ID   CP18B_ARATH             Reviewed;         164 AA.
AC   Q9SIH1; Q8LF78;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP18-2;
DE            Short=PPIase CYP18-2;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin of 18 kDa 2;
DE   AltName: Full=Cyclophilin-18-2;
GN   Name=CYP18-2; OrderedLocusNames=At2g36130; ORFNames=F9C22.6;
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], 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   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., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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;
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   [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, GENE FAMILY, NOMENCLATURE, AND INDUCTION.
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: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15047905,
CC       ECO:0000269|PubMed:15051864}.
CC   -!- INDUCTION: Down-regulated by pathogen. {ECO:0000269|PubMed:15047905}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; AY568516; AAS75299.1; -; mRNA.
DR   EMBL; AC007135; AAD26970.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09209.1; -; Genomic_DNA.
DR   EMBL; AY102153; AAM26720.1; -; mRNA.
DR   EMBL; AF389280; AAK63853.1; -; mRNA.
DR   EMBL; AY085003; AAM61561.1; -; mRNA.
DR   PIR; C84777; C84777.
DR   RefSeq; NP_181157.1; NM_129172.6.
DR   AlphaFoldDB; Q9SIH1; -.
DR   SMR; Q9SIH1; -.
DR   BioGRID; 3530; 5.
DR   IntAct; Q9SIH1; 2.
DR   STRING; 3702.AT2G36130.1; -.
DR   PaxDb; Q9SIH1; -.
DR   PRIDE; Q9SIH1; -.
DR   ProteomicsDB; 240331; -.
DR   EnsemblPlants; AT2G36130.1; AT2G36130.1; AT2G36130.
DR   GeneID; 818186; -.
DR   Gramene; AT2G36130.1; AT2G36130.1; AT2G36130.
DR   KEGG; ath:AT2G36130; -.
DR   Araport; AT2G36130; -.
DR   TAIR; locus:2053491; AT2G36130.
DR   eggNOG; KOG0881; Eukaryota.
DR   HOGENOM; CLU_012062_16_3_1; -.
DR   InParanoid; Q9SIH1; -.
DR   OMA; ELYNDHA; -.
DR   OrthoDB; 1392223at2759; -.
DR   PhylomeDB; Q9SIH1; -.
DR   PRO; PR:Q9SIH1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIH1; baseline and differential.
DR   Genevisible; Q9SIH1; AT.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
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   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PTHR45625; 1.
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   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT   CHAIN           1..164
FT                   /note="Peptidyl-prolyl cis-trans isomerase CYP18-2"
FT                   /id="PRO_0000429933"
FT   DOMAIN          12..162
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        94
FT                   /note="G -> V (in Ref. 5; AAM61561)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   164 AA;  18233 MW;  A512A9F40F69B7C1 CRC64;
     MSARPEGSPP EVTLETSMGP FTVEMYYKHS PRTCRNFLEL SRRGYYDNVL FHRIVKDFIV
     QGGDPTGTGR GGESIYGSKF EDEINKELKH TGAGILSMAN AGPNTNGSQF FITLAPQPSL
     DGKHTIFGRV CRGMEVIKRL GSVQTDNTDR PIHEVKILRT KVID