ID   CP18D_ARATH             Reviewed;         172 AA.
AC   Q42406;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP18-4;
DE            Short=PPIase CYP18-4;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase cyclophilin-5;
DE   AltName: Full=Cyclophilin of 18 kDa 4;
DE            Short=Cyclophilin-1;
GN   Name=CYP18-4; Synonyms=43H1, CYP1, ROC5; OrderedLocusNames=At4g34870;
GN   ORFNames=T11I11.110;
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].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=95002172; PubMed=7918654; DOI=10.1016/0167-4781(94)90083-3;
RA   Hayman G.T., Miernyk J.A.;
RT   "The nucleotide and deduced amino acid sequences of a peptidyl-prolyl
RT   cis-trans isomerase from Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1219:536-538(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   MEDLINE=95285113; PubMed=7767603;
RA   Saito T., Ishiguro S., Ashida H., Kawamukai M., Matsuda H., Ochiai H.,
RA   Nakagawa T.;
RT   "Cloning and sequence analysis of genes for cyclophilin from
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 36:377-382(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
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   [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   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   MEDLINE=98088013; PubMed=9426607; DOI=10.1023/A:1005930024796;
RA   Chou I.T., Gasser C.S.;
RT   "Characterization of the cyclophilin gene family of Arabidopsis
RT   thaliana and phylogenetic analysis of known cyclophilin proteins.";
RL   Plant Mol. Biol. 35:873-892(1997).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99290027; PubMed=10361676; DOI=10.1271/bbb.63.632;
RA   Saito T., Tadakuma K., Takahashi N., Ashida H., Tanaka K.,
RA   Kawamukai M., Matsuda H., Nakagawa T.;
RT   "Two cytosolic cyclophilin genes of Arabidopsis thaliana differently
RT   regulated in temporal- and organ-specific expression.";
RL   Biosci. Biotechnol. Biochem. 63:632-637(1999).
RN   [8]
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   [9]
RP   GENE FAMILY, AND 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).
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: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots and
CC       flowers. Confined to vascular tissues. Also detected in stigmas,
CC       base of siliques and anthers.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
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DR   EMBL; U07276; AAA66197.1; -; mRNA.
DR   EMBL; U32186; AAA75512.1; -; Genomic_DNA.
DR   EMBL; AL079347; CAB45448.1; -; Genomic_DNA.
DR   EMBL; AL161586; CAB80204.1; -; Genomic_DNA.
DR   EMBL; AY054468; AAK96660.1; -; mRNA.
DR   EMBL; BT006560; AAP21368.1; -; mRNA.
DR   EMBL; AY087606; AAM65147.1; -; mRNA.
DR   IPI; IPI00534382; -.
DR   PIR; S50141; S50141.
DR   RefSeq; NP_195213.1; -.
DR   UniGene; At.421; -.
DR   UniGene; At.71932; -.
DR   HSSP; P52011; 1E3B.
DR   SMR; Q42406; 1-171.
DR   PRIDE; Q42406; -.
DR   ProMEX; Q42406; -.
DR   GeneID; 829639; -.
DR   GenomeReviews; CT486007_GR; AT4G34870.
DR   KEGG; ath:AT4G34870; -.
DR   NMPDR; fig|3702.1.peg.21561; -.
DR   GeneFarm; 5174; -.
DR   TAIR; At4g34870; -.
DR   OMA; Q42406; PAGRVEM.
DR   BRENDA; 5.2.1.8; 302.
DR   ArrayExpress; Q42406; -.
DR   GermOnline; AT4G34870; Arabidopsis thaliana.
DR   GO; GO:0048046; C:apoplast; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Complete proteome; Cyclosporin; Cytoplasm; Isomerase;
KW   Rotamase.
FT   CHAIN         1    172       Peptidyl-prolyl cis-trans isomerase
FT                                CYP18-4.
FT                                /FTId=PRO_0000064134.
FT   DOMAIN        7    170       PPIase cyclophilin-type.
SQ   SEQUENCE   172 AA;  18378 MW;  C6E082F594E73913 CRC64;
     MSNPRVFFDM SLSGTPIGRI EMELFADTTP NTAENFRALC TGEKGMGKLG KPLHFKGSIF
     HRVIPGFMCQ GGDFTAKNGT GGESIYGAKF KDENFIKKHT GAGILSMANS GPNTNGSQFF
     ICTDKTSWLD GKHVVFGQVV KGLDVVKAIE KVGSDSGKTS KVVTITDCGQ LS
//