FKB1B_RAT
ID FKB1B_RAT Reviewed; 108 AA.
AC P97534;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1B;
DE Short=PPIase FKBP1B;
DE EC=5.2.1.8;
DE AltName: Full=12.6 kDa FK506-binding protein;
DE Short=12.6 kDa FKBP;
DE Short=FKBP-12.6;
DE AltName: Full=Calstabin-2;
DE AltName: Full=FK506-binding protein 1B;
DE Short=FKBP-1B;
DE AltName: Full=Immunophilin FKBP12.6;
DE AltName: Full=Rotamase;
GN Name=Fkbp1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreatic islet;
RX PubMed=9013543; DOI=10.1074/jbc.272.6.3133;
RA Noguchi N., Takasawa S., Nata K., Tohgo A., Kato I., Ikehata F.,
RA Yonekura H., Okamoto H.;
RT "Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from
RT islet microsomes.";
RL J. Biol. Chem. 272:3133-3136(1997).
RN [2]
RP INTERACTION WITH RYR2, AND TISSUE SPECIFICITY.
RX PubMed=20431056; DOI=10.1161/circresaha.110.219816;
RA Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E., Fruen B.R.,
RA Bers D.M.;
RT "Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized
RT cardiac myocytes and effects on Ca sparks.";
RL Circ. Res. 106:1743-1752(2010).
CC -!- FUNCTION: Has the potential to contribute to the immunosuppressive and
CC toxic effects of FK506 and rapamycin. PPIases accelerate the folding of
CC proteins. It catalyzes the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides.
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;
CC -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC -!- SUBUNIT: Identified in a complex composed of RYR2, FKBP1B, PKA
CC catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A
CC and PP1 (By similarity). Interacts directly with RYR2. {ECO:0000250,
CC ECO:0000269|PubMed:20431056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Sarcoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Detected in heart muscle (at protein level).
CC Ubiquitous. {ECO:0000269|PubMed:20431056}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Has been suggested to play a role in the regulation of RYR2
CC channel activity and thereby contribute to the regulation of
CC excitation-contraction coupling in cardiac muscle. According to
CC PubMed:20431056, the amount of FKBP1B in rat heart is much lower than
CC that of RYR2, suggesting that FKBP1B can play only a minor role in the
CC regulation of RYR2 channel activity. {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; D86642; BAA13154.1; -; mRNA.
DR RefSeq; NP_073166.1; NM_022675.1.
DR AlphaFoldDB; P97534; -.
DR BMRB; P97534; -.
DR SMR; P97534; -.
DR CORUM; P97534; -.
DR STRING; 10116.ENSRNOP00000067023; -.
DR iPTMnet; P97534; -.
DR PhosphoSitePlus; P97534; -.
DR jPOST; P97534; -.
DR PaxDb; P97534; -.
DR PRIDE; P97534; -.
DR Ensembl; ENSRNOT00000071784; ENSRNOP00000067023; ENSRNOG00000047143.
DR GeneID; 58950; -.
DR KEGG; rno:58950; -.
DR CTD; 2281; -.
DR RGD; 61835; Fkbp1b.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000153311; -.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; P97534; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; P97534; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P97534; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000047143; Expressed in frontal cortex and 14 other tissues.
DR Genevisible; P97534; RN.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:RGD.
DR GO; GO:0030551; F:cyclic nucleotide binding; IDA:RGD.
DR GO; GO:0005528; F:FK506 binding; IDA:RGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; ISO:RGD.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; ISO:RGD.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISO:RGD.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0051775; P:response to redox state; ISO:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0006939; P:smooth muscle contraction; ISO:RGD.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase; Sarcoplasmic reticulum.
FT CHAIN 1..108
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1B"
FT /id="PRO_0000075298"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 108 AA; 11795 MW; 36136F4588F62F0B CRC64;
MGVEIETISP GDGRTFPKKG QICVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE
