ID Q94A16 PRELIMINARY; PRT; 125 AA. AC Q94A16; DT 01-DEC-2001 (TrEMBLrel. 19, Created) DT 01-DEC-2001 (TrEMBLrel. 19, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE At2g47320/T8I13.16 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) DE (PPIase) (Rotamase). OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RA Shinn P., Chen H., Cheuk R., Kim C.J., Koesema E., Meyers M.C., RA Banh J., Bowser L., Carninci P., Dale J.M., Goldsmith A.D., RA Hayashizaki Y., Ishida J., Jiang P.X., Jones T., Kamiya A., RA Karlin-Neumann G., Kawai J., Lam B., Lee J.M., Lin J., Liu S.X., RA Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., RA Pham P.K., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., RA Tang C.C., Toriumi M., Yamada K., Yamamura Y., Yu G., Yu S., RA Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Arabidopsis cDNA clones."; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Kim C.J., Chen H., Cheuk R., Meyers M.C., Shinn P., Banh J., RA Bowser L., Carninci P., Chang E., Dale J.M., Goldsmith A.D., RA Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., RA Kawai J., Lam B., Lee J.M., Lin J., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., RA Seki M., Southwick A., Tang C.C., Toriumi M., Wu H.C., Yamada K., RA Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIASES ACCELERATE THE FOLDING OF PROTEINS (BY CC SIMILARITY). CC -!- CATALYTIC ACTIVITY: PEPTIDYLPROLINE (OMEGA=180) = PEPTIDYLPROLINE CC (OMEGA=0). CC -!- SIMILARITY: BELONGS TO THE CYCLOPHILIN-TYPE PPIASE FAMILY. 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; AY050450; AAK91465.1; -. DR EMBL; AY097351; AAM19867.1; -. DR GO; GO:0042027; F:cyclophilin-type peptidyl-prolyl cis-trans ...; IEA. DR GO; GO:0004600; F:cyclophilin; IEA. DR GO; GO:0030051; F:FK506-sensitive peptidyl-prolyl cis-trans i...; IEA. DR GO; GO:0016853; F:isomerase activity; IEA. DR GO; GO:0006457; P:protein folding; IEA. DR InterPro; IPR002130; CSA_PPIase. DR Pfam; PF00160; pro_isomerase; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR PROSITE; PS50072; CSA_PPIASE_2; 1. KW Isomerase; Rotamase. SQ SEQUENCE 125 AA; 14303 MW; BAC0071317CF5A7D CRC64; MKFCQDGYFK GFLFSRVVKH FVIQAGDSAE FDAVKDWALD RKNIDTSLKH EEFMVGTPKA KNEQGGFEFF IVSAQIKDLN EKLTVFGRVS KGQDVVQEIE EVETDDQYQP KSPIEIMSVT LLQDM //