FKB1A_XENLA
ID FKB1A_XENLA Reviewed; 108 AA.
AC O42123; Q5D0D0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
DE Short=PPIase FKBP1A;
DE EC=5.2.1.8;
DE AltName: Full=12 kDa FK506-binding protein;
DE Short=12 kDa FKBP;
DE Short=FKBP-12;
DE AltName: Full=FK506-binding protein 1A;
DE Short=FKBP-1A;
DE AltName: Full=Immunophilin FKBP12;
DE AltName: Full=Rotamase;
GN Name=fkbp1a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9344875; DOI=10.1006/bbrc.1997.7491;
RA Nishinakmaura R., Matsumoto Y., Uochi T., Asashima M., Yokota T.;
RT "Xenopus FK 506-binding protein homolog induces a secondary axis in frog
RT embryos, which is inhibited by coexisting BMP 4 signaling.";
RL Biochem. Biophys. Res. Commun. 239:585-591(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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. May modulate the RYR1 calcium channel
CC activity. PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB006678; BAA23102.1; -; mRNA.
DR EMBL; BC041248; AAH41248.1; -; mRNA.
DR PIR; JC5764; JC5764.
DR RefSeq; NP_001079382.1; NM_001085913.1.
DR RefSeq; XP_018089486.1; XM_018233997.1.
DR AlphaFoldDB; O42123; -.
DR SMR; O42123; -.
DR DNASU; 379069; -.
DR GeneID; 379069; -.
DR KEGG; xla:379069; -.
DR CTD; 379069; -.
DR Xenbase; XB-GENE-5836974; fkbp1a.L.
DR OrthoDB; 1328688at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379069; Expressed in internal ear and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISA:AgBase.
DR GO; GO:0098562; C:cytoplasmic side of membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISA:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISA:AgBase.
DR GO; GO:0031312; C:extrinsic component of organelle membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISA:AgBase.
DR GO; GO:1990425; C:ryanodine receptor complex; ISS:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISA:AgBase.
DR GO; GO:0014802; C:terminal cisterna; IDA:AgBase.
DR GO; GO:0030018; C:Z disc; ISA:AgBase.
DR GO; GO:0048185; F:activin binding; ISA:AgBase.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISA:AgBase.
DR GO; GO:0005528; F:FK506 binding; ISA:AgBase.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISA:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; ISA:AgBase.
DR GO; GO:0046332; F:SMAD binding; ISA:AgBase.
DR GO; GO:0044325; F:transmembrane transporter binding; ISA:AgBase.
DR GO; GO:1990000; P:amyloid fibril formation; ISA:AgBase.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISA:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; ISA:AgBase.
DR GO; GO:0060347; P:heart trabecula formation; ISA:AgBase.
DR GO; GO:0006936; P:muscle contraction; ISA:AgBase.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISA:AgBase.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISA:AgBase.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISA:AgBase.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISA:AgBase.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISA:AgBase.
DR GO; GO:0032092; P:positive regulation of protein binding; ISA:AgBase.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISA:AgBase.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; ISA:AgBase.
DR GO; GO:0032925; P:regulation of activin receptor signaling pathway; ISA:AgBase.
DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISA:AgBase.
DR GO; GO:0050776; P:regulation of immune response; ISA:AgBase.
DR GO; GO:0032880; P:regulation of protein localization; ISA:AgBase.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:AgBase.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISA:AgBase.
DR GO; GO:0007183; P:SMAD protein complex assembly; ISA:AgBase.
DR GO; GO:0097435; P:supramolecular fiber organization; ISA:AgBase.
DR GO; GO:0042098; P:T cell proliferation; ISA:AgBase.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISA: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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..108
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP1A"
FT /id="PRO_0000075293"
FT DOMAIN 20..108
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 108 AA; 11912 MW; CFA335430638BC08 CRC64;
MGVQVETITE GDGRTFPKKG QTVVVHYVGS LENGKKFDSS RDRNKPFKFI IGRCEVIRGW
EEGVAQMSVG QRARLTCSPD FAYGATGHPG IIPPNATLTF DVELLRLE
