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Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic (PPIase FKBP20-2) (EC 5.2.1.8) (FK506-binding protein 20-2) (AtFKBP20-2) (Immunophilin FKBP20-2) (Rotamase)

 FK202_ARATH             Reviewed;         242 AA.
Q0WRJ7; Q9M222;
01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
28-MAR-2018, entry version 82.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP20-2, chloroplastic {ECO:0000303|PubMed:15047905};
Short=PPIase FKBP20-2 {ECO:0000303|PubMed:15047905};
EC=5.2.1.8 {ECO:0000305};
AltName: Full=FK506-binding protein 20-2 {ECO:0000303|PubMed:15047905};
Short=AtFKBP20-2 {ECO:0000303|PubMed:15047905};
AltName: Full=Immunophilin FKBP20-2 {ECO:0000303|PubMed:15047905};
AltName: Full=Rotamase;
Flags: Precursor;
Name=FKBP20-2 {ECO:0000303|PubMed:15047905};
OrderedLocusNames=At3g60370 {ECO:0000312|Araport:AT3G60370};
ORFNames=T8B10.30 {ECO:0000312|EMBL:CAB81823.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 68-84, AND SUBCELLULAR LOCATION.
PubMed=11719511; DOI=10.1074/jbc.M108575200;
Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
Kieselbach T.;
"Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
J. Biol. Chem. 277:8354-8365(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11826309; DOI=10.1105/tpc.010304;
Peltier J.-B., Emanuelsson O., Kalume D.E., Ytterberg J., Friso G.,
Rudella A., Liberles D.A., Soederberg L., Roepstorff P.,
von Heijne G., van Wijk K.J.;
"Central functions of the lumenal and peripheral thylakoid proteome of
Arabidopsis determined by experimentation and genome-wide
prediction.";
Plant Cell 14:211-236(2002).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15047905; DOI=10.1104/pp.103.031005;
He Z., Li L., Luan S.;
"Immunophilins and parvulins. Superfamily of peptidyl prolyl
isomerases in Arabidopsis.";
Plant Physiol. 134:1248-1267(2004).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-227 AND CYS-241.
PubMed=16894144; DOI=10.1073/pnas.0605452103;
Lima A., Lima S., Wong J.H., Phillips R.S., Buchanan B.B., Luan S.;
"A redox-active FKBP-type immunophilin functions in accumulation of
the photosystem II supercomplex in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 103:12631-12636(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
SCALE ANALYSIS].
PubMed=18431481; DOI=10.1371/journal.pone.0001994;
Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
Sun Q., van Wijk K.J.;
"Sorting signals, N-terminal modifications and abundance of the
chloroplast proteome.";
PLoS ONE 3:E1994-E1994(2008).
[10]
INTERACTION WITH LTO1.
PubMed=25412899;
Lu Y., Du J.J., Yu Z.B., Peng J.J., Xu J.N., Wang X.Y.;
"Identification of potential targets for thylakoid oxidoreductase
AtVKOR/LTO1 in chloroplasts.";
Protein Pept. Lett. 22:219-225(2014).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides (By similarity). Involved in the accumulation of the
PSII complex. {ECO:0000250, ECO:0000269|PubMed:16894144}.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0). {ECO:0000305}.
-!- SUBUNIT: Interacts in vitro with LTO1.
{ECO:0000269|PubMed:25412899}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
{ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}.
-!- MISCELLANEOUS: PPIase activity is unaffected on reduction.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB81823.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL138646; CAB81823.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE80052.1; -; Genomic_DNA.
EMBL; BT029531; ABL66787.1; -; mRNA.
EMBL; AK228309; BAF00252.1; -; mRNA.
PIR; T47848; T47848.
RefSeq; NP_567098.2; NM_115901.4.
UniGene; At.34461; -.
ProteinModelPortal; Q0WRJ7; -.
SMR; Q0WRJ7; -.
BioGrid; 10522; 1.
IntAct; Q0WRJ7; 1.
STRING; 3702.AT3G60370.1; -.
iPTMnet; Q0WRJ7; -.
PaxDb; Q0WRJ7; -.
PRIDE; Q0WRJ7; -.
EnsemblPlants; AT3G60370.1; AT3G60370.1; AT3G60370.
GeneID; 825208; -.
Gramene; AT3G60370.1; AT3G60370.1; AT3G60370.
KEGG; ath:AT3G60370; -.
Araport; AT3G60370; -.
TAIR; locus:2103366; AT3G60370.
eggNOG; ENOG410IV9C; Eukaryota.
eggNOG; COG0545; LUCA.
HOGENOM; HOG000012423; -.
InParanoid; Q0WRJ7; -.
OMA; ASDNYIK; -.
OrthoDB; EOG09360LJ0; -.
PhylomeDB; Q0WRJ7; -.
PRO; PR:Q0WRJ7; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q0WRJ7; baseline and differential.
Genevisible; Q0WRJ7; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0031977; C:thylakoid lumen; IDA:TAIR.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0010207; P:photosystem II assembly; IMP:TAIR.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
1: Evidence at protein level;
Chloroplast; Complete proteome; Direct protein sequencing;
Disulfide bond; Isomerase; Plastid; Reference proteome; Rotamase;
Thylakoid; Transit peptide.
TRANSIT 1 31 Chloroplast. {ECO:0000255}.
TRANSIT 32 67 Thylakoid. {ECO:0000269|PubMed:11719511}.
CHAIN 68 242 Peptidyl-prolyl cis-trans isomerase
FKBP20-2, chloroplastic.
/FTId=PRO_0000342097.
DOMAIN 138 225 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
DISULFID 227 241
MUTAGEN 227 227 C->S: 50% reduction of activity; when
associated with S-241.
{ECO:0000269|PubMed:16894144}.
MUTAGEN 241 241 C->S: 50% reduction of activity; when
associated with S-227.
{ECO:0000269|PubMed:16894144}.
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


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