CP21C_ARATH
ID CP21C_ARATH Reviewed; 230 AA.
AC Q94A16; C0Z333; O22906;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP21-3, mitochondrial;
DE Short=PPIase CYP21-3;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 21 kDa 3;
DE AltName: Full=Rotamase CYP21-3;
DE Flags: Precursor;
GN Name=CYP21-3; OrderedLocusNames=At2g47320; ORFNames=T8I13.16;
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=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] (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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
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).
RN [7]
RP INDUCTION.
RX PubMed=16173598; DOI=10.1021/es050385r;
RA Ekman D.R., Wolfe N.L., Dean J.F.D.;
RT "Gene expression changes in Arabidopsis thaliana seedling roots exposed to
RT the munition hexahydro-1,3,5-trinitro-1,3,5-triazine.";
RL Environ. Sci. Technol. 39:6313-6320(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides.
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 -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94A16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94A16-2; Sequence=VSP_055389;
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in aerial organs.
CC {ECO:0000269|PubMed:15047905, ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Repressed by the munition hexahydro-1,3,5-trinitro-1,3,5-
CC triazine, also known as Royal Demolition eXplosive (RDX).
CC {ECO:0000269|PubMed:16173598}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK91465.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK91465.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY568520; AAS75303.1; -; mRNA.
DR EMBL; AC002337; AAB63832.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10827.1; -; Genomic_DNA.
DR EMBL; AY050450; AAK91465.1; ALT_INIT; mRNA.
DR EMBL; AY097351; AAM19867.1; -; mRNA.
DR EMBL; AK318997; BAH57112.1; -; mRNA.
DR PIR; G84913; G84913.
DR RefSeq; NP_182254.1; NM_130300.4. [Q94A16-1]
DR AlphaFoldDB; Q94A16; -.
DR SMR; Q94A16; -.
DR STRING; 3702.AT2G47320.1; -.
DR iPTMnet; Q94A16; -.
DR PaxDb; Q94A16; -.
DR PRIDE; Q94A16; -.
DR ProteomicsDB; 224492; -. [Q94A16-1]
DR EnsemblPlants; AT2G47320.1; AT2G47320.1; AT2G47320. [Q94A16-1]
DR GeneID; 819345; -.
DR Gramene; AT2G47320.1; AT2G47320.1; AT2G47320. [Q94A16-1]
DR KEGG; ath:AT2G47320; -.
DR Araport; AT2G47320; -.
DR TAIR; locus:2065205; AT2G47320.
DR eggNOG; KOG0882; Eukaryota.
DR HOGENOM; CLU_012062_16_1_1; -.
DR InParanoid; Q94A16; -.
DR OMA; ITNIVIY; -.
DR OrthoDB; 1291177at2759; -.
DR PhylomeDB; Q94A16; -.
DR PRO; PR:Q94A16; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q94A16; baseline and differential.
DR Genevisible; Q94A16; AT.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0000137; C:Golgi cis cisterna; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 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 Alternative splicing; Chaperone; Isomerase; Mitochondrion;
KW Reference proteome; Rotamase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..230
FT /note="Peptidyl-prolyl cis-trans isomerase CYP21-3,
FT mitochondrial"
FT /id="PRO_0000044628"
FT DOMAIN 76..226
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_055389"
SQ SEQUENCE 230 AA; 26042 MW; 6198D43EE5B9552F CRC64;
MAKIKPQALL QQSKKKKGPS RISITNIVIY TLAVLLLVFV LFSAYRRWTH RSEIPTHNGR
SVLEDAAFPG MKNVDLPRFA TLDTGKGSVT IELFKDTAPN VVDQFMKFCQ DGYFKGFLFS
RVVKHFVIQA GDSAEFDAVK DWALDRKNID TSLKHEEFMV GTPKAKNEQG GFEFFIVSAQ
IKDLNEKLTV FGRVSKGQDV VQEIEEVETD DQYQPKSPIE IMSVTLLQDM
