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Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase)

 FKB1A_RAT               Reviewed;         108 AA.
Q62658; A0JN04; P97533;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 143.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
Short=PPIase FKBP1A;
EC=5.2.1.8 {ECO:0000250|UniProtKB:P62942};
AltName: Full=12 kDa FK506-binding protein;
Short=12 kDa FKBP;
Short=FKBP-12;
AltName: Full=FK506-binding protein 1A;
Short=FKBP-1A;
AltName: Full=Immunophilin FKBP12;
AltName: Full=Rotamase;
Name=Fkbp1a; Synonyms=Fkbp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=7518616; DOI=10.1126/science.7518616;
Wang T., Donahoe P.K., Zervos A.S.;
"Specific interaction of type I receptors of the TGF-beta family with
the immunophilin FKBP-12.";
Science 265:674-676(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aortic smooth muscle;
Marx S.O., Jayaraman T., Mehran R., Go L.O., Wiederrecht G.J.,
Marks A.R.;
"Identification of a novel FK506-binding protein in rat aortic smooth
muscle cells.";
Circulation 92:297-297(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Pancreatic islet;
PubMed=9013543; DOI=10.1074/jbc.272.6.3133;
Noguchi N., Takasawa S., Nata K., Tohgo A., Kato I., Ikehata F.,
Yonekura H., Okamoto H.;
"Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+
from islet microsomes.";
J. Biol. Chem. 272:3133-3136(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH RYR2, AND TISSUE SPECIFICITY.
PubMed=20431056; DOI=10.1161/CIRCRESAHA.110.219816;
Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E.,
Fruen B.R., Bers D.M.;
"Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized
cardiac myocytes and effects on Ca sparks.";
Circ. Res. 106:1743-1752(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta
type I serine/threonine kinase receptor, preventing TGF-beta
receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B
which prevents the association of SMAD2 and SMAD3 with the activin
receptor complex, thereby blocking the activin signal. May
modulate the RYR1 calcium channel activity. PPIases accelerate the
folding of proteins. It catalyzes the cis-trans isomerization of
proline imidic peptide bonds in oligopeptides (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000250|UniProtKB:P62942}.
-!- ACTIVITY REGULATION: Inhibited by both FK506 and rapamycin.
-!- SUBUNIT: Interacts with TGFBR1; prevents TGFBR1 phosphorylation by
TGFBR2 and stabilizes it in the inactive conformation (By
similarity). Interacts with ACVR1B and SMAD7. Identified in a
complex composed of RYR1, PDE4D, PKA, FKBP1A and protein
phosphatase 1 (PP1) (By similarity). Interacts directly with RYR2
(PubMed:20431056). Interacts directly with RYR3 (By similarity).
Interacts directly with RYR1 (By similarity).
{ECO:0000250|UniProtKB:P26883, ECO:0000250|UniProtKB:P62942,
ECO:0000250|UniProtKB:P62943, ECO:0000269|PubMed:20431056}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P62943}; Cytoplasmic side
{ECO:0000250|UniProtKB:P62943}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:20431056}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U09386; AAA19163.1; -; mRNA.
EMBL; U69485; AAB48933.1; -; mRNA.
EMBL; D86641; BAA13153.1; -; mRNA.
EMBL; BC070519; AAH70519.3; -; mRNA.
EMBL; BC126071; AAI26072.1; -; mRNA.
RefSeq; NP_037234.2; NM_013102.3.
UniGene; Rn.80611; -.
ProteinModelPortal; Q62658; -.
SMR; Q62658; -.
BioGrid; 247668; 1.
CORUM; Q62658; -.
IntAct; Q62658; 1.
MINT; Q62658; -.
STRING; 10116.ENSRNOP00000012608; -.
ChEMBL; CHEMBL2095; -.
GuidetoPHARMACOLOGY; 2609; -.
iPTMnet; Q62658; -.
PhosphoSitePlus; Q62658; -.
PaxDb; Q62658; -.
PRIDE; Q62658; -.
Ensembl; ENSRNOT00000012608; ENSRNOP00000012608; ENSRNOG00000008822.
GeneID; 25639; -.
KEGG; rno:25639; -.
UCSC; RGD:2617; rat.
CTD; 2280; -.
RGD; 2617; Fkbp1a.
eggNOG; KOG0544; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOGENOM; HOG000154887; -.
HOVERGEN; HBG051623; -.
InParanoid; Q62658; -.
KO; K09568; -.
OMA; RVIAGWD; -.
OrthoDB; EOG091G02W1; -.
PhylomeDB; Q62658; -.
Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
PRO; PR:Q62658; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000008822; Expressed in 9 organ(s), highest expression level in Ammon's horn.
Genevisible; Q62658; RN.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0048185; F:activin binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0005528; F:FK506 binding; IDA:RGD.
GO; GO:0030544; F:Hsp70 protein binding; IPI:RGD.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0060347; P:heart trabecula formation; IEA:Ensembl.
GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; IEA:Ensembl.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IEA:Ensembl.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEP:RGD.
GO; GO:0007183; P:SMAD protein complex assembly; IEA:Ensembl.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Isomerase; Membrane;
Phosphoprotein; Reference proteome; Rotamase; Sarcoplasmic reticulum.
CHAIN 1 108 Peptidyl-prolyl cis-trans isomerase
FKBP1A.
/FTId=PRO_0000075292.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 53 53 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
MOD_RES 53 53 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P26883}.
CONFLICT 89 89 P -> T (in Ref. 3; BAA13153).
{ECO:0000305}.
SEQUENCE 108 AA; 11923 MW; 1C195C2A52C17666 CRC64;
MGVQVETISS GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW
EEGVAQMSVG QRAKLIISPD YAYGATGHPG IIPPHATLVF DVELLKLE


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