PPIL2_ARATH
ID PPIL2_ARATH Reviewed; 595 AA.
AC Q9FJX0; Q8W4J7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP65 {ECO:0000305};
DE Short=AtCYP65;
DE Short=PPIase CYP65;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13356};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:Q08752};
DE AltName: Full=Cyclophilin-65;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase-like 2;
DE AltName: Full=Plant U-box protein 49;
DE AltName: Full=RING-type E3 ubiquitin transferase isomerase-like 2 {ECO:0000305};
DE AltName: Full=Rotamase;
DE AltName: Full=U-box domain-containing protein 49;
GN Name=CYP65; Synonyms=PUB49; OrderedLocusNames=At5g67530; ORFNames=K9I9.9;
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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].
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 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).
CC -!- FUNCTION: May catalyze the cis-trans isomerization of proline imidic
CC peptide bonds in oligopeptides thereby assisting the folding of
CC proteins. May also function as a chaperone, playing a role in
CC intracellular transport of proteins. May also have a protein ubiquitin
CC ligase activity acting as an E3 ubiquitin protein ligase or as a
CC ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on
CC proteins. {ECO:0000250|UniProtKB:Q08752, ECO:0000250|UniProtKB:Q13356}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q13356};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13356}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09928,
CC ECO:0000250|UniProtKB:Q13356}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flower buds and stems. Lower
CC levels of expression in roots. {ECO:0000269|PubMed:15051864}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL2
CC subfamily. {ECO:0000305}.
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DR EMBL; AY568528; AAS75311.1; -; mRNA.
DR EMBL; AB013390; BAB08461.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98356.1; -; Genomic_DNA.
DR EMBL; AY062106; AAL32981.1; -; mRNA.
DR EMBL; AY062516; AAL32594.1; -; mRNA.
DR EMBL; AY093296; AAM13295.1; -; mRNA.
DR EMBL; BT001006; AAN46760.1; -; mRNA.
DR RefSeq; NP_201554.1; NM_126153.4.
DR AlphaFoldDB; Q9FJX0; -.
DR SMR; Q9FJX0; -.
DR BioGRID; 22131; 3.
DR IntAct; Q9FJX0; 3.
DR STRING; 3702.AT5G67530.1; -.
DR iPTMnet; Q9FJX0; -.
DR PaxDb; Q9FJX0; -.
DR PRIDE; Q9FJX0; -.
DR ProteomicsDB; 248733; -.
DR EnsemblPlants; AT5G67530.1; AT5G67530.1; AT5G67530.
DR GeneID; 836889; -.
DR Gramene; AT5G67530.1; AT5G67530.1; AT5G67530.
DR KEGG; ath:AT5G67530; -.
DR Araport; AT5G67530; -.
DR TAIR; locus:2158636; AT5G67530.
DR eggNOG; KOG0883; Eukaryota.
DR HOGENOM; CLU_012062_7_0_1; -.
DR InParanoid; Q9FJX0; -.
DR OMA; NFIKHCA; -.
DR OrthoDB; 1392223at2759; -.
DR PhylomeDB; Q9FJX0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FJX0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJX0; baseline and differential.
DR Genevisible; Q9FJX0; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd16663; RING-Ubox_PPIL2; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR026951; PPIL2_U-box_dom.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Isomerase; Nucleus; Reference proteome; Rotamase; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..595
FT /note="Peptidyl-prolyl cis-trans isomerase CYP65"
FT /id="PRO_0000322147"
FT DOMAIN 35..108
FT /note="U-box"
FT DOMAIN 342..496
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 503..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 77
FT /note="P -> H (in Ref. 4; AAL32594/AAM13295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 65023 MW; A3521795707F1796 CRC64;
MGKKQHSKDR MFITKTEWAT EWGGAKSKEN RTPFKSLPYY CCALTFLPFE DPVCTIDGSV
FEITTIVPYI RKFGKHPVTG APLKGEDLIP LIFHKNSEGE YHCPVLNKVF TEFTHIVAVK
TTGNVFCYEA IKELNIKTKN WKELLTEEPF TRADLITIQN PNAVDGKVTV EFDHVKNGLK
IDDEELKKMN SDPAYNINVS GDIKHMLADL GTDKAKEIAL HGGGGNKARN ERAAAIAAIL
ESRSKIKEVS KAEQPKQTYS VVDAASASVF GRSADAAKAG SSDKTAARIA MHMAGDRTPV
NSKMVKSRYS SGAASRSFTS SAFTPVTKND FELIKVEKNP KKKGYVQFQT THGDLNIELH
CDIAPRACEN FITLCERGYY NGVAFHRSIR NFMIQGGDPT GTGKGGESIW GKPFKDEPNS
KLLHSGRGVV SMANSGPHTN GSQFFVLYKS ATHLNYKHTV FGGVVGGLAT LAAMENVPVD
ESDRPLEEIK IIEASVFVNP YTELDEEEEK EKAEKEKNED KDIEKIGSWY SNPGSGTTEA
GAGGGGVGKY LKAMSSTATK DTKGSLDSDI STIGVSKKRK TTASASTGFK DFSSW
