FKB62_ARATH
ID FKB62_ARATH Reviewed; 551 AA.
AC Q38931; Q38949; Q9LSF3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP62;
DE Short=PPIase FKBP62;
DE EC=5.2.1.8;
DE AltName: Full=70 kDa peptidyl-prolyl isomerase;
DE AltName: Full=FK506-binding protein 62;
DE Short=AtFKBP62;
DE AltName: Full=Immunophilin FKBP62;
DE AltName: Full=Peptidylprolyl isomerase ROF1;
DE AltName: Full=Protein ROTAMASE FKBP 1;
DE AltName: Full=Rotamase;
GN Name=FKBP62; Synonyms=ROF1; OrderedLocusNames=At3g25230; ORFNames=MJL12.19;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING AND SODIUM CHLORIDE.
RX PubMed=8914512; DOI=10.1007/bf02172397;
RA Vucich V.A., Gasser C.S.;
RT "Novel structure of a high molecular weight FK506 binding protein from
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 252:510-517(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP POSSIBLE INTERACTION WITH CALMODULIN.
RX PubMed=11782485; DOI=10.1074/jbc.m111626200;
RA Reddy V.S., Ali G.S., Reddy A.S.N.;
RT "Genes encoding calmodulin-binding proteins in the Arabidopsis genome.";
RL J. Biol. Chem. 277:9840-9852(2002).
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 FUNCTION, INDUCTION BY HEAT, TISSUE SPECIFICITY, INTERACTION WITH HSP90,
RP AND MUTAGENESIS OF LYS-484.
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, AND INTERACTION WITH HSP90-1.
RX PubMed=19366428; DOI=10.1111/j.1365-313x.2009.03878.x;
RA Meiri D., Breiman A.;
RT "Arabidopsis ROF1 (FKBP62) modulates thermotolerance by interacting with
RT HSP90.1 and affecting the accumulation of HsfA2-regulated sHSPs.";
RL Plant J. 59:387-399(2009).
RN [8]
RP INTERACTION WITH FKBP65.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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). Co-chaperone that positively modulates
CC thermotolerance by interacting with HSP90.1 and increasing the HSFA2-
CC mediated accumulation of chaperones of the small-HSPs family.
CC {ECO:0000250, ECO:0000269|PubMed:17080288,
CC ECO:0000269|PubMed:19366428}.
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. Interacts with HSP90-1.
CC Forms heterodimers with FKBP65/ROF2. {ECO:0000269|PubMed:17080288,
CC ECO:0000269|PubMed:19366428, ECO:0000269|PubMed:19876748}.
CC -!- INTERACTION:
CC Q38931; Q9FJL3: FKBP65; NbExp=3; IntAct=EBI-2409351, EBI-2620253;
CC Q38931; P27323: HSP90-1; NbExp=4; IntAct=EBI-2409351, EBI-1778266;
CC Q38931; D6RUV9: AGO1; Xeno; NbExp=2; IntAct=EBI-2409351, EBI-7498167;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19366428}. Nucleus
CC {ECO:0000269|PubMed:19366428}. Note=Relocalization from the cytoplasm
CC into the nucleus is induced by heat shock and in association with
CC HSFA2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q38931-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, leaves and
CC flowers. Detected in the vascular elements of roots, in hydathodes and
CC trichomes of leaves and in stigma, sepals, and anthers.
CC {ECO:0000269|PubMed:17080288, ECO:0000269|PubMed:8914512}.
CC -!- INDUCTION: By wounding, NaCl and by heat shock.
CC {ECO:0000269|PubMed:17080288, ECO:0000269|PubMed:8914512}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02082.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U49453; AAB82061.1; -; mRNA.
DR EMBL; U57838; AAB82062.1; -; Genomic_DNA.
DR EMBL; AB026647; BAB02082.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76996.1; -; Genomic_DNA.
DR PIR; S72485; S72485.
DR RefSeq; NP_189160.3; NM_113429.5. [Q38931-1]
DR AlphaFoldDB; Q38931; -.
DR SMR; Q38931; -.
DR BioGRID; 7448; 7.
DR IntAct; Q38931; 4.
DR MINT; Q38931; -.
DR STRING; 3702.AT3G25230.2; -.
DR iPTMnet; Q38931; -.
DR PaxDb; Q38931; -.
DR PRIDE; Q38931; -.
DR EnsemblPlants; AT3G25230.1; AT3G25230.1; AT3G25230. [Q38931-1]
DR GeneID; 822117; -.
DR Gramene; AT3G25230.1; AT3G25230.1; AT3G25230. [Q38931-1]
DR KEGG; ath:AT3G25230; -.
DR Araport; AT3G25230; -.
DR eggNOG; KOG0543; Eukaryota.
DR HOGENOM; CLU_013615_13_4_1; -.
DR InParanoid; Q38931; -.
DR OMA; ELEMLGW; -.
DR PhylomeDB; Q38931; -.
DR PRO; PR:Q38931; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38931; baseline and differential.
DR Genevisible; Q38931; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00254; FKBP_C; 3.
DR Pfam; PF00515; TPR_1; 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; Alternative splicing; Calmodulin-binding; Chaperone;
KW Cytoplasm; Isomerase; Nucleus; Reference proteome; Repeat; Rotamase;
KW TPR repeat.
FT CHAIN 1..551
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP62"
FT /id="PRO_0000075333"
FT DOMAIN 57..145
FT /note="PPIase FKBP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 173..262
FT /note="PPIase FKBP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DOMAIN 290..383
FT /note="PPIase FKBP-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REPEAT 400..433
FT /note="TPR 1"
FT REPEAT 449..482
FT /note="TPR 2"
FT REPEAT 483..516
FT /note="TPR 3"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..545
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 484
FT /note="K->A: Reduces interaction with HSP90."
FT /evidence="ECO:0000269|PubMed:17080288"
FT CONFLICT 430
FT /note="I -> V (in Ref. 1; AAB82061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 61453 MW; 36CF13637466D286 CRC64;
MDANFEMPPV GGMNDDDDMD FGDGASFLKV GEEKEIQQGL KKKLLKEGEG YETPENGDEV
EVHYTGTLLD GTKFDSSRDR ATPFKFTLGQ GQVIKGWDIG IKTMKKGENA VFTIPAELAY
GESGSPPTIP ANATLQFDVE LLKWDSVKDI CKDGGVFKKI LAVGEKWENP KDLDEVLVKF
EAKLEDGTVV GKSDGVEFTV KDGHFCPALT KAVKTMKKGE KVLLTVKPQY GFGEKGKPAS
AGEGAVPPNA TLEINLELVS WKTVSEVTDD NKVVKKVLKE GDGYERPNEG AVVKVKLIGK
LQDGTVFLKK GHGENEEPFE FKTDEEQVVD GLDRAVMKMK KGEVALVTID PEYAFGSNES
QQELAVVPPN STVTYEVDLL TFDKERESWD MNTEEKIEAA SKKKEEGNSK FKGGKYSLAS
KRYEKAVKFI EYDTSFSEEE KKQAKALKVA CNLNDAACKL KLKDYKQAEK LCTKVLELES
TNVKALYRRA QAYMELSDLD LAEFDVKKAL EIDPNNREVK LEQKRLKEKM KEFNKKEAKF
YGNMFAKLSK E
