FK153_ARATH
ID FK153_ARATH Reviewed; 143 AA.
AC Q9FLB3; Q9SCY1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP15-3;
DE Short=PPIase FKBP15-3;
DE EC=5.2.1.8;
DE AltName: Full=15 kDa FK506-binding protein;
DE Short=15 kDa FKBP;
DE AltName: Full=FK506-binding protein 15-3;
DE Short=AtFKBP15-3;
DE AltName: Full=Immunophilin FKBP15-3;
DE AltName: Full=Rotamase;
GN Name=FKBP15-3; OrderedLocusNames=At5g05420; ORFNames=K18I23.23;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-138.
RA Kolukisaoglu U., Billion K., Eckhoff A., Moeller A., Saal B., Wanke D.,
RA Schulz B.;
RT "Structure and evolution of FKBP-like genes in Arabidopsis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15047905; DOI=10.1104/pp.103.031005;
RA He Z., Li L., Luan S.;
RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC 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 -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AB010692; BAB09985.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90872.1; -; Genomic_DNA.
DR EMBL; DQ487720; ABF59282.1; -; mRNA.
DR EMBL; AJ242484; CAB64724.1; -; mRNA.
DR RefSeq; NP_196161.1; NM_120624.1.
DR AlphaFoldDB; Q9FLB3; -.
DR SMR; Q9FLB3; -.
DR BioGRID; 15704; 9.
DR STRING; 3702.AT5G05420.1; -.
DR PaxDb; Q9FLB3; -.
DR PRIDE; Q9FLB3; -.
DR EnsemblPlants; AT5G05420.1; AT5G05420.1; AT5G05420.
DR GeneID; 830425; -.
DR Gramene; AT5G05420.1; AT5G05420.1; AT5G05420.
DR KEGG; ath:AT5G05420; -.
DR Araport; AT5G05420; -.
DR TAIR; locus:2153519; AT5G05420.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_013615_12_0_1; -.
DR InParanoid; Q9FLB3; -.
DR OMA; GQTFPKT; -.
DR OrthoDB; 936280at2759; -.
DR PhylomeDB; Q9FLB3; -.
DR PRO; PR:Q9FLB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLB3; baseline and differential.
DR Genevisible; Q9FLB3; AT.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..143
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP15-3"
FT /id="PRO_0000416129"
FT DOMAIN 56..143
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 143 AA; 15339 MW; 4E64D32BF43493B5 CRC64;
MSPSESAKKN EKISEEATVE SKAFSISVEK QTPDLDGLIV EELCMGNPNG KKAEPGKRVS
VHYTGKLQGN GKIFDSTVGK SRYKFRLDAG KVIKGLDVGL NGMLVGGKRK LTIPPEMGYG
AEGAGSIPPD SWLVFDVELL NVK
