ID   FKB1A_MOUSE             Reviewed;         108 AA.
AC   P26883; Q545E9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 192.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
DE            Short=PPIase FKBP1A;
DE            EC=5.2.1.8 {ECO:0000250|UniProtKB:P62942};
DE   AltName: Full=12 kDa FK506-binding protein;
DE            Short=12 kDa FKBP;
DE            Short=FKBP-12;
DE   AltName: Full=Calstabin-1;
DE   AltName: Full=FK506-binding protein 1A;
DE            Short=FKBP-1A;
DE   AltName: Full=Immunophilin FKBP12;
DE   AltName: Full=Rotamase;
GN   Name=Fkbp1a; Synonyms=Fkbp1;
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/6 X CBA;
RX   PubMed=1722474; DOI=10.1016/0378-1119(91)90617-k;
RA   Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.;
RT   "cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced
RT   amino acid sequence.";
RL   Gene 109:255-258(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv;
RA   Shou W., Bao S., Mathews L.S., Matzuk M.M.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants within
RT   alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [6]
RP   IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE
RP   1.
RX   PubMed=18268335; DOI=10.1073/pnas.0711074105;
RA   Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W.,
RA   Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.;
RT   "Remodeling of ryanodine receptor complex causes 'leaky' channels: a
RT   molecular mechanism for decreased exercise capacity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, SUCCINYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-53, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I
CC       serine/threonine kinase receptor, preventing TGF-beta receptor
CC       activation in absence of ligand. Recruits SMAD7 to ACVR1B which
CC       prevents the association of SMAD2 and SMAD3 with the activin receptor
CC       complex, thereby blocking the activin signal. May modulate the RYR1
CC       calcium channel activity. PPIases accelerate the folding of proteins.
CC       It catalyzes the cis-trans isomerization of proline imidic peptide
CC       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         Evidence={ECO:0000250|UniProtKB:P62942};
CC   -!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
CC   -!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by
CC       TGFBR2 and stabilizes it in the inactive conformation (By similarity).
CC       Interacts with ACVR1B and SMAD7 (By similarity). Identified in a
CC       complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1
CC       (PP1) (PubMed:18268335). Interacts directly with RYR2 and RYR3 (By
CC       similarity). Interacts directly with RYR1 (By similarity). Interacts
CC       with GLMN; rapamycin and FK506 abolish the interaction with GLMN in a
CC       dose dependent manner (By similarity). {ECO:0000250|UniProtKB:P62942,
CC       ECO:0000250|UniProtKB:P62943, ECO:0000250|UniProtKB:Q62658,
CC       ECO:0000269|PubMed:18268335}.
CC   -!- INTERACTION:
CC       P26883; E9PZQ0: Ryr1; NbExp=2; IntAct=EBI-6379901, EBI-642079;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P62943}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P62943}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X60203; CAA42762.1; -; mRNA.
DR   EMBL; U65100; AAB17554.1; -; Genomic_DNA.
DR   EMBL; U65098; AAB17554.1; JOINED; Genomic_DNA.
DR   EMBL; U65099; AAB17554.1; JOINED; Genomic_DNA.
DR   EMBL; AF483488; AAL90762.1; -; mRNA.
DR   EMBL; AF483489; AAL90763.1; -; mRNA.
DR   EMBL; AK002777; BAB22351.1; -; mRNA.
DR   EMBL; AK010693; BAB27125.1; -; mRNA.
DR   EMBL; AK019362; BAB31680.1; -; mRNA.
DR   EMBL; AK154751; BAE32804.1; -; mRNA.
DR   EMBL; AK168333; BAE40271.1; -; mRNA.
DR   EMBL; AK169186; BAE40963.1; -; mRNA.
DR   EMBL; AK169242; BAE41008.1; -; mRNA.
DR   EMBL; BC004671; AAH04671.1; -; mRNA.
DR   CCDS; CCDS16869.1; -.
DR   PIR; JH0528; JH0528.
DR   RefSeq; NP_001289006.1; NM_001302077.1.
DR   RefSeq; NP_001289007.1; NM_001302078.1.
DR   RefSeq; NP_001289008.1; NM_001302079.1.
DR   RefSeq; NP_001289009.1; NM_001302080.1.
DR   RefSeq; NP_032045.1; NM_008019.3.
DR   PDB; 8VJJ; EM; 2.53 A; E/F/G/H=1-108.
DR   PDB; 8VJK; EM; 2.92 A; E/F/G/H=1-108.
DR   PDB; 8VK3; EM; 3.21 A; E/F/G/H=1-108.
DR   PDB; 8VK4; EM; 3.56 A; E/F/G/H=1-108.
DR   PDB; 9NMN; EM; 3.09 A; E/F/G/H=1-108.
DR   PDB; 9NMO; EM; 2.40 A; E/F/G/H=1-108.
DR   PDB; 9NMP; EM; 3.09 A; E/F/G/H=1-108.
DR   PDB; 9NMQ; EM; 2.60 A; E/F/G/H=1-108.
DR   PDB; 9NMR; EM; 2.91 A; E/F/G/H=1-108.
DR   AlphaFoldDB; P26883; -.
DR   BMRB; P26883; -.
DR   EMDB; EMD-43283; -.
DR   EMDB; EMD-43284; -.
DR   EMDB; EMD-43299; -.
DR   EMDB; EMD-43304; -.
DR   EMDB; EMD-49534; -.
DR   EMDB; EMD-49535; -.
DR   EMDB; EMD-49536; -.
DR   EMDB; EMD-49537; -.
DR   EMDB; EMD-49538; -.
DR   SMR; P26883; -.
DR   BioGRID; 199682; 7.
DR   DIP; DIP-29707N; -.
DR   FunCoup; P26883; 2639.
DR   IntAct; P26883; 5.
DR   MINT; P26883; -.
DR   STRING; 10090.ENSMUSP00000037206; -.
DR   ChEMBL; CHEMBL4295736; -.
DR   DrugCentral; P26883; -.
DR   GlyGen; P26883; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P26883; -.
DR   PhosphoSitePlus; P26883; -.
DR   SwissPalm; P26883; -.
DR   jPOST; P26883; -.
DR   PaxDb; 10090-ENSMUSP00000037206; -.
DR   PeptideAtlas; P26883; -.
DR   ProteomicsDB; 271770; -.
DR   Pumba; P26883; -.
DR   DNASU; 14225; -.
DR   Ensembl; ENSMUST00000044011.12; ENSMUSP00000037206.6; ENSMUSG00000032966.15.
DR   GeneID; 14225; -.
DR   KEGG; mmu:14225; -.
DR   UCSC; uc008ndy.2; mouse.
DR   AGR; MGI:95541; -.
DR   CTD; 2280; -.
DR   MGI; MGI:95541; Fkbp1a.
DR   VEuPathDB; HostDB:ENSMUSG00000032966; -.
DR   eggNOG; KOG0544; Eukaryota.
DR   GeneTree; ENSGT00940000153311; -.
DR   HOGENOM; CLU_013615_12_1_1; -.
DR   InParanoid; P26883; -.
DR   OMA; FTSMNNQ; -.
DR   Reactome; R-MMU-166208; mTORC1-mediated signalling.
DR   Reactome; R-MMU-2025928; Calcineurin activates NFAT.
DR   Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
DR   BioGRID-ORCS; 14225; 13 hits in 80 CRISPR screens.
DR   PRO; PR:P26883; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P26883; protein.
DR   Bgee; ENSMUSG00000032966; Expressed in lateral septal nucleus and 275 other cell types or tissues.
DR   ExpressionAtlas; P26883; baseline and differential.
DR   GO; GO:0043679; C:axon terminus; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO:GO_Central.
DR   GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0030018; C:Z disc; ISO:GO_Central.
DR   GO; GO:0070697; F:activin receptor binding; ISO:GO_Central.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISO:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; ISO:GO_Central.
DR   GO; GO:0005528; F:FK506 binding; IDA:MGI.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISO:GO_Central.
DR   GO; GO:0070411; F:I-SMAD binding; ISO:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB.
DR   GO; GO:0030547; F:signaling receptor inhibitor activity; ISO:GO_Central.
DR   GO; GO:0005160; F:transforming growth factor beta receptor binding; ISO:GO_Central.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISO:GO_Central.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060347; P:heart trabecula formation; IMP:BHF-UCL.
DR   GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:0051209; P:release of sequestered calcium ion into cytosol; IDA:MGI.
DR   GO; GO:0031000; P:response to caffeine; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   FunFam; 3.10.50.40:FF:000024; Peptidyl-prolyl cis-trans isomerase FKBP1A; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR050689; FKBP-type_PPIase.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR10516:SF301; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP1A-RELATED; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PDBsum; 8VJJ; -.
DR   PDBsum; 8VJK; -.
DR   PDBsum; 8VK3; -.
DR   PDBsum; 8VK4; -.
DR   PDBsum; 9NMN; -.
DR   PDBsum; 9NMO; -.
DR   PDBsum; 9NMP; -.
DR   PDBsum; 9NMQ; -.
DR   PDBsum; 9NMR; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isomerase; Membrane;
KW   Reference proteome; Rotamase; Sarcoplasmic reticulum.
FT   CHAIN           1..108
FT                   /note="Peptidyl-prolyl cis-trans isomerase FKBP1A"
FT                   /id="PRO_0000075290"
FT   DOMAIN          20..108
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         53
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   STRAND          22..31
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   STRAND          47..50
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   TURN            51..54
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   HELIX           58..66
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   STRAND          72..77
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   TURN            79..86
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:8VJJ"
FT   STRAND          98..107
FT                   /evidence="ECO:0007829|PDB:8VJJ"
SQ   SEQUENCE   108 AA;  11923 MW;  8C265ED5803F6987 CRC64;
     MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW
     EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF DVELLKLE
//