FK173_ARATH
ID FK173_ARATH Reviewed; 234 AA.
AC Q8LB65; Q9C9U6;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic;
DE Short=PPIase FKBP17-3;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 17-3;
DE Short=AtFKBP17-3;
DE AltName: Full=Immunophilin FKBP17-3;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP17-3; OrderedLocusNames=At1g73655; ORFNames=F25P22.7;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012679; AAG52066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35493.1; -; Genomic_DNA.
DR EMBL; BT004233; AAO42248.1; -; mRNA.
DR EMBL; BT020474; AAW38975.1; -; mRNA.
DR EMBL; BT021144; AAX22279.1; -; mRNA.
DR EMBL; AY087399; AAM64948.1; -; mRNA.
DR PIR; E96763; E96763.
DR RefSeq; NP_565069.4; NM_106024.6.
DR AlphaFoldDB; Q8LB65; -.
DR SMR; Q8LB65; -.
DR STRING; 3702.AT1G73655.1; -.
DR PaxDb; Q8LB65; -.
DR PRIDE; Q8LB65; -.
DR ProteomicsDB; 230842; -.
DR EnsemblPlants; AT1G73655.1; AT1G73655.1; AT1G73655.
DR GeneID; 843700; -.
DR Gramene; AT1G73655.1; AT1G73655.1; AT1G73655.
DR KEGG; ath:AT1G73655; -.
DR Araport; AT1G73655; -.
DR TAIR; locus:505006221; AT1G73655.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_090476_0_0_1; -.
DR InParanoid; Q8LB65; -.
DR OMA; GICQGVE; -.
DR OrthoDB; 1514568at2759; -.
DR PhylomeDB; Q8LB65; -.
DR PRO; PR:Q8LB65; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LB65; baseline and differential.
DR Genevisible; Q8LB65; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IDA:TAIR.
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 2: Evidence at transcript level;
KW Chloroplast; Isomerase; Plastid; Reference proteome; Rotamase; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..28
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 29..?
FT /note="Thylakoid"
FT CHAIN ?..234
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP17-3,
FT chloroplastic"
FT /id="PRO_0000416133"
FT DOMAIN 130..228
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT CONFLICT 190
FT /note="R -> K (in Ref. 1; AAG52066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 25748 MW; 8D27DE07E019A26C CRC64;
MATLFTATVP SHHRFVSPSQ HPKQSLLSQS LSVTFTENPQ PTAVVTLQEQ QLTDWITSPV
TRRFGIGAGF TWAGFLAFGV VSEQMKKSRL DVFQEEDNTR GLEKQEEIIL PNGIRYYDLQ
VGSGATPSSG YLVVFDVKGQ VHGTEQVFVD TFGGKGKSLA MVMDSRPYSK GLCQGIEHVL
RSMKAGGKRR VIIPPSLGFG DRNVEFGQGL EIPPSATLDY IIEVDTVYCF QTIV
