CP19D_ARATH
ID CP19D_ARATH Reviewed; 201 AA.
AC Q8LDP4; A8MS66; O22515; O80876;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP19-4;
DE Short=PPIase CYP19-4;
DE EC=5.2.1.8 {ECO:0000305|PubMed:10715321};
DE AltName: Full=Cyclophilin of 19 kDa 4;
DE AltName: Full=Cyclophilin-5 {ECO:0000303|PubMed:10715321};
DE AltName: Full=Rotamase CYP19-4;
DE Flags: Precursor;
GN Name=CYP19-4; Synonyms=CYP5 {ECO:0000303|PubMed:10715321};
GN OrderedLocusNames=At2g29960; ORFNames=F23F1.12;
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 [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10189705; DOI=10.1093/oxfordjournals.pcp.a029477;
RA Saito T., Niwa Y., Ashida H., Tanaka K., Kawamukai M., Matsuda H.,
RA Nakagawa T.;
RT "Expression of a gene for cyclophilin which contains an amino-terminal
RT endoplasmic reticulum-targeting signal.";
RL Plant Cell Physiol. 40:77-87(1999).
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 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH EMB30/GNOM.
RX PubMed=10715321; DOI=10.2307/3870940;
RA Grebe M., Gadea J., Steinmann T., Kientz M., Rahfeld J.-U., Salchert K.,
RA Koncz C., Juergens G.;
RT "A conserved domain of the Arabidopsis GNOM protein mediates subunit
RT interaction and cyclophilin 5 binding.";
RL Plant Cell 12:343-356(2000).
RN [7]
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 [8]
RP 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. May be involved during embryogenesis and organ
CC development by regulating the folding of EMB30/GNOM, and thus, by
CC modulating its activity. {ECO:0000269|PubMed:10715321}.
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 Evidence={ECO:0000305|PubMed:10715321};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC {ECO:0000269|PubMed:10715321}.
CC -!- SUBUNIT: Interacts with EMB30/GNOM. {ECO:0000269|PubMed:10715321}.
CC -!- INTERACTION:
CC Q8LDP4; Q42510: GN; NbExp=6; IntAct=EBI-2320844, EBI-1998836;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10715321}. Membrane
CC {ECO:0000269|PubMed:10715321}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:10189705}. Secreted {ECO:0000269|PubMed:10189705}.
CC Note=Mostly cytoplasmic, also membrane-associated (PubMed:10715321).
CC Present in endoplasmic reticulum and barely secreted (PubMed:10189705).
CC {ECO:0000269|PubMed:10189705, ECO:0000269|PubMed:10715321}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LDP4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LDP4-2; Sequence=VSP_055386;
CC -!- TISSUE SPECIFICITY: Ubiquitous, mostly in aerial organs (at protein
CC level). {ECO:0000269|PubMed:10189705, ECO:0000269|PubMed:10715321,
CC ECO:0000269|PubMed:15047905}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in both apical and basal regions
CC in peduncles and stems (including upper roots) before the bolting
CC stage. Later restricted in the apical region. During embryogenesis,
CC accumulates in all cells during globular stage. From the heart stage,
CC more expressed in inner cells than in epidermal cells (at protein
CC level). {ECO:0000269|PubMed:10189705, ECO:0000269|PubMed:10715321}.
CC -!- INDUCTION: Up-regulated by cold, salt and cytokinin treatment.
CC {ECO:0000269|PubMed:10189705, ECO:0000269|PubMed:15047905}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF020433; AAB71401.1; -; Genomic_DNA.
DR EMBL; AC004680; AAC31856.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08327.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08328.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62829.1; -; Genomic_DNA.
DR EMBL; AY054593; AAK96784.1; -; mRNA.
DR EMBL; BT000068; AAN15387.1; -; mRNA.
DR EMBL; AY085875; AAM63088.1; -; mRNA.
DR PIR; T02489; T02489.
DR PIR; T50837; T50837.
DR RefSeq; NP_001077978.1; NM_001084509.1. [Q8LDP4-2]
DR RefSeq; NP_001318316.1; NM_001336236.1. [Q8LDP4-1]
DR RefSeq; NP_180557.1; NM_128550.4. [Q8LDP4-1]
DR AlphaFoldDB; Q8LDP4; -.
DR SMR; Q8LDP4; -.
DR BioGRID; 2896; 1.
DR IntAct; Q8LDP4; 1.
DR STRING; 3702.AT2G29960.1; -.
DR PaxDb; Q8LDP4; -.
DR PRIDE; Q8LDP4; -.
DR ProMEX; Q8LDP4; -.
DR ProteomicsDB; 240832; -. [Q8LDP4-1]
DR EnsemblPlants; AT2G29960.1; AT2G29960.1; AT2G29960. [Q8LDP4-1]
DR EnsemblPlants; AT2G29960.2; AT2G29960.2; AT2G29960. [Q8LDP4-2]
DR EnsemblPlants; AT2G29960.3; AT2G29960.3; AT2G29960. [Q8LDP4-1]
DR GeneID; 817546; -.
DR Gramene; AT2G29960.1; AT2G29960.1; AT2G29960. [Q8LDP4-1]
DR Gramene; AT2G29960.2; AT2G29960.2; AT2G29960. [Q8LDP4-2]
DR Gramene; AT2G29960.3; AT2G29960.3; AT2G29960. [Q8LDP4-1]
DR KEGG; ath:AT2G29960; -.
DR Araport; AT2G29960; -.
DR TAIR; locus:2045663; AT2G29960.
DR eggNOG; KOG0865; Eukaryota.
DR HOGENOM; CLU_012062_4_2_1; -.
DR InParanoid; Q8LDP4; -.
DR OMA; CSIINSG; -.
DR OrthoDB; 1403619at2759; -.
DR PhylomeDB; Q8LDP4; -.
DR PRO; PR:Q8LDP4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LDP4; baseline and differential.
DR Genevisible; Q8LDP4; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005771; C:multivesicular body; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:TAIR.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0061083; P:regulation of protein refolding; IDA:UniProtKB.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
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; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Endoplasmic reticulum;
KW Isomerase; Membrane; Reference proteome; Rotamase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..201
FT /note="Peptidyl-prolyl cis-trans isomerase CYP19-4"
FT /id="PRO_0000044626"
FT DOMAIN 35..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT VAR_SEQ 131..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055386"
FT CONFLICT 30
FT /note="V -> I (in Ref. 1; AAB71401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 21534 MW; FBE07EB9EC546109 CRC64;
MAKASFILLG TLFLFGAIAS IQAKEDLKEV THKVYFDVEI DGKSAGRVVI GLFGKAVPKT
AENFRALCTG EKGVGKSGKP LHYKGSKFHR IIPSFMIQGG DFTHGNGMGG ESIYGQKFAD
ENFKLKHTGP GVLSMANSGE DTNGSQFFIT TVTTSWLDGR HVVFGKVVQG MDVVYKIEAE
GKQSGTPKSK VVIADSGELP L
