CP20A_ARATH
ID CP20A_ARATH Reviewed; 204 AA.
AC Q9SP02;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP20-1;
DE Short=PPIase CYP20-1;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 20 kDa 1;
DE AltName: Full=Rotamase CYP20-1;
DE AltName: Full=Rotamase cyclophilin-7;
DE Flags: Precursor;
GN Name=CYP20-1; Synonyms=ROC7; OrderedLocusNames=At5g58710; ORFNames=MZN1.15;
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], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH
RP PP2AA1/RCN1, AND MUTAGENESIS OF 124-GLU--LEU-128.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10628867; DOI=10.1007/s004380051147;
RA Jackson K., Soell D.;
RT "Mutations in a new Arabidopsis cyclophilin disrupt its interaction with
RT protein phosphatase 2A.";
RL Mol. Gen. Genet. 262:830-838(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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, 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. Seems to be involved in root development.
CC {ECO:0000269|PubMed:10628867}.
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 the PP2A A subunit PP2AA1/RCN1.
CC {ECO:0000269|PubMed:10628867}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Secreted
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in aerial organs. Higher levels
CC in leaf and buds, and lower levels in seedlings.
CC {ECO:0000269|PubMed:10628867, ECO:0000269|PubMed:15047905}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AF192490; AAF05760.1; -; mRNA.
DR EMBL; AB020755; BAA97339.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97088.1; -; Genomic_DNA.
DR EMBL; AY048227; AAK82490.1; -; mRNA.
DR EMBL; AY094017; AAM16173.1; -; mRNA.
DR EMBL; AY086471; AAM63473.1; -; mRNA.
DR PIR; T50838; T50838.
DR RefSeq; NP_200679.1; NM_125258.5.
DR AlphaFoldDB; Q9SP02; -.
DR SMR; Q9SP02; -.
DR STRING; 3702.AT5G58710.1; -.
DR PaxDb; Q9SP02; -.
DR PRIDE; Q9SP02; -.
DR ProteomicsDB; 224490; -.
DR EnsemblPlants; AT5G58710.1; AT5G58710.1; AT5G58710.
DR GeneID; 835985; -.
DR Gramene; AT5G58710.1; AT5G58710.1; AT5G58710.
DR KEGG; ath:AT5G58710; -.
DR Araport; AT5G58710; -.
DR TAIR; locus:2178863; AT5G58710.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR OMA; MELFADQ; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9SP02; -.
DR PRO; PR:Q9SP02; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SP02; baseline and differential.
DR Genevisible; Q9SP02; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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 GO; GO:0048364; P:root development; IMP: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; Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..204
FT /note="Peptidyl-prolyl cis-trans isomerase CYP20-1"
FT /id="PRO_0000044627"
FT DOMAIN 38..201
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MUTAGEN 124..128
FT /note="ENFKL->AAFAA,KNFEL: Reduced interaction with
FT PP2AA1/RCN1."
FT /evidence="ECO:0000269|PubMed:10628867"
SQ SEQUENCE 204 AA; 21961 MW; CE2967AB4F65AF44 CRC64;
MASSVTLLLW SLLLLGTLSA IQAKKSKENL KEITHKVYFD VEIDGKAAGR IVMGLFGKTV
PKTVENFRAL CTGEKGIGKN GKALHYKGSS FHRIIPSFML QGGDFTHGNG MGGESIYGEK
FADENFKLKH TGPGFLSMAN AGQDTNGSQF FITTVTTSWL DGRHVVFGKV VTGMDVVYKV
EAEGNQSGTP KSKVVIVDSG ELPL
