CYP40_ARATH
ID CYP40_ARATH Reviewed; 361 AA.
AC Q9C566; Q08A80; Q9XIL2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP40 {ECO:0000303|PubMed:15047905};
DE Short=PPIase CYP40 {ECO:0000303|PubMed:15047905};
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 40 kDa {ECO:0000303|PubMed:11264535, ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE Short=AtCYP40 {ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE Short=Cyclophilin-40 {ECO:0000303|PubMed:11264535, ECO:0000303|PubMed:15047905, ECO:0000303|PubMed:15051864};
DE AltName: Full=Protein SQUINT {ECO:0000303|PubMed:11264535};
DE AltName: Full=Rotamase CYP40 {ECO:0000303|PubMed:11264535};
GN Name=CYP40 {ECO:0000303|PubMed:11264535, ECO:0000303|PubMed:15047905,
GN ECO:0000303|PubMed:15051864}; Synonyms=SQN {ECO:0000303|PubMed:11264535};
GN OrderedLocusNames=At2g15790 {ECO:0000312|Araport:AT2G15790};
GN ORFNames=F19G14.21 {ECO:0000312|EMBL:AAD41985.2};
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, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11264535; DOI=10.1126/science.1057144;
RA Berardini T.Z., Bollman K., Sun H., Poethig R.S.;
RT "Regulation of vegetative phase change in Arabidopsis thaliana by
RT cyclophilin 40.";
RL Science 291:2405-2407(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP 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 [6]
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).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18441215; DOI=10.1105/tpc.107.053306;
RA Prunet N., Morel P., Thierry A.-M., Eshed Y., Bowman J.L., Negrutiu I.,
RA Trehin C.;
RT "REBELOTE, SQUINT, and ULTRAPETALA1 function redundantly in the temporal
RT regulation of floral meristem termination in Arabidopsis thaliana.";
RL Plant Cell 20:901-919(2008).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (PubMed:11264535).
CC It catalyzes the cis-trans isomerization of proline imidic peptide
CC bonds in oligopeptides (PubMed:11264535). Involved in promoting the
CC expression of the juvenile phase of vegetative development, and, to a
CC lower extent, in regulating the positioning of floral buds, floral
CC morphogenesis and the expression of HSPs (PubMed:11264535).
CC Collaboratively with RBL and ULT1, influences floral meristem (FM)
CC determinacy in an AGAMOUS and SUPERMAN-dependent manner, thus
CC contributing to the floral developmental homeostasis (PubMed:18441215).
CC {ECO:0000269|PubMed:11264535, ECO:0000269|PubMed:18441215}.
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:0000269|PubMed:18441215}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, roots,
CC shoots, leaves, stems, inflorescences, flowers and siliques, with
CC highest levels dividing tissues. {ECO:0000269|PubMed:11264535,
CC ECO:0000269|PubMed:18441215}.
CC -!- DISRUPTION PHENOTYPE: Plants lacking both CRC and CYP40/SQN exhibit
CC strong floral meristem (FM) indeterminacy with reiterations of extra
CC floral whorls in the center of the flower associated with reduced
CC AGAMOUS and SUPERMAN levels. {ECO:0000269|PubMed:18441215}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AY026065; AAK02067.1; -; mRNA.
DR EMBL; AC006438; AAD41985.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06438.1; -; Genomic_DNA.
DR EMBL; BT028999; ABI93908.1; -; mRNA.
DR PIR; D84533; D84533.
DR RefSeq; NP_565381.1; NM_127141.3.
DR AlphaFoldDB; Q9C566; -.
DR SMR; Q9C566; -.
DR BioGRID; 1433; 3.
DR IntAct; Q9C566; 1.
DR MINT; Q9C566; -.
DR STRING; 3702.AT2G15790.1; -.
DR iPTMnet; Q9C566; -.
DR PaxDb; Q9C566; -.
DR PRIDE; Q9C566; -.
DR ProteomicsDB; 222668; -.
DR EnsemblPlants; AT2G15790.1; AT2G15790.1; AT2G15790.
DR GeneID; 816074; -.
DR Gramene; AT2G15790.1; AT2G15790.1; AT2G15790.
DR KEGG; ath:AT2G15790; -.
DR Araport; AT2G15790; -.
DR TAIR; locus:2044596; AT2G15790.
DR eggNOG; KOG0546; Eukaryota.
DR HOGENOM; CLU_012062_37_3_1; -.
DR InParanoid; Q9C566; -.
DR OMA; CKDFGNK; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9C566; -.
DR PRO; PR:Q9C566; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9C566; baseline and differential.
DR Genevisible; Q9C566; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
DR GO; GO:0010582; P:floral meristem determinacy; IGI: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:0010050; P:vegetative phase change; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF07719; TPR_2; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Isomerase; Reference proteome; Repeat; Rotamase;
KW TPR repeat.
FT CHAIN 1..361
FT /note="Peptidyl-prolyl cis-trans isomerase CYP40"
FT /id="PRO_0000064138"
FT DOMAIN 7..172
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 212..245
FT /note="TPR 1"
FT REPEAT 298..331
FT /note="TPR 2"
SQ SEQUENCE 361 AA; 40607 MW; BF3D1FE56DE7FD57 CRC64;
MGRSKCFMDI SIGGELEGRI VIELYDDVVP KTAENFRLLC TGEKGLGPNT GVPLHYKGNR
FHRVIKGFMI QGGDISANDG TGGESIYGLK FDDENFELKH ERKGMLSMAN SGPNTNGSQF
FITTTRTSHL DGKHVVFGRV TKGMGVVRSI EHVSIEEQSC PSQDVVIHDC GEIPEGADDG
ICDFFKDGDV YPDWPIDLNE SPAELSWWME TVDFVKAHGN EHFKKQDYKM ALRKYRKALR
YLDICWEKEG IDEETSTALR KTKSQIFTNS AACKLKFGDA KGALLDTEFA MRDEDNNVKA
LFRQGQAYMA LNNVDAAAES LEKALQFEPN DAGIKKEYAA VMKKIAFRDN EEKKQYRKMF
V
