CYP22_ARATH
ID CYP22_ARATH Reviewed; 199 AA.
AC Q9ZVJ4;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP22;
DE Short=PPIase CYP22;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 22 kDa;
DE AltName: Full=Cyclophilin-22;
GN Name=CYP22; Synonyms=CYP22-1; OrderedLocusNames=At2g38730;
GN ORFNames=T6A23.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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].
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 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 -!- 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; AY568522; AAS75305.1; -; mRNA.
DR EMBL; AC005499; AAC67345.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09578.1; -; Genomic_DNA.
DR EMBL; BT002031; AAN72042.1; -; mRNA.
DR EMBL; BT006565; AAP21373.1; -; mRNA.
DR PIR; F84808; F84808.
DR RefSeq; NP_181407.1; NM_129430.4.
DR AlphaFoldDB; Q9ZVJ4; -.
DR SMR; Q9ZVJ4; -.
DR BioGRID; 3797; 5.
DR IntAct; Q9ZVJ4; 1.
DR STRING; 3702.AT2G38730.1; -.
DR PaxDb; Q9ZVJ4; -.
DR PRIDE; Q9ZVJ4; -.
DR ProteomicsDB; 224657; -.
DR EnsemblPlants; AT2G38730.1; AT2G38730.1; AT2G38730.
DR GeneID; 818455; -.
DR Gramene; AT2G38730.1; AT2G38730.1; AT2G38730.
DR KEGG; ath:AT2G38730; -.
DR Araport; AT2G38730; -.
DR TAIR; locus:2064153; AT2G38730.
DR eggNOG; KOG0879; Eukaryota.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; Q9ZVJ4; -.
DR OMA; RHPNNPV; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q9ZVJ4; -.
DR PRO; PR:Q9ZVJ4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVJ4; baseline and differential.
DR Genevisible; Q9ZVJ4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 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; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..199
FT /note="Peptidyl-prolyl cis-trans isomerase CYP22"
FT /id="PRO_0000429937"
FT DOMAIN 35..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 199 AA; 21492 MW; FCC6DAB546C68C8C CRC64;
MNSGGGIVAA AAPSSGGGNV EWHVRPPNPK NPVVFFDVSI GGIPAGRIKM ELFADIAPKT
AENFRQFCTG ELRKAGKPLG YKECQFHRVI KDFMVQSGDF LKNDGSGCMS IYGHKFEDEN
FTAKHTGPGL LSMANSGPNT NGCQFFITCA KCDWLDNKHV VFGRVLGDGL LVMRKIENVA
IGPNNRPKLA VVITECGEM
