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Protein

Peptidyl-prolyl cis-trans isomerase CYP19-3

Gene

CYP19-3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase (By similarity).By similarity

GO - Molecular functioni

  • cyclosporin A binding Source: TAIR
  • peptidyl-prolyl cis-trans isomerase activity Source: TAIR

GO - Biological processi

  • protein folding Source: InterPro
  • response to cadmium ion Source: TAIR
  • signal transduction Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

BioCyciARA:AT3G56070-MONOMER.
ARA:GQT-1558-MONOMER.
ReactomeiR-ATH-6781823. Formation of TC-NER Pre-Incision Complex.
R-ATH-6782135. Dual incision in TC-NER.
R-ATH-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase CYP19-3 (EC:5.2.1.8)
Short name:
PPIase CYP19-3
Alternative name(s):
Cyclophilin of 19 kDa 3
Cyclophilin-4
Rotamase cyclophilin-2
Gene namesi
Name:CYP19-3
Synonyms:CYP4, ROC2
Ordered Locus Names:At3g56070
ORF Names:F18O21.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G56070.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • Golgi apparatus Source: TAIR
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 176176Peptidyl-prolyl cis-trans isomerase CYP19-3PRO_0000064137Add
BLAST

Proteomic databases

PaxDbiQ38867.
PRIDEiQ38867.

PTM databases

SwissPalmiQ38867.

Expressioni

Tissue specificityi

Ubiquitous, with highest levels in flowers and lowest levels in roots.2 Publications

Inductioni

By wounding, and slightly by light.1 Publication

Gene expression databases

GenevisibleiQ38867. AT.

Interactioni

Protein-protein interaction databases

IntActiQ38867. 4 interactions.
STRINGi3702.AT3G56070.1.

Structurei

3D structure databases

ProteinModelPortaliQ38867.
SMRiQ38867. Positions 3-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 170164PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the cyclophilin-type PPIase family.Curated
Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000065981.
InParanoidiQ38867.
KOiK01802.
OMAiAGKALHY.
PhylomeDBiQ38867.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q38867-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANPKVFFDI LIGKMKAGRV VMELFADVTP RTANNFRALC TGENGIGKAG
60 70 80 90 100
KALHYKGSAF HRIIPGFMCQ GGDFTRGNGT GGESIYGSKF EDENFKLKHT
110 120 130 140 150
GPGILSMANS GPNTNGSQFF ICTEKTSWLD GKHVVFGKVV DGYNVVKAME
160 170
DVGSDMGNPS ERVVIEDCGE LKNPSS
Length:176
Mass (Da):18,921
Last modified:December 20, 2005 - v2
Checksum:i24C2031B6CB4DD90
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551D → Y in AAA74096 (Ref. 2) Curated
Sequence conflicti172 – 1721K → N in AAB96833 (PubMed:9426607).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40400 Genomic DNA. Translation: AAB96833.1.
U31370 Genomic DNA. Translation: AAA74096.1.
AL163763 Genomic DNA. Translation: CAB87406.1.
CP002686 Genomic DNA. Translation: AEE79473.1.
CP002686 Genomic DNA. Translation: AEE79474.1.
AY072128 mRNA. Translation: AAL59950.1.
AY096697 mRNA. Translation: AAM20331.1.
PIRiT47724.
T50767.
RefSeqiNP_001078301.1. NM_001084832.1.
NP_191166.1. NM_115465.4.
UniGeneiAt.34965.

Genome annotation databases

EnsemblPlantsiAT3G56070.1; AT3G56070.1; AT3G56070.
AT3G56070.2; AT3G56070.2; AT3G56070.
GeneIDi824773.
GrameneiAT3G56070.1; AT3G56070.1; AT3G56070.
AT3G56070.2; AT3G56070.2; AT3G56070.
KEGGiath:AT3G56070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U40400 Genomic DNA. Translation: AAB96833.1.
U31370 Genomic DNA. Translation: AAA74096.1.
AL163763 Genomic DNA. Translation: CAB87406.1.
CP002686 Genomic DNA. Translation: AEE79473.1.
CP002686 Genomic DNA. Translation: AEE79474.1.
AY072128 mRNA. Translation: AAL59950.1.
AY096697 mRNA. Translation: AAM20331.1.
PIRiT47724.
T50767.
RefSeqiNP_001078301.1. NM_001084832.1.
NP_191166.1. NM_115465.4.
UniGeneiAt.34965.

3D structure databases

ProteinModelPortaliQ38867.
SMRiQ38867. Positions 3-171.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ38867. 4 interactions.
STRINGi3702.AT3G56070.1.

PTM databases

SwissPalmiQ38867.

Proteomic databases

PaxDbiQ38867.
PRIDEiQ38867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G56070.1; AT3G56070.1; AT3G56070.
AT3G56070.2; AT3G56070.2; AT3G56070.
GeneIDi824773.
GrameneiAT3G56070.1; AT3G56070.1; AT3G56070.
AT3G56070.2; AT3G56070.2; AT3G56070.
KEGGiath:AT3G56070.

Organism-specific databases

TAIRiAT3G56070.

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
HOGENOMiHOG000065981.
InParanoidiQ38867.
KOiK01802.
OMAiAGKALHY.
PhylomeDBiQ38867.

Enzyme and pathway databases

BioCyciARA:AT3G56070-MONOMER.
ARA:GQT-1558-MONOMER.
ReactomeiR-ATH-6781823. Formation of TC-NER Pre-Incision Complex.
R-ATH-6782135. Dual incision in TC-NER.
R-ATH-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

PROiQ38867.

Gene expression databases

GenevisibleiQ38867. AT.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the cyclophilin gene family of Arabidopsis thaliana and phylogenetic analysis of known cyclophilin proteins."
    Chou I.T., Gasser C.S.
    Plant Mol. Biol. 35:873-892(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  2. Saito T., Ashida H., Kawamukai M., Matsuda H., Nakagawa T.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis."
    He Z., Li L., Luan S.
    Plant Physiol. 134:1248-1267(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE.
  7. Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiCP19C_ARATH
AccessioniPrimary (citable) accession number: Q38867
Secondary accession number(s): Q38901, Q9LYN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 17, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.