CP26B_ARATH
ID CP26B_ARATH Reviewed; 317 AA.
AC F4HTT6; Q8W4C6; Q9C9C7;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP26-2, chloroplastic;
DE Short=PPIase CYP26-2;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 26 kDa 2;
DE AltName: Full=Cyclophilin-26-2;
DE Flags: Precursor;
GN Name=CYP26-2; OrderedLocusNames=At1g74070; ORFNames=F2P9.6;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 10-317.
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).
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Lower levels of expression in roots.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Down-regulated by sucrose treatment.
CC {ECO:0000269|PubMed:15047905}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL32738.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC016662; AAG52521.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35545.1; -; Genomic_DNA.
DR EMBL; AY062660; AAL32738.1; ALT_INIT; mRNA.
DR EMBL; AY093323; AAM13322.1; -; mRNA.
DR PIR; F96768; F96768.
DR RefSeq; NP_001321038.1; NM_001334626.1.
DR RefSeq; NP_565079.1; NM_106067.3.
DR AlphaFoldDB; F4HTT6; -.
DR SMR; F4HTT6; -.
DR STRING; 3702.AT1G74070.1; -.
DR iPTMnet; F4HTT6; -.
DR PaxDb; F4HTT6; -.
DR PRIDE; F4HTT6; -.
DR ProteomicsDB; 224540; -.
DR EnsemblPlants; AT1G74070.1; AT1G74070.1; AT1G74070.
DR GeneID; 843747; -.
DR Gramene; AT1G74070.1; AT1G74070.1; AT1G74070.
DR KEGG; ath:AT1G74070; -.
DR Araport; AT1G74070; -.
DR TAIR; locus:2031546; AT1G74070.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_064825_0_0_1; -.
DR InParanoid; F4HTT6; -.
DR OrthoDB; 868053at2759; -.
DR PRO; PR:F4HTT6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HTT6; baseline and differential.
DR Genevisible; F4HTT6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044185; CYP26-2-like.
DR PANTHER; PTHR47724; PTHR47724; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; Isomerase; Plastid; Reference proteome; Rotamase;
KW Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..74
FT /note="Thylakoid"
FT CHAIN 75..317
FT /note="Peptidyl-prolyl cis-trans isomerase CYP26-2,
FT chloroplastic"
FT /id="PRO_0000429940"
FT DOMAIN 95..311
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34375 MW; 8C89FA22F0B739FE CRC64;
MMQPNAKLLS PSAKFLPSPI EPPQHNRRTT VGAPPSLERN CKLSRRNLSK SSLLLLLTTQ
TTLTPLLDFS KAQADTIANP NLTNCENRIP TKKAFIDVSI DGEPIGRIII GLYGDDVPAG
TARFSSIVSG KAGITYRRKD FVKIMPGYVQ HGGIRSYGVD AERATAAVGS LQNLIEEWER
GKRGEICNVN KAGSVGIVVR DPSKPPPKTK LVARNGKLVV EEEVIAVGPN GTEFVITAVD
SPELEDSVLV IGKVLEGMGV VEKMREVKTV RDNTSSPYFR VAKVIGDKRA VVAERGFNRP
YSKVVVTNCG LIESQTL
