FK202_ARATH
ID FK202_ARATH Reviewed; 242 AA.
AC Q0WRJ7; Q9M222;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic {ECO:0000303|PubMed:15047905};
DE Short=PPIase FKBP20-2 {ECO:0000303|PubMed:15047905};
DE EC=5.2.1.8 {ECO:0000305};
DE AltName: Full=FK506-binding protein 20-2 {ECO:0000303|PubMed:15047905};
DE Short=AtFKBP20-2 {ECO:0000303|PubMed:15047905};
DE AltName: Full=Immunophilin FKBP20-2 {ECO:0000303|PubMed:15047905};
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP20-2 {ECO:0000303|PubMed:15047905};
GN OrderedLocusNames=At3g60370 {ECO:0000312|Araport:AT3G60370};
GN ORFNames=T8B10.30 {ECO:0000312|EMBL:CAB81823.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 68-84, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11826309; DOI=10.1105/tpc.010304;
RA Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
RA Rudella A., Liberles D.A., Soederberg L., Roepstorff P., von Heijne G.,
RA van Wijk K.J.;
RT "Central functions of the lumenal and peripheral thylakoid proteome of
RT Arabidopsis determined by experimentation and genome-wide prediction.";
RL Plant Cell 14:211-236(2002).
RN [7]
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 [8]
RP FUNCTION, AND MUTAGENESIS OF CYS-227 AND CYS-241.
RX PubMed=16894144; DOI=10.1073/pnas.0605452103;
RA Lima A., Lima S., Wong J.H., Phillips R.S., Buchanan B.B., Luan S.;
RT "A redox-active FKBP-type immunophilin functions in accumulation of the
RT photosystem II supercomplex in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:12631-12636(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [10]
RP INTERACTION WITH LTO1.
RX PubMed=25412899; DOI=10.2174/0929866521666141121153138;
RA Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
RT "Identification of potential targets for thylakoid oxidoreductase
RT AtVKOR/LTO1 in chloroplasts.";
RL Protein Pept. Lett. 22:219-225(2014).
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). Involved in the accumulation of the PSII
CC complex. {ECO:0000250, ECO:0000269|PubMed:16894144}.
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts in vitro with LTO1. {ECO:0000269|PubMed:25412899}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}.
CC -!- MISCELLANEOUS: PPIase activity is unaffected on reduction.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138646; CAB81823.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80052.1; -; Genomic_DNA.
DR EMBL; BT029531; ABL66787.1; -; mRNA.
DR EMBL; AK228309; BAF00252.1; -; mRNA.
DR PIR; T47848; T47848.
DR RefSeq; NP_567098.2; NM_115901.4.
DR AlphaFoldDB; Q0WRJ7; -.
DR SMR; Q0WRJ7; -.
DR BioGRID; 10522; 1.
DR IntAct; Q0WRJ7; 1.
DR STRING; 3702.AT3G60370.1; -.
DR iPTMnet; Q0WRJ7; -.
DR PaxDb; Q0WRJ7; -.
DR PRIDE; Q0WRJ7; -.
DR ProteomicsDB; 230513; -.
DR EnsemblPlants; AT3G60370.1; AT3G60370.1; AT3G60370.
DR GeneID; 825208; -.
DR Gramene; AT3G60370.1; AT3G60370.1; AT3G60370.
DR KEGG; ath:AT3G60370; -.
DR Araport; AT3G60370; -.
DR TAIR; locus:2103366; AT3G60370.
DR eggNOG; ENOG502QVUR; Eukaryota.
DR HOGENOM; CLU_083172_0_1_1; -.
DR InParanoid; Q0WRJ7; -.
DR PhylomeDB; Q0WRJ7; -.
DR PRO; PR:Q0WRJ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WRJ7; baseline and differential.
DR Genevisible; Q0WRJ7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044239; FKBP20-2-like.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR47414; PTHR47414; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Disulfide bond; Isomerase; Plastid;
KW Reference proteome; Rotamase; Thylakoid; Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 32..67
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 68..242
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP20-2,
FT chloroplastic"
FT /id="PRO_0000342097"
FT DOMAIN 138..225
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT DISULFID 227..241
FT MUTAGEN 227
FT /note="C->S: 50% reduction of activity; when associated
FT with S-241."
FT /evidence="ECO:0000269|PubMed:16894144"
FT MUTAGEN 241
FT /note="C->S: 50% reduction of activity; when associated
FT with S-227."
FT /evidence="ECO:0000269|PubMed:16894144"
SQ SEQUENCE 242 AA; 27192 MW; A288DC4D46C481D9 CRC64;
MVTILSTPLS PRLTFLCETK LSLSRSNRSV CCSLSEEPKD QCLSRRSLVY VLVASPCLLL
PALSSSAKTK SKSPYDERRL LEQNKRIQRE NNAPDEFPNF VREGFEVKVL ASDNYIKADS
GLIYRDFNVG QGDFPKDGQQ VTFHYIGYNE SGRRIDSTYI QGSPARIRMG TNALVPGFEM
GIRDMKPGGR RRIIIPPELG PPVGPSTFFS SKQFEVFDVE LLSIQNCERR TIIGFYSDVT
CS
