CP19C_ARATH
ID CP19C_ARATH Reviewed; 176 AA.
AC Q38867; Q38901; Q9LYN4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP19-3;
DE Short=PPIase CYP19-3;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 19 kDa 3;
DE AltName: Full=Cyclophilin-4;
DE AltName: Full=Rotamase cyclophilin-2;
GN Name=CYP19-3; Synonyms=CYP4, ROC2; OrderedLocusNames=At3g56070;
GN ORFNames=F18O21.30;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Saito T., Ashida H., Kawamukai M., Matsuda H., Nakagawa T.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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).
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: Ubiquitous, with highest levels in flowers and
CC lowest levels in roots. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:9426607}.
CC -!- INDUCTION: By wounding, and slightly by light.
CC {ECO:0000269|PubMed:9426607}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; U40400; AAB96833.1; -; Genomic_DNA.
DR EMBL; U31370; AAA74096.1; -; Genomic_DNA.
DR EMBL; AL163763; CAB87406.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79473.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79474.1; -; Genomic_DNA.
DR EMBL; AY072128; AAL59950.1; -; mRNA.
DR EMBL; AY096697; AAM20331.1; -; mRNA.
DR PIR; T47724; T47724.
DR PIR; T50767; T50767.
DR RefSeq; NP_001319764.1; NM_001339763.1.
DR RefSeq; NP_191166.1; NM_115465.5.
DR AlphaFoldDB; Q38867; -.
DR SMR; Q38867; -.
DR BioGRID; 10089; 6.
DR IntAct; Q38867; 4.
DR STRING; 3702.AT3G56070.1; -.
DR MetOSite; Q38867; -.
DR SwissPalm; Q38867; -.
DR PaxDb; Q38867; -.
DR PRIDE; Q38867; -.
DR ProteomicsDB; 240666; -.
DR EnsemblPlants; AT3G56070.1; AT3G56070.1; AT3G56070.
DR EnsemblPlants; AT3G56070.2; AT3G56070.2; AT3G56070.
DR GeneID; 824773; -.
DR Gramene; AT3G56070.1; AT3G56070.1; AT3G56070.
DR Gramene; AT3G56070.2; AT3G56070.2; AT3G56070.
DR KEGG; ath:AT3G56070; -.
DR Araport; AT3G56070; -.
DR TAIR; locus:2078451; AT3G56070.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q38867; -.
DR OMA; SIVSMRV; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q38867; -.
DR BRENDA; 5.2.1.8; 399.
DR PRO; PR:Q38867; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q38867; baseline and differential.
DR Genevisible; Q38867; AT.
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:0016018; F:cyclosporin A binding; ISS:TAIR.
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 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..176
FT /note="Peptidyl-prolyl cis-trans isomerase CYP19-3"
FT /id="PRO_0000064137"
FT DOMAIN 7..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT CONFLICT 155
FT /note="D -> Y (in Ref. 2; AAA74096)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="K -> N (in Ref. 1; AAB96833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 18921 MW; 24C2031B6CB4DD90 CRC64;
MANPKVFFDI LIGKMKAGRV VMELFADVTP RTANNFRALC TGENGIGKAG KALHYKGSAF
HRIIPGFMCQ GGDFTRGNGT GGESIYGSKF EDENFKLKHT GPGILSMANS GPNTNGSQFF
ICTEKTSWLD GKHVVFGKVV DGYNVVKAME DVGSDMGNPS ERVVIEDCGE LKNPSS
