CYP95_ARATH
ID CYP95_ARATH Reviewed; 837 AA.
AC Q8RWY7; B3H620; F4JUB0; F4JUB1; Q9SUV0;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP95;
DE Short=AtCYP95;
DE Short=PPIase CYP95;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin-like protein CypRS92;
GN Name=CYP95; Synonyms=CYPRS92; OrderedLocusNames=At4g32420;
GN ORFNames=F8B4.120;
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).
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 INTERACTION WITH SCL28; SCL30; SR34; RNU1 AND SNRNP35.
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 [6]
RP GENE FAMILY, AND NOMENCLATURE.
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).
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). {ECO:0000250}.
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 SCL28, SCL30, SR34, RNU1 and SNRNP35.
CC {ECO:0000269|PubMed:15166240}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8RWY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWY7-2; Sequence=VSP_055204;
CC Name=3;
CC IsoId=Q8RWY7-3; Sequence=VSP_055205;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, roots and stems.
CC {ECO:0000269|PubMed:15051864}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA22569.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79959.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY091023; AAM13845.1; -; mRNA.
DR EMBL; AL034567; CAA22569.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161581; CAB79959.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86054.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86055.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86056.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86057.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67682.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67683.1; -; Genomic_DNA.
DR EMBL; AY568529; AAS75312.1; -; mRNA.
DR PIR; T05352; T05352.
DR RefSeq; NP_001119097.1; NM_001125625.2. [Q8RWY7-2]
DR RefSeq; NP_001190888.1; NM_001203959.1. [Q8RWY7-3]
DR RefSeq; NP_001190889.1; NM_001203960.2. [Q8RWY7-1]
DR RefSeq; NP_001329498.1; NM_001342150.1. [Q8RWY7-1]
DR RefSeq; NP_001329499.1; NM_001342149.1. [Q8RWY7-1]
DR RefSeq; NP_194968.2; NM_119394.4. [Q8RWY7-1]
DR AlphaFoldDB; Q8RWY7; -.
DR SMR; Q8RWY7; -.
DR BioGRID; 14663; 5.
DR IntAct; Q8RWY7; 4.
DR STRING; 3702.AT4G32420.3; -.
DR iPTMnet; Q8RWY7; -.
DR PaxDb; Q8RWY7; -.
DR PRIDE; Q8RWY7; -.
DR ProteomicsDB; 222773; -. [Q8RWY7-1]
DR EnsemblPlants; AT4G32420.1; AT4G32420.1; AT4G32420. [Q8RWY7-1]
DR EnsemblPlants; AT4G32420.2; AT4G32420.2; AT4G32420. [Q8RWY7-2]
DR EnsemblPlants; AT4G32420.3; AT4G32420.3; AT4G32420. [Q8RWY7-1]
DR EnsemblPlants; AT4G32420.4; AT4G32420.4; AT4G32420. [Q8RWY7-3]
DR EnsemblPlants; AT4G32420.5; AT4G32420.5; AT4G32420. [Q8RWY7-1]
DR EnsemblPlants; AT4G32420.6; AT4G32420.6; AT4G32420. [Q8RWY7-1]
DR GeneID; 829377; -.
DR Gramene; AT4G32420.1; AT4G32420.1; AT4G32420. [Q8RWY7-1]
DR Gramene; AT4G32420.2; AT4G32420.2; AT4G32420. [Q8RWY7-2]
DR Gramene; AT4G32420.3; AT4G32420.3; AT4G32420. [Q8RWY7-1]
DR Gramene; AT4G32420.4; AT4G32420.4; AT4G32420. [Q8RWY7-3]
DR Gramene; AT4G32420.5; AT4G32420.5; AT4G32420. [Q8RWY7-1]
DR Gramene; AT4G32420.6; AT4G32420.6; AT4G32420. [Q8RWY7-1]
DR KEGG; ath:AT4G32420; -.
DR Araport; AT4G32420; -.
DR TAIR; locus:2127786; AT4G32420.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_33_5_1; -.
DR OMA; YDHYERS; -.
DR PRO; PR:Q8RWY7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RWY7; baseline and differential.
DR Genevisible; Q8RWY7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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 Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; Nucleus; Reference proteome; Rotamase.
FT CHAIN 1..837
FT /note="Peptidyl-prolyl cis-trans isomerase CYP95"
FT /id="PRO_0000429769"
FT DOMAIN 10..174
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 176..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..204
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..600
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..651
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..740
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055204"
FT VAR_SEQ 161..177
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055205"
FT CONFLICT 54
FT /note="G -> R (in Ref. 1; AAM13845 and 4; AAS75312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 94630 MW; 1E2ADDB203DE6B4C CRC64;
MAKKKNPQVF MDVSIDGDPA ETMVFELFPE VAPKTSENFR ALCTGEKGIG PRSGKPLHYK
GSFFHRIMKG SSAQAGDFVN RNGTAGESIY AGKFPDESPK LRHEETGLLS MSIADRDKFG
SHFHITFRPN QQLDRNNVVF GKLIQGKEIL KKIERVGDEE GKPTVSVKII RCGEYSGDKK
KSDGKKNGKH KKSLRVRRKK RRRHSSSESE SSSDSETDSS ESDSESDSDL SSPSFLSSSS
HERQKKRKRS SKKDKHRRSK QRDKRHEKKR SMRDKRPKRK SRRSPDSLED SNSGSEASLS
DVNVEIGAKK RKHRVSRRTG NSAPAVEKEA ESLHQGKRKG PDLLENRGLR SNGISDAASE
QISDRQPDIV DDHPSKSRSR SLSPKRTVSK STSVSPRRSQ SKSPSSSPRW NGGRSPAKGS
RQVKNLTNSR RESPGSEEKG RHVRRSPTKS VSRSPVRVKK ERDISRSPSK SLSRSPLRSP
KRVISRSPVR GRIARSPSRS PVRSASRGSL GRGPLRRSSR RSPSRSPVRS SRRSLSRSPI
QLSRRSLSRS PTRLSRRSLS RSPIRSPRKS VSRSPVRSSR KSVSRSPVRS SRRRISRSPV
RSSRKSVSRS PIRLSRRSIS RSPIRLSRRS ISRSPVRGRR RISRSPVPAR RRSVRPRSPP
PDRRRSLSRS ASPNGRIRRG RGFSQRFSYA RRYRTSPSPD RSPYRFSDRS DRDRFRSRRR
FSPSRFRSPL RGRTPPRYRR RSRSVSPGLC YRNRRYSRSP IRSRSPPYRK RRSPSASHSL
SPSRSRSRSK SYSKSPIGTG KARSVSRSPS KARSPSKSDS TSSDNSPGGK KGLVAYD
