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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Arabidopsis thaliana and UniProt Accession P34790
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5.2.1.8 peptidylprolyl isomeraseIUBMB Comments
The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
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Word Map
- 5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
- calcineurin
- isomerases
- necrosis
- cardiac
- lymphocyte
- immunodeficiency
- capsid
-
ryanodine
- t-cells
- steroid
- glucocorticoid
- alzheimer
-
tetratricopeptide
- tacrolimus
-
refolding
- hsp70
- mtor
- interactor
- virion
- imperfecta
- gapdh
-
co-chaperone
-
genorm
- dnak
-
anti-hcv
- ptp
- groel
- legionella
-
osteogenesis
-
sarcoplasmic
- translocase
-
heterocomplexes
- pneumophila
-
voltage-dependent
-
phosphorylation-dependent
- ns5a
- analysis
-
ca2+-induced
-
direct-acting
- sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
- medicine
- ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
- agriculture
- pharmacology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclophilin, cyclophilin a, fkbp12, ppiase, fkbp51, trigger factor, fkbp52, fk506-binding protein, peptidyl-prolyl isomerase, cyclophilin b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
12 kDa FKBP
-
-
-
-
12.6 kDa FKBP
-
-
-
-
13 kDa FKBP
-
-
-
-
15 kDa FKBP
-
-
-
-
19 kDa FK506-binding protein
-
-
-
-
22 kDa FK506-binding protein
-
-
-
-
25 kDa FKBP
-
-
-
-
27 kDa membrane protein
-
-
-
-
36 kDa FK506 binding protein
-
-
-
-
40 kDa thylakoid lumen PPIase
-
-
-
-
40 kDa thylakoid lumen rotamase
-
-
-
-
51 kDa FK506-binding protein
-
-
-
-
52 kDa FK506 binding protein
-
-
-
-
54 kDa progesterone receptor-associated immunophilin
-
-
-
-
65 kDa FK506-binding protein
-
-
-
-
CGI-124
-
-
-
-
Chl-Mip
-
-
-
-
CPH
-
-
-
-
Cyclophilin
-
-
-
-
Cyclophilin 18
-
-
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
-
-
-
-
Cyclophilin B
-
-
-
-
Cyclophilin C
-
-
-
-
Cyclophilin cyp2
-
-
-
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Cyclophilin homolog
-
-
-
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Cyclophilin ScCypA
-
-
-
-
Cyclophilin ScCypB
-
-
-
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Cyclophilin-10
-
-
-
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Cyclophilin-11
-
-
-
-
Cyclophilin-40
-
-
-
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Cyclophilin-60
-
-
-
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Cyclophilin-like protein Cyp-60
-
-
-
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Cyclophilin-related protein
-
-
-
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Cyclosporin A-binding protein
-
-
-
-
CYP-40
-
-
-
-
CYP-S1
-
-
-
-
CYP20-3
Cyp3 PPIase
-
-
-
-
CyPA
-
-
-
-
CyPB
-
-
-
-
Estrogen receptor binding cyclophilin
-
-
-
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FF1 antigen
-
-
-
-
FKBP
-
-
-
-
FKBP-12
-
-
-
-
FKBP-12.6
-
-
-
-
FKBP-13
-
-
-
-
FKBP-15
-
-
-
-
FKBP-19
-
-
-
-
FKBP-21
-
-
-
-
FKBP-22
-
-
-
-
FKBP-23
-
-
-
-
FKBP-25
-
-
-
-
FKBP-36
-
-
-
-
FKBP-51
-
-
-
-
FKBP-70
-
-
-
-
FKBP22
-
-
-
-
FKBP52 protein
-
-
-
-
FKBP54
-
-
-
-
FKBP59
-
-
-
-
FKBP65
-
-
-
-
FKBP65RS
-
-
-
-
HBI
-
-
-
-
Histidine rich protein
-
-
-
-
hPar14
-
-
-
-
HSP binding immunophilin
-
-
-
-
HSP90-binding immunophilin
-
-
-
-
Immunophilin FKBP12
-
-
-
-
Immunophilin FKBP12.6
-
-
-
-
Immunophilin FKBP36
-
-
-
-
Immunophilin FKBP65
-
-
-
-
Isomerase, peptidylprolyl cis-trans
-
-
-
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Macrolide binding protein
-
-
-
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Macrophage infectivity potentiator
-
-
-
-
MtFK
-
-
-
-
Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
-
-
-
-
Parvulin
-
-
-
-
Parvulin 14
-
-
-
-
Peptide bond isomerase
-
-
-
-
Peptidyl-prolyl cis-trans isomerase
Peptidyl-prolyl cis-trans isomerase plp
-
-
-
-
Peptidyl-prolyl cis-trans isomerase surA
-
-
-
-
Peptidyl-prolyl cis/trans isomerase EPVH
-
-
-
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Peptidylprolyl cis-trans isomerase
-
-
-
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PfCyP
-
-
-
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Planta-induced rust protein 28
-
-
-
-
PPIase
PPIase Pin1
-
-
-
-
PPIase Pin4
-
-
-
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Proline rotamase
-
-
-
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Proteins, cyclophilins
-
-
-
-
Proteins, specific or class, cyclophilins
-
-
-
-
Rapamycin-binding protein
-
-
-
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Rapamycin-selective 25 kDa immunophilin
-
-
-
-
Rotamase
-
-
-
-
Rotamase Pin1
-
-
-
-
Rotamase Pin4
-
-
-
-
Rotamase plp
-
-
-
-
S-cyclophilin
-
-
-
-
S1205-06
-
-
-
-
SCYLP
-
-
-
-
SmCYP A
-
-
-
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SmCYP B
-
-
-
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Smp17.7
-
-
-
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SP18
-
-
-
-
WHP
-
-
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
-
-
PPIase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Peptidylproline cis-trans-isomerase
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
CAS REGISTRY NUMBER
COMMENTARY
95076-93-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
N-succinyl-Ala-Ala-(trans)-Pro-Phe-4-nitroanilide
-
-
-
?
Suc-Ala-Ala-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Ala-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
Suc-Ala-Leu-cis-Pro-Phe-4-nitroanilide
Suc-Ala-Leu-trans-Pro-Phe-4-nitroanilide
cis/trans-isomerization
-
-
?
AGL24 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
SOC1 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
-
-
?
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24
-
-
?
additional information
?
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
additional information
?
-
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
AGL24 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif. The interaction between Pin1At and AGL24 mediates the AGL24 stability in the nucleus
-
-
?
SOC1 protein
?
-
cis/trans conformational change of phosphorylated Ser/Thr-Pro motif
-
-
?
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
not essential for protein import into chloroplast
-
?
additional information
?
-
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24
-
-
?
additional information
?
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
additional information
?
-
-
AtFKBP13 and AtCYP20-2 possess peptidyl-prolyl cis/trans isomerase activity and might be involved in protein folding catalysis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.036
N-succinyl-Ala-Ala-(cis)-Pro-Phe-4-nitroanilide
pH 8.0, 15°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the isomerization and disulfide-reduction activities are two independent functions of the enzyme that both are regulated by the redox state of the active centre. Dithiol-disulfide transitions have a regulatory role in protein function
additional information
-
the isomerization and disulfide-reduction activities are two independent functions of the enzyme that both are regulated by the redox state of the active centre. Dithiol-disulfide transitions have a regulatory role in protein function
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ROC1, cytosolic enzyme; two genes encoding CypP: ROC1 and ROC4
Swissprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
no activity detected in root. ROC4 is expressed only in photosynthetic organs
additional information
no activity detected in root. ROC4 is expressed only in photosynthetic organs
additional information
-
no activity detected in root. ROC4 is expressed only in photosynthetic organs
additional information
ROC1 is expressed in all tested plant organs
additional information
ROC1 is expressed in all tested plant organs
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
in stroma of chloroplasts, not in thylakoid membrane and thylakoid lumen the ROC4 protein is imported into chloroplasts where it is processed to the predicted mature size
-
lumen of thylakoid, enzyme isoforms AtCYP20-2 and AtFKBP13. In thiol-reducing conditions, enzyme activity of AtFKBP13 is suppressed severalfold
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
ROF2 encodes a peptidyl-prolyl cis-trans isomerase of the FK506-binding protein class
malfunction
loss of function of ROF2, and especially double mutation of ROF2 and the closely related gene ROF1, results in acid sensitivity, stress and development phenotypes of ROF mutants, overview
physiological function
additional information
physiological function
-
Arabidopsis thaliana PIN1-type parvulin 1, Pin1At, controls floral transition by accelerating cis/trans isomerization of the phosphorylated Ser/Thr-Pro motifs in two MADS-domain transcription factors, SOC1 and AGL24. The Ser/Thr-Pro motifs are important for Pin1At function in promoting flowering through AGL24 and SOC1. Phosphorylation-dependent prolyl cis/trans isomerization of key transcription factors is an important flowering regulatory mechanism, overview
physiological function
peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis. As ROF2 induction and intracellular acidification are common consequences of many stresses, this mechanism of pH homeostasis may be of general importance for stress tolerance. Chaperone ROF2 not only helps to refold proteins but also activates H+ extrusion to restore intracellular pH
physiological function
enzyme interacts with calmodulin in vivo and in vitro. In vitro interaction is Ca2+-dependent, and the calmodulin-binding domain is localized to 35-70 amino acid residues in the N-terminus
additional information
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
additional information
-
ROF2 overexpressing plants show tolerance to toxic cations such as lithium, norspermidine and hygromycin B, whose uptake is driven by the membrane potential, due to activation of the electrogenic plasma membrane proton pump, ROF2 activates K+ transport, H+-ATPase, phenotypes, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CP18C_ARATH
172
0
18373
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 23000, SDS-PAGE, 18920, calculated from sequence, His-tagged recombinant protein
additional information
-
solution structure determined by three-dimensional nuclear magnetic resonance spectroscopy
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C129S
presence of dithiothreitol, 49% of wild-type activity, presence of H2O2, 84% of wild-type activity
C171S
presence of dithiothreitol, 25% of wild-type activity, presence of H2O2, 87% of wild-type activity
C176S
presence of dithiothreitol, 94% of wild-type activity, presence of H2O2, 231% of wild-type activity
C54S
presence of dithiothreitol, 40% of wild-type activity, presence of H2O2, 123% of wild-type activity
additional information
additional information
construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
-
construction of DNA T-insertion mutants. PPIase activity in the thylakoid lumen of the mutants lacking either AtFKBP13 or both AtFKBP13 and AtCYP20-2 is 10% and 2%, respectively, of wild-type activity. Residual PPIase activity detected in the double mutant originates from AtCYP20-3. None of the mutants differs from the wild-type plants when grown under normal, cold stress or high light conditions
additional information
overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
additional information
-
overexpression of ROF2 confers tolerance to intracellular acidification by increasing proton extrusion from cells. Expression of ROF2 activates K+ uptake, causing depolarization of the plasma membrane, which activates the electrogenic plasma membrane proton pump, H+-ATPase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ROF2, overexpression in transgenic Arabidopsis thaliana lines
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
intracellular acid stress generated by weak organic acids at normal external pH induces expression of several chaperone genes, including ROF2
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lippuner, V.; Chou, I.T.; Scott, S.V.; Ettinger, W.F.; Theg, S.M.; Gasser, C.S.
Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana
J. Biol. Chem.
269
7863-7868
1994
Arabidopsis thaliana (P34790), Arabidopsis thaliana (P34791), Arabidopsis thaliana
Landrieu, I.; Wieruszeski, J.M.; Wintjens, R.; Inz, D.; Lippens, G.
Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana
J. Mol. Biol.
320
321-332
2002
Arabidopsis thaliana
Laxa, M.; Koenig, J.; Dietz, K.J.; Kandlbinder, A.
Role of the cysteine residues in Arabidopsis thaliana cyclophilin CYP20-3 in peptidyl-prolyl cis-trans isomerase and redox-related functions
Biochem. J.
401
287-297
2007
Arabidopsis thaliana (P34791), Arabidopsis thaliana
Shapiguzov, A.; Edvardsson, A.; Vener, A.V.
Profound redox sensitivity of peptidyl-prolyl isomerase activity in Arabidopsis thylakoid lumen
FEBS Lett.
580
3671-3676
2006
Arabidopsis thaliana
Wang, Y.; Liu, C.; Yang, D.; Yu, H.; Liou, Y.C.
Pin1At encoding a peptidyl-prolyl cis/trans isomerase regulates flowering time in Arabidopsis
Mol. Cell
37
112-122
2010
Arabidopsis thaliana
Ingelsson, B.; Shapiguzov, A.; Kieselbach, T.; Vener, A.V.
Peptidyl-prolyl isomerase activity in chloroplast thylakoid lumen is a dispensable function of immunophilins in Arabidopsis thaliana
Plant Cell Physiol.
50
1801-1814
2009
Arabidopsis thaliana (Q9SCY2), Arabidopsis thaliana
Bissoli, G.; Ninoles, R.; Fresquet, S.; Palombieri, S.; Bueso, E.; Rubio, L.; Garcia-Sanchez, M.J.; Fernandez, J.A.; Mulet, J.M.; Serrano, R.
Peptidyl-prolyl cis-trans isomerase ROF2 modulates intracellular pH homeostasis in Arabidopsis
Plant J.
70
704-716
2012
Arabidopsis thaliana (Q9FJL3), Arabidopsis thaliana
Kaur, G.; Singh, S.; Singh, H.; Chawla, M.; Dutta, T.; Kaur, H.; Bender, K.; Snedden, W.A.; Kapoor, S.; Pareek, A.; Singh, P.
Characterization of peptidyl-prolyl cis-trans isomerase- and calmodulin-binding activity of a cytosolic Arabidopsis thaliana cyclophilin AtCyp19-3
PLoS ONE
10
e0136692
2015
Arabidopsis thaliana (Q38867), Arabidopsis thaliana
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