FKB1B_RABIT
ID FKB1B_RABIT Reviewed; 108 AA.
AC Q8HYX6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 84.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Heart;
RX PubMed=15033987; DOI=10.1074/jbc.m309574200;
RA Lee E.H., Rho S.H., Kwon S.J., Eom S.H., Allen P.D., Kim D.H.;
RT "N-terminal region of FKBP12 is essential for binding to the skeletal
RT ryanodine receptor.";
RL J. Biol. Chem. 279:26481-26488(2004).
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 -!- 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 {ECO:0000250}.
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:0000250}. Sarcoplasmic reticulum
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY159324; AAN72433.1; -; mRNA.
DR RefSeq; NP_001075614.1; NM_001082145.1.
DR AlphaFoldDB; Q8HYX6; -.
DR BMRB; Q8HYX6; -.
DR SMR; Q8HYX6; -.
DR PRIDE; Q8HYX6; -.
DR GeneID; 100008888; -.
DR KEGG; ocu:100008888; -.
DR CTD; 2281; -.
DR InParanoid; Q8HYX6; -.
DR OrthoDB; 1328688at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:AgBase.
DR GO; GO:0014802; C:terminal cisterna; IDA:AgBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:AgBase.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP: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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Reference proteome; Rotamase; Sarcoplasmic reticulum.
FT CHAIN 1..108
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1B"
FT /id="PRO_0000075297"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 108 AA; 11724 MW; 15C2A25945F63AC6 CRC64;
MGVEIETISP GDGRTFPKKG QTCVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGAAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF GVELLNLE
