CPY28_ARATH
ID CPY28_ARATH Reviewed; 281 AA.
AC O65220; A8MQM4; Q8VXW1;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic;
DE Short=PPIase CYP28;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 28 kDa;
DE AltName: Full=Cyclophilin-28;
DE Flags: Precursor;
GN Name=CYP28; OrderedLocusNames=At5g35100; ORFNames=F7N22.3;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 PROTEIN SEQUENCE OF 25-44, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND INDUCTION.
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 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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND S-NYTROSYLATION.
RX PubMed=18297659; DOI=10.1002/pmic.200700536;
RA Romero-Puertas M.C., Campostrini N., Matte A., Righetti P.G.,
RA Perazzolli M., Zolla L., Roepstorff P., Delledonne M.;
RT "Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana
RT undergoing hypersensitive response.";
RL Proteomics 8:1459-1469(2008).
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: Plastid, chloroplast
CC {ECO:0000269|PubMed:11719511}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O65220-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O65220-2; Sequence=VSP_055390;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Not detected in roots.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Down-regulated by dark and high CO(2) treatment.
CC {ECO:0000269|PubMed:15047905}.
CC -!- PTM: S-nytrosylated during the hypersensitive disease resistance
CC response.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL67133.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP000421; BAB10017.1; -; Genomic_DNA.
DR EMBL; AF058825; AAC13578.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93931.1; -; Genomic_DNA.
DR EMBL; AY074520; AAL67133.1; ALT_INIT; mRNA.
DR EMBL; BT015407; AAU05530.1; -; mRNA.
DR PIR; T01157; T01157.
DR RefSeq; NP_001078636.1; NM_001085167.1. [O65220-2]
DR AlphaFoldDB; O65220; -.
DR SMR; O65220; -.
DR STRING; 3702.AT5G35100.1; -.
DR PaxDb; O65220; -.
DR PRIDE; O65220; -.
DR ProteomicsDB; 222672; -. [O65220-1]
DR EnsemblPlants; AT5G35100.1; AT5G35100.1; AT5G35100.
DR EnsemblPlants; AT5G35100.2; AT5G35100.2; AT5G35100. [O65220-2]
DR GeneID; 833461; -.
DR Gramene; AT5G35100.1; AT5G35100.1; AT5G35100.
DR Gramene; AT5G35100.2; AT5G35100.2; AT5G35100. [O65220-2]
DR KEGG; ath:AT5G35100; -.
DR Araport; AT5G35100; -.
DR TAIR; locus:2150371; AT5G35100.
DR eggNOG; KOG0865; Eukaryota.
DR InParanoid; O65220; -.
DR PRO; PR:O65220; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65220; baseline and differential.
DR Genevisible; O65220; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; 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; IPR044178; CYP28-like.
DR PANTHER; PTHR47875; PTHR47875; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Chloroplast; Direct protein sequencing;
KW Isomerase; Plastid; Reference proteome; Rotamase; Transit peptide.
FT TRANSIT 1..24
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 25..281
FT /note="Peptidyl-prolyl cis-trans isomerase CYP28,
FT chloroplastic"
FT /id="PRO_0000429941"
FT DOMAIN 66..268
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 134..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055390"
SQ SEQUENCE 281 AA; 30505 MW; C5B1576D8BA9796E CRC64;
MASSSILIPP ILTRRNLLLS TTIATVTPPP PAKPPSPDIT ITDRVFLDFS LCPTYFRSDP
SATLSSTTPC SDSTPLGRVV LGLYGRHVPI TVSTFKRMCT SSSTSYKNTP VHKIFPGQYF
LAGRQGGGRR DTAEVGYSLR DLPRNTDVVN SKAFLLPHAR AGVVSLCLSE NDDDDDIRLD
PDYRNVEFLI TTGPGPSPQL DGGNIVFGTV LEGLDVVTSI SSIPTYKPSE NIKQFNDFAE
FLGDERAQNA RSLWNRPLKT VFISGCGELK VTNPSLSPTL P
