CPY57_ARATH
ID CPY57_ARATH Reviewed; 504 AA.
AC Q6Q152; O82646; Q0WU97;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP57;
DE Short=PPIase CYP57;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 57 kDa;
DE AltName: Full=Cyclophilin-57;
GN Name=CYP57; OrderedLocusNames=At4g33060; ORFNames=F4I10.3;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GENE FAMILY,
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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).
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
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).
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). Involved in plant response to pathogen
CC infection by increasing PAD4 expression in absence of EDS1 up-
CC regulation. {ECO:0000250, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24440291}. Cytoplasm
CC {ECO:0000269|PubMed:24440291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6Q152-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6Q152-2; Sequence=VSP_055393, VSP_055394;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Up-regulated upon pathogen infection.
CC {ECO:0000269|PubMed:24440291}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA21215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY568525; AAS75308.1; -; mRNA.
DR EMBL; AL031804; CAA21215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161582; CAB80023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86168.1; -; Genomic_DNA.
DR EMBL; BT025329; ABF57285.1; -; mRNA.
DR EMBL; AK227277; BAE99301.1; -; mRNA.
DR PIR; T05314; T05314.
DR RefSeq; NP_195032.2; NM_119460.5. [Q6Q152-1]
DR AlphaFoldDB; Q6Q152; -.
DR SMR; Q6Q152; -.
DR BioGRID; 14728; 2.
DR STRING; 3702.AT4G33060.1; -.
DR iPTMnet; Q6Q152; -.
DR PaxDb; Q6Q152; -.
DR PRIDE; Q6Q152; -.
DR ProteomicsDB; 224399; -. [Q6Q152-1]
DR EnsemblPlants; AT4G33060.1; AT4G33060.1; AT4G33060. [Q6Q152-1]
DR GeneID; 829443; -.
DR Gramene; AT4G33060.1; AT4G33060.1; AT4G33060. [Q6Q152-1]
DR KEGG; ath:AT4G33060; -.
DR Araport; AT4G33060; -.
DR TAIR; locus:2123822; AT4G33060.
DR eggNOG; KOG0885; Eukaryota.
DR HOGENOM; CLU_012062_14_4_1; -.
DR InParanoid; Q6Q152; -.
DR OMA; KKRRNQG; -.
DR PhylomeDB; Q6Q152; -.
DR PRO; PR:Q6Q152; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6Q152; baseline and differential.
DR Genevisible; Q6Q152; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 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 Acetylation; Alternative splicing; Chaperone; Coiled coil; Cytoplasm;
KW Isomerase; Nucleus; Reference proteome; Rotamase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..504
FT /note="Peptidyl-prolyl cis-trans isomerase CYP57"
FT /id="PRO_0000429942"
FT DOMAIN 16..167
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 237..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..274
FT /evidence="ECO:0000255"
FT COMPBIAS 237..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 249..252
FT /note="NASE -> AKLY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_055393"
FT VAR_SEQ 253..504
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_055394"
FT CONFLICT 59
FT /note="P -> H (in Ref. 5; BAE99301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56515 MW; 824E62DA59EB113B CRC64;
MSTVYVLEPP TKGKVIVNTT HGPIDVELWP KEAPKSVRNF VQLCLEGYFD NTIFHRVIPG
FLVQGGDPTG SGTGGDSIYG GVFADEFHSR LRFSHRGIVA MANASSPNSN GSQFFFTLDK
CDWLDKKHTI FGKVTGDSIY NLLRLGEVDT SKDDRPLDPA PKILSVEVLW NPFEDIVPRV
LAKTSEESAA EIKEPPTKPV KKLNLLSFGE EAEEEEKELA VVKQKIKSSH DVLNDPRLLK
AEASDKERNA SESKEVLSVR EALNAKKEAA QKDKSFSVSD TVGNSDDDDD GEDETKFDAK
MRNQVLSRRK EIGDTPSKPT QKKKSSSLKG REESTQRSDA VSSEDEKPRM EKLSLKKKGI
GSEAKAEHME KGDTDLQLYN ASERARQLHK LKKRRLQGNE DSVLAKLEKF KQSISAKPFT
SSNEPVVLTS SSEPVDNKEE DLSDWKNVKL KFAPERGKDK MSRRDDPDAY MVVDPLLEKG
KEKFNRMQAK QKRREREWSG KSLA
