FK171_ARATH
ID FK171_ARATH Reviewed; 229 AA.
AC O81864; Q8GY75;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic;
DE Short=PPIase FKBP17-1;
DE EC=5.2.1.8;
DE AltName: Full=FK506-binding protein 17-1;
DE Short=AtFKBP17-1;
DE AltName: Full=Immunophilin FKBP17-1;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=FKBP17-1; Synonyms=FKBP24-1, FKBP25I; OrderedLocusNames=At4g19830;
GN ORFNames=T16H5.190;
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 [MRNA].
RA Kolukisaoglu U., Billion K., Eckhoff A., Moeller A., Saal B., Wanke D.,
RA Schulz B.;
RT "Structure and evolution of FKBP-like genes in Arabidopsis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-229.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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=BAC42456.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ242482; CAB64722.1; -; mRNA.
DR EMBL; AL024486; CAA19700.1; -; Genomic_DNA.
DR EMBL; AL161551; CAB78985.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84231.1; -; Genomic_DNA.
DR EMBL; BT024613; ABD43011.1; -; mRNA.
DR EMBL; AK117814; BAC42456.1; ALT_INIT; mRNA.
DR PIR; T04764; T04764.
DR RefSeq; NP_193718.1; NM_118103.4.
DR AlphaFoldDB; O81864; -.
DR SMR; O81864; -.
DR STRING; 3702.AT4G19830.1; -.
DR PaxDb; O81864; -.
DR PRIDE; O81864; -.
DR ProteomicsDB; 230105; -.
DR EnsemblPlants; AT4G19830.1; AT4G19830.1; AT4G19830.
DR GeneID; 827727; -.
DR Gramene; AT4G19830.1; AT4G19830.1; AT4G19830.
DR KEGG; ath:AT4G19830; -.
DR Araport; AT4G19830; -.
DR TAIR; locus:2134035; AT4G19830.
DR eggNOG; KOG0552; Eukaryota.
DR HOGENOM; CLU_089785_3_0_1; -.
DR InParanoid; O81864; -.
DR OMA; PSPPIIY; -.
DR OrthoDB; 1601308at2759; -.
DR PhylomeDB; O81864; -.
DR PRO; PR:O81864; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81864; baseline and differential.
DR Genevisible; O81864; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR044197; FKBP17-1-like.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR47860; PTHR47860; 1.
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..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 64..?
FT /note="Thylakoid"
FT CHAIN ?..229
FT /note="Peptidyl-prolyl cis-trans isomerase FKBP17-1,
FT chloroplastic"
FT /id="PRO_0000416132"
FT DOMAIN 105..225
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ SEQUENCE 229 AA; 24713 MW; D96627F933CF23AE CRC64;
MIRCFAWTPL VGAPLITTVH FTSPPSLRIF ASRSSAPSSS SSSSSTVAAA SRRSISLSII
AVTSSVVSSF CFSSPALADF SEIPNSGGVK ALDLRIGDGD VPIEGDQIEI HYYGRLAAKQ
GWRFDSTYDH KDSNGEAVPF TFVLGSSKVI PGIETAVRSM KVGGIRRVVI PPSQGYQNTS
QEPLPPNFFD RQRLFTTIFN PTRLANGEGS TLGTLVFDIE LVSTRRLHR
