ID CP21C_ARATH Reviewed; 230 AA. AC Q94A16; O22906; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 2. DT 28-NOV-2006, entry version 29. DE Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial precursor DE (EC 5.2.1.8) (PPIase CYP21-3) (Rotamase CYP21-3) (Cyclophilin of 21 DE kDa 3). GN Name=CYP21-3; OrderedLocusNames=At2g47320; ORFNames=T8I13.16; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND RP NOMENCLATURE. RX PubMed=15051864; DOI=10.1104/pp.103.022160; RA Romano P.G.N., Horton P., Gray J.E.; RT "The Arabidopsis cyclophilin gene family."; RL Plant Physiol. 134:1268-1282(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; 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., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP TISSUE SPECIFICITY. RX PubMed=15047905; DOI=10.1104/pp.103.031005; RA He Z., Li L., Luan S.; RT "Immunophilins and parvulins. Superfamily of peptidyl prolyl RT isomerases in Arabidopsis."; RL Plant Physiol. 134:1248-1267(2004). RN [5] RP INDUCTION. RX MEDLINE=102499135; PubMed=16173598; DOI=10.1021/es050385r; RA Ekman D.R., Wolfe N.L., Dean J.F.D.; RT "Gene expression changes in Arabidopsis thaliana seedling roots RT exposed to the munition hexahydro-1,3,5-trinitro-1,3,5-triazine."; RL Environ. Sci. Technol. 39:6313-6320(2005). CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes CC the cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of CC its effects via an inhibitory action on PPIase (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (Potential). CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in aerial organs. CC -!- INDUCTION: Repressed by the munition hexahydro-1,3,5-trinitro- CC 1,3,5-triazine, also known as Royal Demolition eXplosive (RDX). CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain. CC -!- CAUTION: Ref.3 (AAK91465) sequence differs from that shown due to CC a stop codon at position 82 which was translated as Leu to extend CC the sequence. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY568520; AAS75303.1; -; mRNA. DR EMBL; AC002337; AAB63832.1; -; Genomic_DNA. DR EMBL; AY050450; AAK91465.1; ALT_INIT; mRNA. DR EMBL; AY097351; AAM19867.1; -; mRNA. DR PIR; G84913; G84913. DR UniGene; At.25582; -. DR HSSP; P20752; 1J2A. DR GenomeReviews; CT485783_GR; AT2G47320. DR KEGG; ath:At2g47320; -. DR TAIR; At2g47320; -. DR InterPro; IPR002130; CSA_PPIase. DR Gene3D; G3DSA:2.40.100.10; CSA_PPIase; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS00170; CSA_PPIASE_1; FALSE_NEG. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Chaperone; Cyclosporin; Isomerase; Mitochondrion; Rotamase; KW Transit peptide. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 230 Peptidyl-prolyl cis-trans isomerase FT CYP21-3. FT /FTId=PRO_0000044628. FT DOMAIN 76 226 PPIase cyclophilin-type. SQ SEQUENCE 230 AA; 26042 MW; 6198D43EE5B9552F CRC64; MAKIKPQALL QQSKKKKGPS RISITNIVIY TLAVLLLVFV LFSAYRRWTH RSEIPTHNGR SVLEDAAFPG MKNVDLPRFA TLDTGKGSVT IELFKDTAPN VVDQFMKFCQ DGYFKGFLFS RVVKHFVIQA GDSAEFDAVK DWALDRKNID TSLKHEEFMV GTPKAKNEQG GFEFFIVSAQ IKDLNEKLTV FGRVSKGQDV VQEIEEVETD DQYQPKSPIE IMSVTLLQDM //