FKB1B_MOUSE
ID FKB1B_MOUSE Reviewed; 108 AA.
AC Q9Z2I2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=9880681; DOI=10.1007/s003359900928;
RA Bennett J.A., Clancy Y.C., McNeish J.D.;
RT "Identification and characterization of the murine FK506 binding protein
RT (FKBP) 12.6 gene.";
RL Mamm. Genome 9:1069-1071(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(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 (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 -!- INTERACTION:
CC Q9Z2I2; E9Q401: Ryr2; NbExp=3; IntAct=EBI-6379859, EBI-643628;
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}.
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; AF060872; AAC64923.1; -; mRNA.
DR EMBL; AK005201; BAB23879.1; -; mRNA.
DR EMBL; BC061121; AAH61121.1; -; mRNA.
DR CCDS; CCDS25792.1; -.
DR RefSeq; NP_058559.3; NM_016863.3.
DR AlphaFoldDB; Q9Z2I2; -.
DR BMRB; Q9Z2I2; -.
DR SMR; Q9Z2I2; -.
DR BioGRID; 199683; 3.
DR DIP; DIP-61117N; -.
DR IntAct; Q9Z2I2; 1.
DR STRING; 10090.ENSMUSP00000020964; -.
DR iPTMnet; Q9Z2I2; -.
DR PhosphoSitePlus; Q9Z2I2; -.
DR MaxQB; Q9Z2I2; -.
DR PaxDb; Q9Z2I2; -.
DR PRIDE; Q9Z2I2; -.
DR ProteomicsDB; 267476; -.
DR Antibodypedia; 27417; 134 antibodies from 29 providers.
DR DNASU; 14226; -.
DR Ensembl; ENSMUST00000020964; ENSMUSP00000020964; ENSMUSG00000020635.
DR GeneID; 14226; -.
DR KEGG; mmu:14226; -.
DR UCSC; uc007myj.1; mouse.
DR CTD; 2281; -.
DR MGI; MGI:1336205; Fkbp1b.
DR VEuPathDB; HostDB:ENSMUSG00000020635; -.
DR eggNOG; KOG0544; Eukaryota.
DR GeneTree; ENSGT00940000153311; -.
DR HOGENOM; CLU_013615_12_1_1; -.
DR InParanoid; Q9Z2I2; -.
DR OMA; RVIAGWD; -.
DR OrthoDB; 1328688at2759; -.
DR PhylomeDB; Q9Z2I2; -.
DR TreeFam; TF105291; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 14226; 3 hits in 70 CRISPR screens.
DR PRO; PR:Q9Z2I2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9Z2I2; protein.
DR Bgee; ENSMUSG00000020635; Expressed in trigeminal ganglion and 208 other tissues.
DR ExpressionAtlas; Q9Z2I2; baseline and differential.
DR Genevisible; Q9Z2I2; MM.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0030018; C:Z disc; ISO:MGI.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:MGI.
DR GO; GO:0030551; F:cyclic nucleotide binding; ISO:MGI.
DR GO; GO:0005528; F:FK506 binding; IDA:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR GO; GO:0048680; P:positive regulation of axon regeneration; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:MGI.
DR GO; GO:0051284; P:positive regulation of sequestering of calcium ion; ISO:MGI.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISO:MGI.
DR GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:BHF-UCL.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:MGI.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; ISO:MGI.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
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_0000075296"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 108 AA; 11798 MW; 36137EB599F62F1A CRC64;
MGVEIETISP GDGRTFPKKG QICVVHYTGM LQNGKKFDSS RDRNKPFKFR IGKQEVIKGF
EEGTAQMSLG QRAKLTCTPD VAYGATGHPG VIPPNATLIF DVELLSLE
