FKB1B_BOVIN
ID FKB1B_BOVIN Reviewed; 108 AA.
AC P68107; A5D7G8; Q13664; Q16645; Q9BQ40;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=FK506-binding protein 1B;
DE Short=FKBP-1B;
DE AltName: Full=Immunophilin FKBP12.6;
DE AltName: Full=Rotamase;
GN Name=FKBP1B; Synonyms=FKBP12.6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-108, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain;
RX PubMed=7520438; DOI=10.1016/s0021-9258(17)31934-8;
RA Sewell T.J., Lam E., Martin M.M., Leszyk J., Weidner J., Calaycay J.,
RA Griffin P., Williams H., Hung S., Cryan J., Sigal N.H., Wiederrecht G.J.;
RT "Inhibition of calcineurin by a novel FK-506-binding protein.";
RL J. Biol. Chem. 269:21094-21102(1994).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:7520438}.
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. Interacts directly with RYR2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7520438}.
CC Sarcoplasmic reticulum {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=11652; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:7520438};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC140549; AAI40550.1; -; mRNA.
DR PIR; A53924; A53924.
DR RefSeq; NP_001091627.1; NM_001098158.1.
DR AlphaFoldDB; P68107; -.
DR BMRB; P68107; -.
DR SMR; P68107; -.
DR STRING; 9913.ENSBTAP00000004419; -.
DR PaxDb; P68107; -.
DR Ensembl; ENSBTAT00000004419; ENSBTAP00000004419; ENSBTAG00000003409.
DR GeneID; 785179; -.
DR KEGG; bta:785179; -.
DR CTD; 2281; -.
DR VEuPathDB; HostDB:ENSBTAG00000003409; -.
DR VGNC; VGNC:29021; FKBP1B.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000153311; -.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; P68107; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 435947at2759; -.
DR TreeFam; TF105291; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003409; Expressed in semen and 88 other tissues.
DR ExpressionAtlas; P68107; baseline.
DR GO; GO:0034704; C:calcium channel complex; ISA:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISA:AgBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISA:AgBase.
DR GO; GO:0016020; C:membrane; ISA:AgBase.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISA:AgBase.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISA:AgBase.
DR GO; GO:0030018; C:Z disc; ISA:AgBase.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISA:AgBase.
DR GO; GO:0030551; F:cyclic nucleotide binding; ISA:AgBase.
DR GO; GO:0005528; F:FK506 binding; ISA:AgBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISA:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; ISA:AgBase.
DR GO; GO:0044325; F:transmembrane transporter binding; ISA:AgBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; ISA:AgBase.
DR GO; GO:0010459; P:negative regulation of heart rate; ISA:AgBase.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISA:AgBase.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISA:AgBase.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISA:AgBase.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
DR GO; GO:0019227; P:neuronal action potential propagation; ISA:AgBase.
DR GO; GO:0048680; P:positive regulation of axon regeneration; ISA:AgBase.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISA:AgBase.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; ISA:AgBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISA:AgBase.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; ISA:AgBase.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISA:AgBase.
DR GO; GO:0002027; P:regulation of heart rate; ISA:AgBase.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISA:AgBase.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISA:AgBase.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISA:AgBase.
DR GO; GO:0009749; P:response to glucose; ISA:AgBase.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISA:AgBase.
DR GO; GO:0010033; P:response to organic substance; ISA:AgBase.
DR GO; GO:0051775; P:response to redox state; ISA:AgBase.
DR GO; GO:0033197; P:response to vitamin E; ISA:AgBase.
DR GO; GO:0006939; P:smooth muscle contraction; ISA:AgBase.
DR GO; GO:0042098; P:T cell proliferation; ISA:AgBase.
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; Direct protein sequencing; Isomerase; Reference proteome;
KW Rotamase; Sarcoplasmic reticulum.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7520438"
FT CHAIN 2..108
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1B"
FT /id="PRO_0000075294"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 108 AA; 11783 MW; BAC2A25945F63AC4 CRC64;
MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLNLE
