CP21D_ARATH
ID CP21D_ARATH Reviewed; 236 AA.
AC Q9C835;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP21-4;
DE Short=PPIase CYP21-4;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin of 21 kDa 4;
DE AltName: Full=Cyclophilin-21-4;
GN Name=CYP21-4; OrderedLocusNames=At3g66654; ORFNames=T8E24.14;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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).
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 type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15047905,
CC ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Down-regulated by dark treatment.
CC {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; AY568521; AAS75304.1; -; mRNA.
DR EMBL; AC036106; AAG50994.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74429.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74430.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74431.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64487.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64488.1; -; Genomic_DNA.
DR EMBL; BT005430; AAO63850.1; -; mRNA.
DR EMBL; AK117708; BAC42359.1; -; mRNA.
DR RefSeq; NP_001326512.1; NM_001340222.1.
DR RefSeq; NP_001326513.1; NM_001340221.1.
DR RefSeq; NP_187319.1; NM_111543.4.
DR RefSeq; NP_974240.1; NM_202511.1.
DR RefSeq; NP_974241.1; NM_202512.2.
DR AlphaFoldDB; Q9C835; -.
DR SMR; Q9C835; -.
DR BioGRID; 5182; 382.
DR IntAct; Q9C835; 383.
DR STRING; 3702.AT3G66654.3; -.
DR SwissPalm; Q9C835; -.
DR PaxDb; Q9C835; -.
DR PRIDE; Q9C835; -.
DR ProteomicsDB; 224401; -.
DR EnsemblPlants; AT3G66654.1; AT3G66654.1; AT3G66654.
DR EnsemblPlants; AT3G66654.2; AT3G66654.2; AT3G66654.
DR EnsemblPlants; AT3G66654.3; AT3G66654.3; AT3G66654.
DR EnsemblPlants; AT3G66654.4; AT3G66654.4; AT3G66654.
DR EnsemblPlants; AT3G66654.5; AT3G66654.5; AT3G66654.
DR GeneID; 819847; -.
DR Gramene; AT3G66654.1; AT3G66654.1; AT3G66654.
DR Gramene; AT3G66654.2; AT3G66654.2; AT3G66654.
DR Gramene; AT3G66654.3; AT3G66654.3; AT3G66654.
DR Gramene; AT3G66654.4; AT3G66654.4; AT3G66654.
DR Gramene; AT3G66654.5; AT3G66654.5; AT3G66654.
DR KEGG; ath:AT3G66654; -.
DR Araport; AT3G66654; -.
DR TAIR; locus:2103420; AT3G66654.
DR eggNOG; KOG0882; Eukaryota.
DR HOGENOM; CLU_012062_16_1_1; -.
DR InParanoid; Q9C835; -.
DR OMA; QVIKHYV; -.
DR OrthoDB; 1291177at2759; -.
DR PhylomeDB; Q9C835; -.
DR PRO; PR:Q9C835; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9C835; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; 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 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 Signal-anchor; Transit peptide; Transmembrane; Transmembrane helix.
FT CHAIN 1..236
FT /note="Peptidyl-prolyl cis-trans isomerase CYP21-4"
FT /id="PRO_0000429936"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 82..232
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 236 AA; 26427 MW; 32B213485EEE5BF6 CRC64;
MAKIKPQALL NQSKKKKGPS RISISTIIVC NLVVAVVILS LVTTYRHWSQ RSRNTIEHET
RSQRFEDTNT ASGQKTYDLP GFADINTSKG LITVELFKEG SPEVVDKFLD LCQKDHFKGM
PFQRVIKNYL VQAGHSPSSI PVEEWTAKGK LRGRLHIGPK HEAFMLGTPK NKGNNKDFEL
LITTAPIPDL NDQLIVFGRV LKGEDVVQEI EEVDTDEHFQ PKSPIGITGV VLKLET
