FKB65_ARATH
ID FKB65_ARATH Reviewed; 578 AA.
AC Q9FJL3; B9DGC2; Q0WSA8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP65;
DE Short=PPIase FKBP65;
DE EC=5.2.1.8;
DE AltName: Full=70 kDa peptidyl-prolyl isomerase;
DE AltName: Full=FK506-binding protein 65;
DE Short=AtFKBP65;
DE AltName: Full=Immunophilin FKBP65;
DE AltName: Full=Peptidyl-prolyl isomerase ROF2;
DE AltName: Full=Protein ROTAMASE FKBP 2;
DE AltName: Full=Rotamase;
GN Name=FKBP65; Synonyms=ROF2; OrderedLocusNames=At5g48570;
GN ORFNames=K15N18.12;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-453.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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).
RN [6]
RP INDUCTION BY HEAT, AND TISSUE SPECIFICITY.
RX PubMed=17080288; DOI=10.1007/s11103-006-9085-z;
RA Aviezer-Hagai K., Skovorodnikova J., Galigniana M., Farchi-Pisanty O.,
RA Maayan E., Bocovza S., Efrat Y., von Koskull-Doring P., Ohad N.,
RA Breiman A.;
RT "Arabidopsis immunophilins ROF1 (AtFKBP62) and ROF2 (AtFKBP65) exhibit
RT tissue specificity, are heat-stress induced, and bind HSP90.";
RL Plant Mol. Biol. 63:237-255(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH FKBP62.
RX PubMed=19876748; DOI=10.1007/s11103-009-9561-3;
RA Meiri D., Tazat K., Cohen-Peer R., Farchi-Pisanty O., Aviezer-Hagai K.,
RA Avni A., Breiman A.;
RT "Involvement of Arabidopsis ROF2 (FKBP65) in thermotolerance.";
RL Plant Mol. Biol. 72:191-203(2010).
RN [8]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22268595; DOI=10.1111/j.1365-313x.2012.04921.x;
RA Bissoli G., Ninoles R., Fresquet S., Palombieri S., Bueso E., Rubio L.,
RA Garcia-Sanchez M.J., Fernandez J.A., Mulet J.M., Serrano R.;
RT "Peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH
RT homeostasis in Arabidopsis.";
RL Plant J. 70:704-716(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PATHOGEN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24440291; DOI=10.1016/j.gene.2014.01.029;
RA Pogorelko G.V., Mokryakova M., Fursova O.V., Abdeeva I., Piruzian E.S.,
RA Bruskin S.A.;
RT "Characterization of three Arabidopsis thaliana immunophilin genes involved
RT in the plant defense response against Pseudomonas syringae.";
RL Gene 538:12-22(2014).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Co-chaperone that negatively modulates thermotolerance
CC by interacting with FKBP62 and decreasing the HSFA2-mediated
CC accumulation of chaperones of the small-HSPs family. Plays a positive
CC role in tolerance to intracellular acid stress by maintaining the pH
CC homeostasis. May be a part of transcription regulation pathways upon
CC pathogen infection. {ECO:0000269|PubMed:19876748,
CC ECO:0000269|PubMed:22268595, ECO:0000269|PubMed:24440291}.
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 -!- SUBUNIT: This PPIase probably binds calmodulin (By similarity). Forms
CC heterodimers with FKBP62/ROF1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9FJL3; Q38931: FKBP62; NbExp=3; IntAct=EBI-2620253, EBI-2409351;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19876748}. Nucleus
CC {ECO:0000269|PubMed:19876748, ECO:0000269|PubMed:24440291}.
CC Note=Relocalization from the cytoplasm into the nucleus is induced by
CC heat shock. {ECO:0000269|PubMed:19876748}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC {ECO:0000269|PubMed:17080288}.
CC -!- INDUCTION: By heat shock and by intracellular acid stress. Up-regulated
CC by HSFA2 and upon pathogen infection. {ECO:0000269|PubMed:17080288,
CC ECO:0000269|PubMed:19876748, ECO:0000269|PubMed:22268595,
CC ECO:0000269|PubMed:24440291}.
CC -!- DISRUPTION PHENOTYPE: Acid sensitivity and increased susceptibility to
CC P.syringae infection. {ECO:0000269|PubMed:22268595,
CC ECO:0000269|PubMed:24440291}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AB015468; BAB10690.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95689.1; -; Genomic_DNA.
DR EMBL; AK228029; BAE99990.1; -; mRNA.
DR EMBL; AK317098; BAH19789.1; -; mRNA.
DR RefSeq; NP_199668.1; NM_124233.3.
DR AlphaFoldDB; Q9FJL3; -.
DR SMR; Q9FJL3; -.
DR BioGRID; 20159; 6.
DR IntAct; Q9FJL3; 2.
DR MINT; Q9FJL3; -.
DR STRING; 3702.AT5G48570.1; -.
DR iPTMnet; Q9FJL3; -.
DR PaxDb; Q9FJL3; -.
DR PRIDE; Q9FJL3; -.
DR ProteomicsDB; 230623; -.
DR EnsemblPlants; AT5G48570.1; AT5G48570.1; AT5G48570.
DR GeneID; 834913; -.
DR Gramene; AT5G48570.1; AT5G48570.1; AT5G48570.
DR KEGG; ath:AT5G48570; -.
DR Araport; AT5G48570; -.
DR TAIR; locus:2152561; AT5G48570.
DR eggNOG; KOG0543; Eukaryota.
DR HOGENOM; CLU_013615_13_4_1; -.
DR InParanoid; Q9FJL3; -.
DR OMA; YIEYDST; -.
DR OrthoDB; 897391at2759; -.
DR PhylomeDB; Q9FJL3; -.
DR BRENDA; 5.2.1.8; 399.
DR PRO; PR:Q9FJL3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJL3; baseline and differential.
DR Genevisible; Q9FJL3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.10.50.40; -; 3.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 3.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 3.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Chaperone; Cytoplasm; Isomerase; Nucleus;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..578
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP65"
FT /id="PRO_0000416137"
FT DOMAIN 65..153
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 181..271
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 299..393
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 410..443
FT /note="TPR 1"
FT REPEAT 459..492
FT /note="TPR 2"
FT REPEAT 493..526
FT /note="TPR 3"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..555
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q38931"
FT CONFLICT 205
FT /note="E -> G (in Ref. 3; BAE99990)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65223 MW; 0C56F57D22E37A3B CRC64;
MEDDFDTQNQ FPEEEPEEMD MDLPDNDEAD SAPYLKIGEE MEIGKSGLKK KLVKECEKWD
TPENGDEVEV HYTGTLLDGT KFDSSRDRGT PFKFTLGQGH VIKGWDLGIK TMKKGENAIF
TIPPELAYGE TGSPPTIPPN ATLQFDVELI AWRSVKDICG DGGVSKKIIV EGEKWEKPKD
LDEVYVKYEA RLEDGTIVGK SDGVEFTVKE GHFCPALSKA VKTMKRGEKV LLTVKPQYGF
GEFGRPASDG LQAAIPPNAT LQIDLELVSW KTVVEVTDDR KVIKKILKEG EGYERPNEGA
IVKLKLIGKL QDGTTVFVKK GHEEDEEPFE FKIDEEQVIE GLEKAVMGMK KGEVALITIS
PEYAFGSSES KQELAVIPPN STVYYEVELV SFIKEKESWD MNTQERIEAA GKKKEEGNVL
FKAGKYARAS KRYERGVKYI EYDSTFDEEE KKKSKDLKIA CNLNDAACKL KLKDYKEAAK
LSTKVLEMDS RNVKAMYRRA HAYLETADLD LAELDIKKAL EIDPDNKEVK IEYKKLKEKV
KEYNKKDAKF YSNMLSKMLE PHKGTQKEAQ AMSIDTKA
