CP19A_ARATH
ID CP19A_ARATH Reviewed; 173 AA.
AC Q38900; F4IL99;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP19-1 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE Short=PPIase CYP19-1 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:P62937};
DE AltName: Full=Cyclophilin of 19 kDa 1 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE AltName: Full=Rotamase cyclophilin-3 {ECO:0000303|PubMed:15051864, ECO:0000303|PubMed:9426607};
GN Name=CYP19-1 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
GN Synonyms=ROC3 {ECO:0000303|PubMed:15051864, ECO:0000303|PubMed:9426607};
GN OrderedLocusNames=At2g16600 {ECO:0000312|Araport:AT2G16600};
GN ORFNames=T24I21.1 {ECO:0000312|EMBL:AAD24594.1};
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] (ISOFORM 1), TISSUE SPECIFICITY, 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 [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] (ISOFORM 1).
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] (ISOFORM 1).
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, 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 [7]
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).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=16014362; DOI=10.1093/jxb/eri242;
RA Stangeland B., Nestestog R., Grini P.E., Skrbo N., Berg A., Salehian Z.,
RA Mandal A., Aalen R.B.;
RT "Molecular analysis of Arabidopsis endosperm and embryo promoter trap
RT lines: reporter-gene expression can result from T-DNA insertions in
RT antisense orientation, in introns and in intergenic regions, in addition to
RT sense insertion at the 5' end of genes.";
RL J. Exp. Bot. 56:2495-2505(2005).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PATHOGEN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24440291; DOI=10.1016/j.gene.2014.01.029;
RA Pogorelko G.V., Mokryakova M., Fursova O.V., Abdeeva I., Piruzian E.S.,
RA Bruskin S.A.;
RT "Characterization of three Arabidopsis thaliana immunophilin genes involved
RT in the plant defense response against Pseudomonas syringae.";
RL Gene 538:12-22(2014).
RN [10]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Involved in reactive oxygen species production in
CC response to pathogen infection. {ECO:0000269|PubMed:24440291}.
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 Evidence={ECO:0000250|UniProtKB:P62937};
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 DEK3. {ECO:0000269|PubMed:25387881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24440291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q38900-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q38900-2; Sequence=VSP_055385;
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in stems and flowers.
CC In seeds, present in endosperm and embryo.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:16014362,
CC ECO:0000269|PubMed:9426607}.
CC -!- INDUCTION: Up-regulated by light, wounding and pathogen infection.
CC {ECO:0000269|PubMed:24440291, ECO:0000269|PubMed:9426607}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to P.syringae infection.
CC {ECO:0000269|PubMed:24440291}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; U40399; AAB96832.1; -; mRNA.
DR EMBL; AC005825; AAD24594.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06517.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06518.1; -; Genomic_DNA.
DR EMBL; AY048215; AAK82478.1; -; mRNA.
DR EMBL; AY091694; AAM10293.1; -; mRNA.
DR EMBL; AY086330; AAM64399.1; -; mRNA.
DR PIR; S71219; S71219.
DR RefSeq; NP_001077901.1; NM_001084432.1. [Q38900-2]
DR RefSeq; NP_001318231.1; NM_001335481.1. [Q38900-1]
DR AlphaFoldDB; Q38900; -.
DR SMR; Q38900; -.
DR BioGRID; 1518; 6.
DR IntAct; Q38900; 2.
DR STRING; 3702.AT2G16600.1; -.
DR iPTMnet; Q38900; -.
DR MetOSite; Q38900; -.
DR PaxDb; Q38900; -.
DR PRIDE; Q38900; -.
DR ProteomicsDB; 240661; -. [Q38900-1]
DR EnsemblPlants; AT2G16600.1; AT2G16600.1; AT2G16600. [Q38900-1]
DR EnsemblPlants; AT2G16600.2; AT2G16600.2; AT2G16600. [Q38900-2]
DR GeneID; 816161; -.
DR Gramene; AT2G16600.1; AT2G16600.1; AT2G16600. [Q38900-1]
DR Gramene; AT2G16600.2; AT2G16600.2; AT2G16600. [Q38900-2]
DR KEGG; ath:AT2G16600; -.
DR Araport; AT2G16600; -.
DR TAIR; locus:2045076; AT2G16600.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q38900; -.
DR OMA; CKGTVVN; -.
DR PhylomeDB; Q38900; -.
DR PRO; PR:Q38900; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q38900; baseline and differential.
DR Genevisible; Q38900; AT.
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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
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 Alternative splicing; Chaperone; Cytoplasm; Isomerase; Reference proteome;
KW Rotamase.
FT CHAIN 1..173
FT /note="Peptidyl-prolyl cis-trans isomerase CYP19-1"
FT /id="PRO_0000064135"
FT DOMAIN 8..171
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 51..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055385"
SQ SEQUENCE 173 AA; 18492 MW; 9D292651B005F492 CRC64;
MATNPKVYFD MTVGGKSAGR IVMELYADTT PETAENFRAL CTGERGIGKQ GKPLHYKGSS
FHRVIPKFMC QGGDFTAGNG TGGESIYGSK FKDENFIKKH TGPGILSMAN AGANTNGSQF
FICTEKTSWL DGKHVVFGQV VEGLNVVRDI EKVGSDSGRT SKPVVIADCG QIS
