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Peptidyl-prolyl cis-trans isomerase FKBP1B (PPIase FKBP1B) (EC 5.2.1.8) (12.6 kDa FK506-binding protein) (12.6 kDa FKBP) (FKBP-12.6) (Calstabin-2) (FK506-binding protein 1B) (FKBP-1B) (Immunophilin FKBP12.6) (Rotamase)

 FKB1B_RAT               Reviewed;         108 AA.
P97534;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 118.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1B;
Short=PPIase FKBP1B;
EC=5.2.1.8;
AltName: Full=12.6 kDa FK506-binding protein;
Short=12.6 kDa FKBP;
Short=FKBP-12.6;
AltName: Full=Calstabin-2;
AltName: Full=FK506-binding protein 1B;
Short=FKBP-1B;
AltName: Full=Immunophilin FKBP12.6;
AltName: Full=Rotamase;
Name=Fkbp1b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Pancreatic islet;
PubMed=9013543; DOI=10.1074/jbc.272.6.3133;
Noguchi N., Takasawa S., Nata K., Tohgo A., Kato I., Ikehata F.,
Yonekura H., Okamoto H.;
"Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+
from islet microsomes.";
J. Biol. Chem. 272:3133-3136(1997).
[2]
INTERACTION WITH RYR2, AND TISSUE SPECIFICITY.
PubMed=20431056; DOI=10.1161/CIRCRESAHA.110.219816;
Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E.,
Fruen B.R., Bers D.M.;
"Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized
cardiac myocytes and effects on Ca sparks.";
Circ. Res. 106:1743-1752(2010).
-!- FUNCTION: Has the potential to contribute to the immunosuppressive
and toxic effects of FK506 and rapamycin. 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: Identified in a complex composed of RYR2, FKBP1B, PKA
catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases
PP2A and PP1 (By similarity). Interacts directly with RYR2.
{ECO:0000250, ECO:0000269|PubMed:20431056}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic
reticulum.
-!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
Ubiquitous. {ECO:0000269|PubMed:20431056}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
-!- CAUTION: Has been suggested to play a role in the regulation of
RYR2 channel activity and thereby contribute to the regulation of
excitation-contraction coupling in cardiac muscle. According to
PubMed:20431056, the amount of FKBP1B in rat heart is much lower
than that of RYR2, suggesting that FKBP1B can play only a minor
role in the regulation of RYR2 channel activity. {ECO:0000305}.
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EMBL; D86642; BAA13154.1; -; mRNA.
RefSeq; NP_073166.1; NM_022675.1.
UniGene; Rn.46439; -.
ProteinModelPortal; P97534; -.
SMR; P97534; -.
CORUM; P97534; -.
STRING; 10116.ENSRNOP00000067023; -.
iPTMnet; P97534; -.
PhosphoSitePlus; P97534; -.
PaxDb; P97534; -.
PRIDE; P97534; -.
Ensembl; ENSRNOT00000071784; ENSRNOP00000067023; ENSRNOG00000047143.
GeneID; 58950; -.
KEGG; rno:58950; -.
CTD; 2281; -.
RGD; 61835; Fkbp1b.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOVERGEN; HBG051623; -.
InParanoid; P97534; -.
KO; K09568; -.
OMA; WGIMPNS; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; P97534; -.
Reactome; R-RNO-2672351; Stimuli-sensing channels.
Reactome; R-RNO-5578775; Ion homeostasis.
PRO; PR:P97534; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000047143; -.
Genevisible; P97534; RN.
GO; GO:0034704; C:calcium channel complex; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0019855; F:calcium channel inhibitor activity; IEA:Ensembl.
GO; GO:0030551; F:cyclic nucleotide binding; IDA:RGD.
GO; GO:0005528; F:FK506 binding; IDA:RGD.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0010459; P:negative regulation of heart rate; IEA:Ensembl.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
GO; GO:0048680; P:positive regulation of axon regeneration; IDA:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IBA:GO_Central.
GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0051775; P:response to redox state; IEA:Ensembl.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
GO; GO:0006939; P:smooth muscle contraction; IEA:Ensembl.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
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;
Complete proteome; Cytoplasm; Isomerase; Reference proteome; Rotamase;
Sarcoplasmic reticulum.
CHAIN 1 108 Peptidyl-prolyl cis-trans isomerase
FKBP1B.
/FTId=PRO_0000075298.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
SEQUENCE 108 AA; 11795 MW; 36136F4588F62F0B CRC64;
MGVEIETISP GDGRTFPKKG QICVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE


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