FK163_ARATH
ID FK163_ARATH Reviewed; 223 AA.
AC O22870; Q940C0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP16-3, chloroplastic;
DE Short=PPIase FKBP16-3;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 16-3;
DE Short=AtFKBP16-3;
DE AltName: Full=Immunophilin FKBP16-3;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP16-3; Synonyms=FKBP17; OrderedLocusNames=At2g43560;
GN ORFNames=T1O24.30;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 PROTEIN SEQUENCE OF 77-96, 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 [5]
RP SUBCELLULAR LOCATION, AND 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 [6]
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).
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). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:11826309}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AC002335; AAB64339.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10290.1; -; Genomic_DNA.
DR EMBL; AY056125; AAL07204.1; -; mRNA.
DR EMBL; AY113988; AAM45036.1; -; mRNA.
DR PIR; F84867; F84867.
DR RefSeq; NP_181884.1; NM_129918.3.
DR AlphaFoldDB; O22870; -.
DR SMR; O22870; -.
DR BioGRID; 4294; 1.
DR IntAct; O22870; 1.
DR STRING; 3702.AT2G43560.1; -.
DR iPTMnet; O22870; -.
DR MetOSite; O22870; -.
DR PaxDb; O22870; -.
DR PRIDE; O22870; -.
DR EnsemblPlants; AT2G43560.1; AT2G43560.1; AT2G43560.
DR GeneID; 818958; -.
DR Gramene; AT2G43560.1; AT2G43560.1; AT2G43560.
DR KEGG; ath:AT2G43560; -.
DR Araport; AT2G43560; -.
DR TAIR; locus:2058218; AT2G43560.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_092197_0_1_1; -.
DR InParanoid; O22870; -.
DR OrthoDB; 1498711at2759; -.
DR PhylomeDB; O22870; -.
DR PRO; PR:O22870; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22870; baseline and differential.
DR Genevisible; O22870; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Isomerase; Plastid;
KW Reference proteome; Rotamase; Thylakoid; Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 37..76
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 77..223
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP16-3,
FT chloroplastic"
FT /id="PRO_0000025525"
FT DOMAIN 124..216
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 223 AA; 23564 MW; BE3A48D0C1A59C38 CRC64;
MAASSPSLLL PLGSASRNGL TTKNPNSSRY IAARVIASET REQSCKISNL SSRREAMLLV
LGVSGGLSMS SLAAYAAGLP PEDKPRLCEA ECEKELENVP MVTTESGLQY KDIKVGRGPS
PPVGFQVAAN YVAMVPSGQI FDSSLEKGLP YLFRVGSGQV IKGLDEGILS MKAGGKRRLY
IPGPLAFPKG LVSAPGRPRV APNSPVIFDV SLEFIPGLDS EEE
