ID   CP26A_ARATH             Reviewed;         232 AA.
AC   Q9LIK6;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP26-1;
DE            Short=PPIase CYP26-1;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin of 26 kDa 1;
DE   AltName: Full=Cyclophilin-26-1;
GN   Name=CYP26-1; OrderedLocusNames=At3g22920; ORFNames=F5N5;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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].
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY, 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: 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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed only in flowers.
CC       {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864}.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000305}.
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DR   EMBL; AY568523; AAS75306.1; -; mRNA.
DR   EMBL; AP001300; BAB03037.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76691.1; -; Genomic_DNA.
DR   EMBL; BT029019; ABI93928.1; -; mRNA.
DR   RefSeq; NP_188932.1; NM_113192.2.
DR   AlphaFoldDB; Q9LIK6; -.
DR   SMR; Q9LIK6; -.
DR   STRING; 3702.AT3G22920.1; -.
DR   PaxDb; Q9LIK6; -.
DR   PRIDE; Q9LIK6; -.
DR   ProteomicsDB; 220332; -.
DR   EnsemblPlants; AT3G22920.1; AT3G22920.1; AT3G22920.
DR   GeneID; 821864; -.
DR   Gramene; AT3G22920.1; AT3G22920.1; AT3G22920.
DR   KEGG; ath:AT3G22920; -.
DR   Araport; AT3G22920; -.
DR   TAIR; locus:2084588; AT3G22920.
DR   eggNOG; KOG0865; Eukaryota.
DR   HOGENOM; CLU_012062_4_3_1; -.
DR   InParanoid; Q9LIK6; -.
DR   OMA; HEDGPGI; -.
DR   OrthoDB; 1403619at2759; -.
DR   PhylomeDB; Q9LIK6; -.
DR   PRO; PR:Q9LIK6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIK6; baseline and differential.
DR   Genevisible; Q9LIK6; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Chaperone; Glycoprotein; Isomerase; Membrane; Reference proteome; Rotamase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..232
FT                   /note="Peptidyl-prolyl cis-trans isomerase CYP26-1"
FT                   /id="PRO_0000429939"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT   DOMAIN          7..166
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   232 AA;  26045 MW;  D2EF0126D263A302 CRC64;
     MANPKVFFDL TVDGKPAGRI VIELFADLTP RTAENFRGLC TGERGIGKCG KPIHYKGSTF
     DHIVPDLMWC GGDIIFENEP IHSEELDDEY FILNHEDGPG IISMADSNGS QFQIHMKDYG
     LQVDGDHVVI GKVVEGLDLM RNIEKEVITT TTRTPSKPVV IADCGELSDY RSERCYLMKN
     IEKEVIIKTA KDNKPVVIAD CGGLSDDRSE RYYLINIVVA CMVLMCFWSW FV