FKB53_ARATH
ID FKB53_ARATH Reviewed; 477 AA.
AC Q93ZG9; Q9STK2;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP53;
DE Short=PPIase FKBP53;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 53;
DE Short=AtFKBP53;
DE AltName: Full=Immunophilin FKBP53;
DE AltName: Full=Rotamase;
GN Name=FKBP53; OrderedLocusNames=At4g25340; ORFNames=T30C3_20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP H3.
RX PubMed=20142844; DOI=10.1038/cr.2010.22;
RA Li H., Luan S.;
RT "AtFKBP53 is a histone chaperone required for repression of ribosomal RNA
RT gene expression in Arabidopsis.";
RL Cell Res. 20:357-366(2010).
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). Histone chaperone possibly involved in
CC H3/H4 deposition to the nucleosome. Associates with 18S rDNA chromatin
CC and negatively regulates the level of its expression. {ECO:0000250,
CC ECO:0000269|PubMed:20142844}.
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: Interacts with histone H3. {ECO:0000269|PubMed:20142844}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20142844}.
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=Q93ZG9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Broadly expressed in leaves, flowers, stems and
CC roots. Detected in root apical meristem region and pollen.
CC {ECO:0000269|PubMed:20142844}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45512.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL079350; CAB45512.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85043.1; -; Genomic_DNA.
DR EMBL; AY057543; AAL09783.1; -; mRNA.
DR EMBL; AY143978; AAN28917.1; -; mRNA.
DR PIR; T10215; T10215.
DR RefSeq; NP_567717.1; NM_118666.3. [Q93ZG9-1]
DR PDB; 6J2M; X-ray; 1.13 A; A=360-477.
DR PDB; 6J2Z; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-100.
DR PDB; 7F2J; X-ray; 1.60 A; A/B=362-477.
DR PDBsum; 6J2M; -.
DR PDBsum; 6J2Z; -.
DR PDBsum; 7F2J; -.
DR AlphaFoldDB; Q93ZG9; -.
DR SMR; Q93ZG9; -.
DR BioGRID; 13924; 10.
DR STRING; 3702.AT4G25340.1; -.
DR iPTMnet; Q93ZG9; -.
DR SwissPalm; Q93ZG9; -.
DR PaxDb; Q93ZG9; -.
DR PRIDE; Q93ZG9; -.
DR ProteomicsDB; 230427; -. [Q93ZG9-1]
DR EnsemblPlants; AT4G25340.1; AT4G25340.1; AT4G25340. [Q93ZG9-1]
DR GeneID; 828637; -.
DR Gramene; AT4G25340.1; AT4G25340.1; AT4G25340. [Q93ZG9-1]
DR KEGG; ath:AT4G25340; -.
DR Araport; AT4G25340; -.
DR TAIR; locus:2138029; AT4G25340.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_022297_1_1_1; -.
DR InParanoid; Q93ZG9; -.
DR OrthoDB; 402681at2759; -.
DR PhylomeDB; Q93ZG9; -.
DR PRO; PR:Q93ZG9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93ZG9; baseline and differential.
DR Genevisible; Q93ZG9; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
DR GO; GO:0006334; P:nucleosome assembly; IDA:TAIR.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR041232; NPL.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR023566; PPIase_Fpr3/Fpr4-like.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF17800; NPL; 1.
DR PIRSF; PIRSF001473; FK506-bp_FPR3; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Isomerase; Nucleus;
KW Reference proteome; Rotamase.
FT CHAIN 1..477
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP53"
FT /id="PRO_0000416136"
FT DOMAIN 389..477
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 104..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6J2Z"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:6J2Z"
FT STRAND 372..377
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 390..400
FT /evidence="ECO:0007829|PDB:6J2M"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:6J2M"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6J2M"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6J2M"
FT TURN 451..455
FT /evidence="ECO:0007829|PDB:6J2M"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:6J2M"
FT STRAND 467..477
FT /evidence="ECO:0007829|PDB:6J2M"
SQ SEQUENCE 477 AA; 52223 MW; 10C405953B17675E CRC64;
MGFWGLEVKP GKPQAYNPKN EQGKIHVTQA TLGTGLSKEK SVIQCSIGDK APIALCSLLP
NKIECCPLNL EFDDDDEPVE FTVTGDRSIH LSGFLEYYQD DEDDYEHDED DSDGIDVGES
EEDDSCEYDS EEDEQLDEFE DFLDSNLERY RNAAAPKSGV IIEEIEDEEK PAKDNKAKQT
KKKSQASEGE NAKKQIVAIE GAHVPVLESE DEDEDGLPIP KGKSSEVENA SGEKMVVDND
EQGSNKKRKA KAAEQDDGQE SANKSKKKKN QKEKKKGENV LNEEAGQVQT GNVLKKQDIS
QISSNTKAQD GTANNAMSES SKTPDKSAEK KTKNKKKKKP SDEAAEISGT VEKQTPADSK
SSQVRTYPNG LIVEELSMGK PNGKRADPGK TVSVRYIGKL QKNGKIFDSN IGKSPFKFRL
GIGSVIKGWD VGVNGMRVGD KRKLTIPPSM GYGVKGAGGQ IPPNSWLTFD VELINVQ
