CP18D_ARATH
ID CP18D_ARATH Reviewed; 172 AA.
AC Q42406; Q0WRR9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 152.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP18-4;
DE Short=PPIase CYP18-4;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 18 kDa 4;
DE Short=Cyclophilin-1;
DE AltName: Full=Rotamase cyclophilin-5;
GN Name=CYP18-4; Synonyms=43H1, CYP1, CYPA, ROC5; OrderedLocusNames=At4g34870;
GN ORFNames=T11I11.110;
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].
RC STRAIN=cv. Columbia;
RX 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 cis-
RT 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 PubMed=7767603; DOI=10.1093/oxfordjournals.pcp.a078770;
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 Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 36:377-382(1995).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND INDUCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9426607; DOI=10.1023/a:1005930024796;
RA Chou I.T., Gasser C.S.;
RT "Characterization of the cyclophilin gene family of Arabidopsis thaliana
RT and phylogenetic analysis of known cyclophilin proteins.";
RL Plant Mol. Biol. 35:873-892(1997).
RN [9]
RP INTERACTION WITH AGROBACTERIUM VIRD2.
RX PubMed=9618535; DOI=10.1073/pnas.95.12.7040;
RA Deng W., Chen L., Wood D.W., Metcalfe T., Liang X., Gordon M.P., Comai L.,
RA Nester E.W.;
RT "Agrobacterium VirD2 protein interacts with plant host cyclophilins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7040-7045(1998).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10361676; DOI=10.1271/bbb.63.632;
RA Saito T., Tadakuma K., Takahashi N., Ashida H., Tanaka K., Kawamukai M.,
RA 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 [11]
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 isomerases in
RT Arabidopsis.";
RL Plant Physiol. 134:1248-1267(2004).
RN [12]
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 the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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 -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with A.tumefaciens VirD2.
CC {ECO:0000269|PubMed:9618535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in roots and
CC flowers. Confined to vascular tissues. Also detected in stigmas, base
CC of siliques and anthers. {ECO:0000269|PubMed:10361676,
CC ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:9426607}.
CC -!- INDUCTION: Down-regulated by salt and cytokinin treatment.
CC {ECO:0000269|PubMed:9426607}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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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; CP002687; AEE86431.1; -; Genomic_DNA.
DR EMBL; AY054468; AAK96660.1; -; mRNA.
DR EMBL; BT006560; AAP21368.1; -; mRNA.
DR EMBL; AK228231; BAF00180.1; -; mRNA.
DR EMBL; AY087606; AAM65147.1; -; mRNA.
DR PIR; S50141; S50141.
DR RefSeq; NP_195213.1; NM_119653.4.
DR AlphaFoldDB; Q42406; -.
DR SMR; Q42406; -.
DR BioGRID; 14921; 6.
DR IntAct; Q42406; 1.
DR STRING; 3702.AT4G34870.1; -.
DR MetOSite; Q42406; -.
DR PaxDb; Q42406; -.
DR PRIDE; Q42406; -.
DR ProteomicsDB; 240859; -.
DR EnsemblPlants; AT4G34870.1; AT4G34870.1; AT4G34870.
DR GeneID; 829639; -.
DR Gramene; AT4G34870.1; AT4G34870.1; AT4G34870.
DR KEGG; ath:AT4G34870; -.
DR Araport; AT4G34870; -.
DR TAIR; locus:2116880; AT4G34870.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q42406; -.
DR OMA; NTANNEF; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q42406; -.
DR PRO; PR:Q42406; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42406; baseline and differential.
DR Genevisible; Q42406; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISS:TAIR.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..172
FT /note="Peptidyl-prolyl cis-trans isomerase CYP18-4"
FT /id="PRO_0000064134"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
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
