CYP23_ARATH
ID CYP23_ARATH Reviewed; 226 AA.
AC Q8LDR3; Q9ZVG4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP23;
DE Short=PPIase CYP23;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 23 kDa;
DE AltName: Full=Cyclophilin-23;
DE Flags: Precursor;
GN Name=CYP23; Synonyms=CYP23-1; OrderedLocusNames=At1g26940;
GN ORFNames=T2P11.13;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 TISSUE SPECIFICITY, 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 (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: Endoplasmic reticulum {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Lower expression in roots.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD14500.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005508; AAD14500.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30762.1; -; Genomic_DNA.
DR EMBL; AK118273; BAC42891.1; -; mRNA.
DR EMBL; BT005541; AAO63961.1; -; mRNA.
DR EMBL; AY085848; AAM63062.1; -; mRNA.
DR PIR; D86396; D86396.
DR RefSeq; NP_564267.1; NM_102458.2.
DR AlphaFoldDB; Q8LDR3; -.
DR SMR; Q8LDR3; -.
DR STRING; 3702.AT1G26940.1; -.
DR PaxDb; Q8LDR3; -.
DR PRIDE; Q8LDR3; -.
DR ProteomicsDB; 224695; -.
DR EnsemblPlants; AT1G26940.1; AT1G26940.1; AT1G26940.
DR GeneID; 839584; -.
DR Gramene; AT1G26940.1; AT1G26940.1; AT1G26940.
DR KEGG; ath:AT1G26940; -.
DR Araport; AT1G26940; -.
DR TAIR; locus:2202775; AT1G26940.
DR eggNOG; KOG0884; Eukaryota.
DR HOGENOM; CLU_012062_16_6_1; -.
DR InParanoid; Q8LDR3; -.
DR OrthoDB; 1245241at2759; -.
DR PhylomeDB; Q8LDR3; -.
DR PRO; PR:Q8LDR3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LDR3; baseline and differential.
DR Genevisible; Q8LDR3; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044233; CYP23-like.
DR PANTHER; PTHR47511; PTHR47511; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Endoplasmic reticulum; Isomerase; Reference proteome; Rotamase;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..226
FT /note="Peptidyl-prolyl cis-trans isomerase CYP23"
FT /id="PRO_0000429938"
FT DOMAIN 34..191
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 226 AA; 25515 MW; 95183C1BDD014118 CRC64;
MGITRNLILG LACLAFVSIA KALPHEPELG SARVVFQTSY GDIEFGFYPT VAPKTVDHIF
KLVRLGGYNT NHFFRVDKGF VAQVADVASG RSAPMNEEQR KEAEKKIVGE FSDVKHVRGT
LSMGRYDDPN SAQSSFSMLL GNAPHLDRQY AVFGKVTKGD ETLSKLEEVP TRREGIFVMP
TERITILSTY YYDTKMESCE EERSVLKRRL QASFVEVERQ RMKCFP
