CYP63_ARATH
ID CYP63_ARATH Reviewed; 570 AA.
AC Q9LY75; C0Z3E4; F4J100; Q6Q150;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP63;
DE Short=AtCYP63;
DE Short=PPIase CYP63;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-63;
DE AltName: Full=Cyclophilin-like protein CypRS64;
GN Name=CYP63; Synonyms=CYPRS64; OrderedLocusNames=At3g63400;
GN ORFNames=MAA21.30;
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 2), 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=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 [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).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 ALTERNATIVE SPLICING, INTERACTION WITH RNU1; SCL28; SCL30; SR30 AND SR34,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15166240; DOI=10.1074/jbc.m400270200;
RA Lorkovic Z.J., Lopato S., Pexa M., Lehner R., Barta A.;
RT "Interactions of Arabidopsis RS domain containing cyclophilins with SR
RT proteins and U1 and U11 small nuclear ribonucleoprotein-specific proteins
RT suggest their involvement in pre-mRNA Splicing.";
RL J. Biol. Chem. 279:33890-33898(2004).
RN [8]
RP INTERACTION WITH SNRNP35.
RX PubMed=15987817; DOI=10.1261/rna.2440305;
RA Lorkovic Z.J., Lehner R., Forstner C., Barta A.;
RT "Evolutionary conservation of minor U12-type spliceosome between plants and
RT humans.";
RL RNA 11:1095-1107(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. May be implicated in the folding, transport, and
CC assembly of proteins. Probably involved in early steps of spliceosomal
CC assembly.
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 -!- SUBUNIT: Interacts with SNRNP35, RNU1, SCL28, SCL30, SR30 and SR34. The
CC binding to SR34 is phosphorylation-dependent (PubMed:15166240).
CC {ECO:0000269|PubMed:15166240, ECO:0000269|PubMed:15987817}.
CC -!- INTERACTION:
CC Q9LY75; Q1PDV2: SCL28; NbExp=4; IntAct=EBI-2360522, EBI-927052;
CC Q9LY75; Q8L3X8: SCL30; NbExp=4; IntAct=EBI-2360522, EBI-927061;
CC Q9LY75; Q9XFR5: SR30; NbExp=4; IntAct=EBI-2360522, EBI-1540237;
CC Q9LY75; O22315: SR34; NbExp=3; IntAct=EBI-2360522, EBI-927464;
CC Q9LY75; Q9SEE9: SR45; NbExp=2; IntAct=EBI-2360522, EBI-1792008;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15166240}. Nucleus speckle
CC {ECO:0000269|PubMed:15166240}. Note=Moves from nuclear bodies to
CC nuclear speckles upon interaction with SR proteins.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LY75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LY75-2; Sequence=VSP_055003;
CC Name=3;
CC IsoId=Q9LY75-3; Sequence=VSP_055002;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:15051864}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AY568527; AAS75310.1; -; mRNA.
DR EMBL; AL163818; CAB87793.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80475.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80476.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80477.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64659.1; -; Genomic_DNA.
DR EMBL; BT000915; AAN41315.1; -; mRNA.
DR EMBL; AK319108; BAH57223.1; -; mRNA.
DR PIR; T49181; T49181.
DR RefSeq; NP_001190169.1; NM_001203240.1. [Q9LY75-1]
DR RefSeq; NP_001326672.1; NM_001340212.1. [Q9LY75-1]
DR RefSeq; NP_191899.1; NM_116205.5. [Q9LY75-1]
DR RefSeq; NP_850740.1; NM_180409.2. [Q9LY75-3]
DR AlphaFoldDB; Q9LY75; -.
DR SMR; Q9LY75; -.
DR BioGRID; 10829; 4.
DR IntAct; Q9LY75; 8.
DR STRING; 3702.AT3G63400.3; -.
DR iPTMnet; Q9LY75; -.
DR PaxDb; Q9LY75; -.
DR PRIDE; Q9LY75; -.
DR ProteomicsDB; 224696; -. [Q9LY75-1]
DR EnsemblPlants; AT3G63400.1; AT3G63400.1; AT3G63400. [Q9LY75-1]
DR EnsemblPlants; AT3G63400.2; AT3G63400.2; AT3G63400. [Q9LY75-3]
DR EnsemblPlants; AT3G63400.3; AT3G63400.3; AT3G63400. [Q9LY75-1]
DR EnsemblPlants; AT3G63400.4; AT3G63400.4; AT3G63400. [Q9LY75-1]
DR GeneID; 825515; -.
DR Gramene; AT3G63400.1; AT3G63400.1; AT3G63400. [Q9LY75-1]
DR Gramene; AT3G63400.2; AT3G63400.2; AT3G63400. [Q9LY75-3]
DR Gramene; AT3G63400.3; AT3G63400.3; AT3G63400. [Q9LY75-1]
DR Gramene; AT3G63400.4; AT3G63400.4; AT3G63400. [Q9LY75-1]
DR KEGG; ath:AT3G63400; -.
DR Araport; AT3G63400; -.
DR TAIR; locus:2087383; AT3G63400.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_33_5_1; -.
DR InParanoid; Q9LY75; -.
DR OMA; ERDHSQT; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9LY75; -.
DR PRO; PR:Q9LY75; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LY75; baseline and differential.
DR Genevisible; Q9LY75; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
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:0008380; P:RNA splicing; NAS:TAIR.
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 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 Alternative splicing; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..570
FT /note="Peptidyl-prolyl cis-trans isomerase CYP63"
FT /id="PRO_0000429608"
FT DOMAIN 10..174
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 180..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..487
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 312..494
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055002"
FT VAR_SEQ 554..570
FT /note="SHSPSPPGKRGLVSYAD -> FSLTFSTRKERSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15051864"
FT /id="VSP_055003"
FT CONFLICT 299
FT /note="N -> D (in Ref. 5; BAH57223)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="K -> E (in Ref. 5; BAH57223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 63540 MW; 1137880ED360102B CRC64;
MTKKKNPNVF LDVSIGGDPV QRIVIELFAD VVPKTAENFR ALCTGEAGVG KSTGKPLHFK
GSSFHRVIKG FMAQGGDFSN GNGTGGESIY GGKFSDENFR LDHDGAGVLS MANCGPNTNG
SQFFILFKRQ PHLDGKHVVF GKVVEGMAVI KKMELVGTSD GKPTSPVKII DCGETSQIRA
HDAAEREKGK SKKSNKNFSP GDVSDREAKE TRKKESNEKR IKRKRRYSSS DSYSSSSDSD
SDSESEAYSS SSYESSSSSD GKHRKRKSTT RHKGRRGERK SKGRSGKKKA RPDRKPSTNS
SSDTESSSSS DDEKVGHKAI KSVKVDNADQ HANLDDSVKS RSRSPIRRRN QNSRSKSPSR
SPVRVLGNGN RSPSRSPVRD LGNGSRSPRE KPTEETVGKS FRSPSPSGVP KRIRKGRGFT
ERYSFARKYH TPSPERSPPR HWPDRRNFQD RNRDRYPSNR SYSERSPRGR FRSPPRRRSP
PRYNRRRRST SRSPDGYRRR LRDGSRSQSP RHRSRSQSPR KRQPISQDLK SRLGPQRSPI
RGGRTSPAES LSPSHSPSPP GKRGLVSYAD
