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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
 
 
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