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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_XENLA             Reviewed;         108 AA.
O42123; Q5D0D0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 83.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
Short=PPIase FKBP1A;
EC=5.2.1.8;
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;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9344875; DOI=10.1006/bbrc.1997.7491;
Nishinakmaura R., Matsumoto Y., Uochi T., Asashima M., Yokota T.;
"Xenopus FK 506-binding protein homolog induces a secondary axis in
frog embryos, which is inhibited by coexisting BMP 4 signaling.";
Biochem. Biophys. Res. Commun. 239:585-591(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
-!- 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. 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.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
subfamily. {ECO:0000305}.
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EMBL; AB006678; BAA23102.1; -; mRNA.
EMBL; BC041248; AAH41248.1; -; mRNA.
PIR; JC5764; JC5764.
RefSeq; NP_001079382.1; NM_001085913.1.
RefSeq; XP_018089486.1; XM_018233997.1.
UniGene; Xl.960; -.
ProteinModelPortal; O42123; -.
SMR; O42123; -.
PRIDE; O42123; -.
GeneID; 379069; -.
KEGG; xla:379069; -.
CTD; 379069; -.
Xenbase; XB-GENE-5836974; fkbp1a.
HOVERGEN; HBG051623; -.
KO; K09568; -.
BRENDA; 5.2.1.8; 6725.
GO; GO:0005737; C:cytoplasm; ISA:AgBase.
GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISA:AgBase.
GO; GO:0070062; C:extracellular exosome; ISA:AgBase.
GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISA:AgBase.
GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISA:AgBase.
GO; GO:0014802; C:terminal cisterna; IDA:AgBase.
GO; GO:0030018; C:Z disc; ISA:AgBase.
GO; GO:0048185; F:activin binding; ISA:AgBase.
GO; GO:0019855; F:calcium channel inhibitor activity; ISA:AgBase.
GO; GO:0008144; F:drug binding; IDA:AgBase.
GO; GO:0005528; F:FK506 binding; ISA:AgBase.
GO; GO:0044325; F:ion channel binding; ISA:AgBase.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISA:AgBase.
GO; GO:0042803; F:protein homodimerization activity; ISA:AgBase.
GO; GO:0046332; F:SMAD binding; ISA:AgBase.
GO; GO:1990000; P:amyloid fibril formation; ISA:AgBase.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISA:AgBase.
GO; GO:0003007; P:heart morphogenesis; ISA:AgBase.
GO; GO:0060347; P:heart trabecula formation; ISA:AgBase.
GO; GO:0006936; P:muscle contraction; ISA:AgBase.
GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISA:AgBase.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISA:AgBase.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISA:AgBase.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISA:AgBase.
GO; GO:0032092; P:positive regulation of protein binding; ISA:AgBase.
GO; GO:0031398; P:positive regulation of protein ubiquitination; ISA:AgBase.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISA:AgBase.
GO; GO:0032925; P:regulation of activin receptor signaling pathway; ISA:AgBase.
GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISA:AgBase.
GO; GO:0050776; P:regulation of immune response; ISA:AgBase.
GO; GO:0032880; P:regulation of protein localization; ISA:AgBase.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:AgBase.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISA:AgBase.
GO; GO:0031000; P:response to caffeine; ISA:AgBase.
GO; GO:0007183; P:SMAD protein complex assembly; ISA:AgBase.
GO; GO:0097435; P:supramolecular fiber organization; ISA:AgBase.
GO; GO:0042098; P:T cell proliferation; ISA:AgBase.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISA:AgBase.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
3: Inferred from homology;
Cytoplasm; Isomerase; Rotamase.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 108 Peptidyl-prolyl cis-trans isomerase
FKBP1A.
/FTId=PRO_0000075293.
DOMAIN 20 108 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
SEQUENCE 108 AA; 11912 MW; CFA335430638BC08 CRC64;
MGVQVETITE GDGRTFPKKG QTVVVHYVGS LENGKKFDSS RDRNKPFKFI IGRCEVIRGW
EEGVAQMSVG QRARLTCSPD FAYGATGHPG IIPPNATLTF DVELLRLE


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