1016/0092-8674(95)90439-5;
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.;
"X-ray structure of calcineurin inhibited by the immunophilin-
immunosuppressant FKBP12-FK506 complex.";
Cell 82:507-522(1995).
-!- 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). {ECO:0000250|UniProtKB:P62942}.
-!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
-!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by
TGFBR2 and stabilizes it in the inactive conformation (By
similarity). Interacts with ACVR1B and SMAD7. Identified in a
complex composed of RYR1, PDE4D, PKA, FKBP1A and protein
phosphatase 1 (PP1). Interacts directly with RYR2 and RYR3 (By
similarity). Interacts directly with RYR1 (By similarity).
{ECO:0000250|UniProtKB:P26883, ECO:0000250|UniProtKB:P62942,
ECO:0000250|UniProtKB:P62943, ECO:0000250|UniProtKB:Q62658}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P62943}; Cytoplasmic side
{ECO:0000250|UniProtKB:P62943}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
-!- 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). {ECO:0000305|PubMed:2253615}.
-----------------------------------------------------------------------
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EMBL; BT021075; AAX09092.1; -; mRNA.
PIR; A61431; A61431.
RefSeq; NP_001030533.1; NM_001035456.1.
UniGene; Bt.63982; -.
PDB; 1FKK; X-ray; 2.20 A; A=2-108.
PDB; 1FKL; X-ray; 1.70 A; A=2-108.
PDB; 1TCO; X-ray; 2.50 A; C=2-108.
PDBsum; 1FKK; -.
PDBsum; 1FKL; -.
PDBsum; 1TCO; -.
ProteinModelPortal; P18203; -.
SMR; P18203; -.
STRING; 9913.ENSBTAP00000010928; -.
BindingDB; P18203; -.
PaxDb; P18203; -.
PeptideAtlas; P18203; -.
PRIDE; P18203; -.
Ensembl; ENSBTAT00000010928; ENSBTAP00000010928; ENSBTAG00000008303.
GeneID; 614795; -.
KEGG; bta:614795; -.
CTD; 2280; -.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOVERGEN; HBG051623; -.
InParanoid; P18203; -.
KO; K09568; -.
OMA; RVIAGWD; -.
OrthoDB; EOG091G02W1; -.
TreeFam; TF105291; -.
Reactome; R-BTA-2173789; TGF-beta receptor signaling activates SMADs.
EvolutionaryTrace; P18203; -.
Proteomes; UP000009136; Chromosome 13.
Bgee; ENSBTAG00000008303; -.
GO; GO:0005737; C:cytoplasm; ISA:AgBase.
GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; ISA:AgBase.
GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISA:AgBase.
GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISA:AgBase.
GO; GO:0030018; C:Z disc; ISA:AgBase.
GO; GO:0048185; F:activin binding; ISA:AgBase.
GO; GO:0019855; F:calcium channel inhibitor activity; ISA:AgBase.
GO; GO:0008144; F:drug binding; ISA:AgBase.
GO; GO:0005528; F:FK506 binding; ISA:AgBase.
GO; GO:0044325; F:ion channel binding; ISA:AgBase.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISA:AgBase.
GO; GO:0004871; F:signal transducer activity; ISA:AgBase.
GO; GO:0046332; F:SMAD binding; ISA:AgBase.
GO; GO:1990000; P:amyloid fibril formation; ISA:AgBase.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISA:AgBase.
GO; GO:0003007; P:heart morphogenesis; ISA:AgBase.
GO; GO:0060347; P:heart trabecula formation; ISA:AgBase.
GO; GO:0006936; P:muscle contraction; ISA:AgBase.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISA:AgBase.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISA:AgBase.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISA:AgBase.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISA:AgBase.
GO; GO:0032092; P:positive regulation of protein binding; ISA:AgBase.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISA:AgBase.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISA:AgBase.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; ISA:AgBase.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISA:AgBase.
GO; GO:0050776; P:regulation of immune response; ISA:AgBase.
GO; GO:0032880; P:regulation of protein localization; ISA:AgBase.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISA:AgBase.
GO; GO:0031000; P:response to caffeine; ISA:AgBase.
GO; GO:0007183; P:SMAD protein complex assembly; ISA:AgBase.
GO; GO:0097435; P:supramolecular fiber organization; ISA:AgBase.
GO; GO:0042110; P:T cell activation; NAS:BHF-UCL.
GO; GO:0042098; P:T cell proliferation; ISA:AgBase.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISA:AgBase.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isomerase; Membrane; Reference proteome;
Rotamase; Sarcoplasmic reticulum.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1701173,
ECO:0000269|PubMed:1718307,
ECO:0000269|PubMed:2253615,
ECO:0000269|PubMed:2477715}.
CHAIN 2 108 Peptidyl-prolyl cis-trans isomerase
FKBP1A.
/FTId=PRO_0000075288.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOD_RES 53 53 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
MOD_RES 53 53 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
STRAND 3 9 {ECO:0000244|PDB:1FKL}.
STRAND 22 31 {ECO:0000244|PDB:1FKL}.
STRAND 36 40 {ECO:0000244|PDB:1FKL}.
TURN 41 44 {ECO:0000244|PDB:1FKL}.
STRAND 47 50 {ECO:0000244|PDB:1FKL}.
STRAND 53 56 {ECO:0000244|PDB:1FKL}.
HELIX 58 65 {ECO:0000244|PDB:1FKL}.
STRAND 72 77 {ECO:0000244|PDB:1FKL}.
HELIX 79 81 {ECO:0000244|PDB:1FKL}.
TURN 82 86 {ECO:0000244|PDB:1FKL}.
TURN 89 91 {ECO:0000244|PDB:1FKL}.
STRAND 98 108 {ECO:0000244|PDB:1FKL}.
SEQUENCE 108 AA; 11910 MW; 9CD0F1278039C5B4 CRC64;
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFV LGKQEVIRGW
EEGVAQMSVG QRAKLTISPD YAYGATGHPG IIPPNATLIF DVELLKLE


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