ID   CP19B_ARATH             Reviewed;         174 AA.
AC   Q9SKQ0; O22516; Q1H5D7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP19-2;
DE            Short=PPIase CYP19-2;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin of 19 kDa 2;
DE            Short=Cyclophilin-2;
DE   AltName: Full=Rotamase cyclophilin-6;
GN   Name=CYP19-2; Synonyms=CYP2, ROC6; OrderedLocusNames=At2g21130;
GN   ORFNames=F26H11.11;
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 [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   [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].
RA   Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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, AND DEVELOPMENTAL STAGE.
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   [7]
RP   TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
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   [8]
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in aerial organs, at high levels
CC       in young rosette leaves and flowers, at low levels in older tissues.
CC       {ECO:0000269|PubMed:10361676, ECO:0000269|PubMed:15047905}.
CC   -!- DEVELOPMENTAL STAGE: Mostly expressed in young tissues. Expressed in
CC       all parts of floral buds, but later confined to stigma and anthers.
CC       {ECO:0000269|PubMed:10361676}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; AF020434; AAB71402.1; -; Genomic_DNA.
DR   EMBL; AC006264; AAD29803.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07126.1; -; Genomic_DNA.
DR   EMBL; BT025527; ABF58945.1; -; mRNA.
DR   EMBL; AY087454; AAM65000.1; -; mRNA.
DR   PIR; E84597; E84597.
DR   PIR; T50772; T50772.
DR   RefSeq; NP_179709.1; NM_127683.3.
DR   AlphaFoldDB; Q9SKQ0; -.
DR   SMR; Q9SKQ0; -.
DR   BioGRID; 2001; 1.
DR   STRING; 3702.AT2G21130.1; -.
DR   PaxDb; Q9SKQ0; -.
DR   PRIDE; Q9SKQ0; -.
DR   ProteomicsDB; 241218; -.
DR   EnsemblPlants; AT2G21130.1; AT2G21130.1; AT2G21130.
DR   GeneID; 816648; -.
DR   Gramene; AT2G21130.1; AT2G21130.1; AT2G21130.
DR   KEGG; ath:AT2G21130; -.
DR   Araport; AT2G21130; -.
DR   TAIR; locus:2047097; AT2G21130.
DR   eggNOG; KOG0865; Eukaryota.
DR   HOGENOM; CLU_012062_4_2_1; -.
DR   InParanoid; Q9SKQ0; -.
DR   OMA; MRAPIVN; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; Q9SKQ0; -.
DR   PRO; PR:Q9SKQ0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SKQ0; baseline and differential.
DR   Genevisible; Q9SKQ0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; 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; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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   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..174
FT                   /note="Peptidyl-prolyl cis-trans isomerase CYP19-2"
FT                   /id="PRO_0000064136"
FT   DOMAIN          8..171
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CONFLICT        166
FT                   /note="I -> V (in Ref. 1; AAB71402)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  18464 MW;  6D322CB197ABC7AF CRC64;
     MASHPKVFFD MTIGGAPAGK IVMELYTDKT PKTAENFRAL CTGEKGVGRS GKPLHFKGSS
     FHRVIPNFMC QGGDFTKGNG TGGESIYGAK FEDENFERKH TGPGILSMAN AGANTNGSQF
     FICTVKTDWL DGKHVVFGQV VEGLDVVKAI EKIGSSSGKP TKPVVIADCG EISS