CYP37_ARATH
ID CYP37_ARATH Reviewed; 466 AA.
AC P82869; Q1JPN6; Q9LDZ3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase CYP37, chloroplastic;
DE Short=PPIase CYP37;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase CYP37;
DE AltName: Full=Thylakoid lumen PPIase of 38 kDa;
DE Short=TLP38;
DE Short=p38;
DE Flags: Precursor;
GN Name=CYP37; OrderedLocusNames=At3g15520; ORFNames=MJK13.18;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 115-138, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [6]
RP INDUCTION, 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 TISSUE SPECIFICITY, 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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
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: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Aerial parts. {ECO:0000269|PubMed:15051864}.
CC -!- INDUCTION: Up-regulated by light. Down-regulated by dark.
CC {ECO:0000269|PubMed:15047905}.
CC -!- CAUTION: Both gene predictions and some EST data suggest that there may
CC be an additional exon at the C-terminus, adding another 10 kDa to the
CC protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB02381.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022218; BAB02381.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024081; AAF35418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75686.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64682.1; -; Genomic_DNA.
DR EMBL; BT025317; ABF57273.1; -; mRNA.
DR RefSeq; NP_001326694.1; NM_001338175.1.
DR RefSeq; NP_188171.2; NM_112420.5.
DR AlphaFoldDB; P82869; -.
DR SMR; P82869; -.
DR BioGRID; 6125; 1.
DR STRING; 3702.AT3G15520.1; -.
DR PaxDb; P82869; -.
DR PRIDE; P82869; -.
DR EnsemblPlants; AT3G15520.1; AT3G15520.1; AT3G15520.
DR EnsemblPlants; AT3G15520.3; AT3G15520.3; AT3G15520.
DR GeneID; 820791; -.
DR Gramene; AT3G15520.1; AT3G15520.1; AT3G15520.
DR Gramene; AT3G15520.3; AT3G15520.3; AT3G15520.
DR KEGG; ath:AT3G15520; -.
DR Araport; AT3G15520; -.
DR TAIR; locus:2090101; AT3G15520.
DR eggNOG; ENOG502QRM6; Eukaryota.
DR HOGENOM; CLU_012062_19_0_1; -.
DR InParanoid; P82869; -.
DR OrthoDB; 1419161at2759; -.
DR PhylomeDB; P82869; -.
DR PRO; PR:P82869; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P82869; baseline and differential.
DR Genevisible; P82869; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0031977; C:thylakoid lumen; 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; 1.20.120.290; -; 1.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044259; CYP37-like.
DR InterPro; IPR023222; PsbQ-like_dom_sf.
DR PANTHER; PTHR47318; PTHR47318; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Isomerase; Plastid;
KW Reference proteome; Rotamase; Thylakoid; Transit peptide.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT 66..114
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 115..466
FT /note="Peptidyl-prolyl cis-trans isomerase CYP37,
FT chloroplastic"
FT /id="PRO_0000025504"
FT DOMAIN 278..466
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 466 AA; 50483 MW; F160CC1CF95D89E5 CRC64;
MASPLSSSTV VSHRLFFLHP SPLNRKFLFV KPKLPFNRTN SGDFRMRLHS TSSKTGTKEL
IHSCNSSIDS KLNTFEAGSK NLEKLVATIL IFVQVWSPLP LFGLDSAYIS PAEAVLYSPD
TKVPRTGELA LRRAIPANPS MKIIQASLED ISYLLRIPQR KPYGTMESNV KKALKVAIDD
KDKILASIPV DLKDKGSELY TTLIDGKGGL QALITSIKKQ DPDKVSLGLA ASLDTVADLE
LLQASGLSFL LPQQYLNYPR LAGRGTVEIT IEKADGSTFS AEAGGDQRKS ATVQIVIDGY
SAPLTAGNFA KLVTSGAYDG AKLNTVNQAV ITEDGSGKVE SVSVPLEVMP SGQFEPLYRT
PLSVQDGELP VLPLSVYGAV AMAHSENSEE YSSPYQFFFY LYDKRNSGLG GLSFDEGQFS
VFGYTIAGKD ILGQIKTGDI IKSAKLIEGQ DRLSLPVQNN NINEST
