CPY71_ARATH
ID CPY71_ARATH Reviewed; 631 AA.
AC Q8W4D0; Q9LXM7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP71 {ECO:0000303|PubMed:15047905};
DE Short=PPIase CYP71 {ECO:0000303|PubMed:15047905};
DE EC=5.2.1.8 {ECO:0000269|PubMed:33098102};
DE AltName: Full=Cyclophilin of 71 kDa {ECO:0000305};
DE AltName: Full=Cyclophilin-71 {ECO:0000303|PubMed:17704213};
DE Short=AtCYP71 {ECO:0000303|PubMed:15047905};
GN Name=CYP71 {ECO:0000303|PubMed:15047905};
GN OrderedLocusNames=At3g44600 {ECO:0000312|Araport:AT3G44600};
GN ORFNames=F14L2.150 {ECO:0000312|EMBL:CAB88542.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 [4]
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 [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH HISTONE H3.
RX PubMed=17704213; DOI=10.1105/tpc.107.053579;
RA Li H., He Z., Lu G., Lee S.C., Alonso J., Ecker J.R., Luan S.;
RT "A WD40 domain cyclophilin interacts with histone H3 and functions in gene
RT repression and organogenesis in Arabidopsis.";
RL Plant Cell 19:2403-2416(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH FAS1 AND LHP1.
RX PubMed=21596687; DOI=10.1093/mp/ssr036;
RA Li H., Luan S.;
RT "The cyclophilin AtCYP71 interacts with CAF-1 and LHP1 and functions in
RT multiple chromatin remodeling processes.";
RL Mol. Plant 4:748-758(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 469-628, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=33098102; DOI=10.1002/1873-3468.13965;
RA Lakhanpal S., Fan J.S., Luan S., Swaminathan K.;
RT "Structural and functional analyses of the PPIase domain of
RT Arabidopsisthaliana CYP71 reveal its catalytic activity toward histone
RT H3.";
RL FEBS Lett. 595:145-154(2021).
CC -!- FUNCTION: PPIases accelerate the folding of proteins (Probable). It
CC catalyzes the cis-trans isomerization of proline imidic peptide bonds
CC in oligopeptides (PubMed:33098102). Histone proline isomerase that
CC increases the rate of cis-trans isomerization of the synthetic histone
CC H3 peptides H3P30 (RKSAP30F-p-nitroanilide) and H3P30K27me3 (RKme3-
CC SAP30F-p-nitroanilide) in the histone H3 N-terminal tail, in vitro
CC (PubMed:33098102). Histone remodeling factor involved in chromatin-
CC based gene silencing (PubMed:17704213). Reinforces H3K27 methylation
CC (PubMed:17704213). Involved in fundamental processes of chromatin
CC assembly and histone modification by mediating the targeting of FAS1
CC and LHP1 on the chromatin (PubMed:21596687). Required for the formation
CC and development of leaves, for normal phyllotaxy and for the formation,
CC maintenance and activity of root and shoot apical meristems
CC (PubMed:17704213). {ECO:0000269|PubMed:17704213,
CC ECO:0000269|PubMed:21596687, ECO:0000269|PubMed:33098102,
CC ECO:0000305|PubMed:17704213, ECO:0000305|PubMed:21596687}.
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 Evidence={ECO:0000269|PubMed:33098102};
CC -!- SUBUNIT: Interacts with FAS1 and LHP1 (PubMed:21596687). Interacts (via
CC WD repeat domain) with histone H3 (PubMed:17704213).
CC {ECO:0000269|PubMed:17704213, ECO:0000269|PubMed:21596687}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17704213}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the meristems.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864,
CC ECO:0000269|PubMed:17704213}.
CC -!- INDUCTION: Down-regulated by auxin treatment.
CC {ECO:0000269|PubMed:15047905}.
CC -!- DISRUPTION PHENOTYPE: Bushy and stunted stature.
CC {ECO:0000269|PubMed:17704213}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353818; CAB88542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77920.1; -; Genomic_DNA.
DR EMBL; AY062653; AAL32731.1; -; mRNA.
DR EMBL; BT008382; AAP37741.1; -; mRNA.
DR PIR; T48940; T48940.
DR RefSeq; NP_190046.2; NM_114328.4.
DR PDB; 6LKB; X-ray; 1.65 A; A/B=469-628.
DR PDBsum; 6LKB; -.
DR AlphaFoldDB; Q8W4D0; -.
DR SMR; Q8W4D0; -.
DR BioGRID; 8905; 5.
DR STRING; 3702.AT3G44600.1; -.
DR iPTMnet; Q8W4D0; -.
DR PaxDb; Q8W4D0; -.
DR PRIDE; Q8W4D0; -.
DR ProteomicsDB; 222617; -.
DR EnsemblPlants; AT3G44600.1; AT3G44600.1; AT3G44600.
DR GeneID; 823585; -.
DR Gramene; AT3G44600.1; AT3G44600.1; AT3G44600.
DR KEGG; ath:AT3G44600; -.
DR Araport; AT3G44600; -.
DR TAIR; locus:2076003; AT3G44600.
DR eggNOG; KOG0882; Eukaryota.
DR HOGENOM; CLU_012062_31_0_1; -.
DR InParanoid; Q8W4D0; -.
DR OMA; GGMVEYW; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q8W4D0; -.
DR PRO; PR:Q8W4D0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W4D0; baseline and differential.
DR Genevisible; Q8W4D0; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0042393; F:histone binding; IDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
DR GO; GO:0048440; P:carpel development; IMP:TAIR.
DR GO; GO:0000412; P:histone peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0010338; P:leaf formation; IMP:TAIR.
DR GO; GO:0010358; P:leaf shaping; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IDA:UniProtKB.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0031060; P:regulation of histone methylation; IMP:TAIR.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:TAIR.
DR GO; GO:0048453; P:sepal formation; IMP:TAIR.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Isomerase; Nucleus; Reference proteome; Repeat;
KW Rotamase; WD repeat.
FT CHAIN 1..631
FT /note="Peptidyl-prolyl cis-trans isomerase CYP71"
FT /id="PRO_0000429943"
FT REPEAT 68..106
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 111..150
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 201..240
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 257..297
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT DOMAIN 474..628
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:6LKB"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:6LKB"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:6LKB"
FT TURN 509..514
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6LKB"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:6LKB"
FT HELIX 584..586
FT /evidence="ECO:0007829|PDB:6LKB"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 592..598
FT /evidence="ECO:0007829|PDB:6LKB"
FT HELIX 600..607
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:6LKB"
FT STRAND 622..627
FT /evidence="ECO:0007829|PDB:6LKB"
SQ SEQUENCE 631 AA; 70984 MW; 15CCAD94C2EA09D4 CRC64;
MEEESKNGGT TIPTEELAVV AVPPVVEEEE PMVGPGPAPR GKRKRPLQFE QAYLDSLPSA
NMYEKSYMHR DVVTHVAVSA AEFFISGSMD GHLKFWKKKG VGIEFAKHFR SHLGPIEGLA
VSIDGLLCCT ISNDHAVKIY DVVNYDMMAM IRLPYIPGAV EWVYKQGDVK AKLAVSDRDS
LFVHIYDPRS GSNEPIASKE IHMNPIKVMK YNPVSDTMIS GDTKGIIEYW SATTLQFPED
EVNFKLKSDT NLFEIIKCKT TISAIEVSPD GKQFSITAPD RRIRVFWFRT GKLRRVYDES
LVVAQDLQRS DAPLYRLEAI DFGRRMAVEK ELEKTESAPQ PNAVFDESSN FLIYATFLGI
KVINLHTNTV ARILGKVESN ERYLRVALYQ GDQGGKKVRK IPAAAANVNE SKEPLTDPTI
LCCAFKKHRI YMFSRREPEE PEDASQGRDV FNEKPAADEL MSVSDIGNSA TTSLPENVIM
HTTLGDIHMK LYPEECPKTV ENFTTHCRNG YYDNHLFHRV IRGFMIQTGD PLGDGTGGQS
IWGREFEDEF HKSLRHDRPF TLSMANAGPN TNGSQFFITT VATPWLDNKH TVFGRVVKGM
DVVQGIEKVK TDKNDRPYQD VKILNVTVPK S
