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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Rattus norvegicus and UniProt Accession B0BNL2

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EC Tree
IUBMB 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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This record set is specific for:
Rattus norvegicus
UNIPROT: B0BNL2
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
-
-
Cyclophilin-10
-
-
-
-
Cyclophilin-11
-
-
-
-
Cyclophilin-40
-
-
-
-
Cyclophilin-60
-
-
-
-
cyclophilin-D
-
-
Cyclophilin-like protein Cyp-60
-
-
-
-
Cyclophilin-related protein
-
-
-
-
Cyclosporin A-binding protein
-
-
-
-
CYP-40
-
-
-
-
CYP-S1
-
-
-
-
Cyp3 PPIase
-
-
-
-
CyPA
-
-
-
-
CyPB
-
-
-
-
Estrogen receptor binding cyclophilin
-
-
-
-
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
-
-
-
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Histidine rich protein
-
-
-
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hPar14
-
-
-
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HSP binding immunophilin
-
-
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HSP90-binding immunophilin
-
-
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Immunophilin FKBP12
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-
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Immunophilin FKBP12.6
-
-
-
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Immunophilin FKBP36
-
-
-
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Immunophilin FKBP65
-
-
-
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Isomerase, peptidylprolyl cis-trans
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-
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Macrolide binding protein
-
-
-
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Macrophage infectivity potentiator
-
-
-
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MtFK
-
-
-
-
Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
-
-
-
-
Parvulin
-
-
-
-
Parvulin 14
-
-
-
-
Peptide bond isomerase
-
-
-
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Peptidyl-prolyl cis-trans isomerase
-
-
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Peptidyl-prolyl cis-trans isomerase plp
-
-
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Peptidyl-prolyl cis-trans isomerase surA
-
-
-
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Peptidyl-prolyl cis/trans isomerase EPVH
-
-
-
-
peptidyl-prolyl isomerase
peptidyl-prolyl isomerase 1
-
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Peptidylprolyl cis-trans isomerase
-
-
-
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PfCyP
-
-
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Planta-induced rust protein 28
-
-
-
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PPIase
PPIase Pin1
-
-
-
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PPIase Pin4
-
-
-
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Proline rotamase
-
-
-
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Proteins, cyclophilins
-
-
-
-
Proteins, specific or class, cyclophilins
-
-
-
-
Rapamycin-binding protein
-
-
-
-
Rapamycin-selective 25 kDa immunophilin
-
-
-
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Rotamase
-
-
-
-
Rotamase Pin1
-
-
-
-
Rotamase Pin4
-
-
-
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Rotamase plp
-
-
-
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S-cyclophilin
-
-
-
-
S1205-06
-
-
-
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SCYLP
-
-
-
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SmCYP A
-
-
-
-
SmCYP B
-
-
-
-
Smp17.7
-
-
-
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SP18
-
-
-
-
WHP
-
-
-
-
additional information
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 hide
95076-93-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
Suc-Ala-Glu-Pro-Phe-7-amido-4-methylcoumarin
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
RNA polymerase II
?
show the reaction diagram
-
Pin1 modulates RNA polymerase II CTD domain during transcription cycles by interacting with numerous YSPTSPS heptapeptide repeats in the substrate protein
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
juglone
pharmacological inhibitor of isoform Pin1, application of juglone partially prevents dephosphorylation of phosphoptotein Tau at Thr231
cyclosporin A
-
-
diethyl 2,2'-(1,3,6,8-tetraoxo-1,3,6,8-tetrahydrobenzo[lmn][3,8]phenanthroline-2,7-diyl)diacetate
-
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diethyl 2,2'-(1,3,8,10-tetraoxo-1,3,8,10-tetrahydroisoquinolino[4',5',6':6,5,10]anthra[2,1,9-def]isoquinoline-2,9-diyl)diacetate
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-
dipentamethylene thiuram monosulfide
-
-
juglone
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i.e. 5-hydroxy-1,4-naphthalenedione, from leaves, roots, and bark of plants of family Juglandaceae. The compound causes a partial unfolding of the PPIase active site
additional information
-
inhibition of Pin1 inhibits okadaic acid-induced aberrant perikaryal phosphorylation of NF, and inhibition of Pin1 inhibits the okadaic acid- or Fos-induced neuronal apoptosis
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
primary cortical neuron, enzyme isoform Pin1 partly colocalizes with phosphoprotein Tau,which is involved in Alzheimer’s disease
Manually annotated by BRENDA team
-
neuronal cell line
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
2 isoforms
Manually annotated by BRENDA team
additional information
-
Pin1 associates with neurofilaments
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
Pin1 plays a role in neurodegenerative disease such as Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis, overview
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B0BNL2_RAT
165
0
18332
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
-
x * 17000, cytosolic enzyme form, SDS-PAGE
18000
18600
-
x * 18600, major mitochondrial enzyme form, SDS-PAGE
22000
-
x * 22000, microsomal isoform
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
microsomal isoform
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R62A
-
overexpression of wild-type isoform CypB attenuates endoplasmic reticulum stress-induced cell death, whereas overexpression of isomerase activity-defective mutant R62A increases Ca2+ leakage from the endoplasmic reticulum and generation of reactive oxygen species and decreases mitochondrial membrane potential resulting in cell death
S16A
-
a dominant negative mutant
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in H9C2 cell
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bose, S.; Freedman, R.B.
The characterization of peptidyl prolyl cis-trans isomerase (PPI) activity associated with the endoplasmic reticulum
Biochem. Soc. Trans.
20
256S
1992
Bos taurus, Rattus norvegicus
Manually annotated by BRENDA team
Thalhammer, T.; Kiefer, L.J.; Jiang, T.; Handschumacher, R.E.
Isolation and partial characterization of membran-associated cyclophilin and a related 22-kDa glycoprotein
Eur. J. Biochem.
206
31-37
1992
Rattus norvegicus
Manually annotated by BRENDA team
Connern, C.P.; Halestrap., A.P.
Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
Biochem. J.
284
381-385
1992
Rattus norvegicus
Manually annotated by BRENDA team
Li, Y.; Johnson, N.; Capano, M.; Edwards, M.; Crompton, M.
Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis
Biochem. J.
383
101-109
2004
Rattus norvegicus
Manually annotated by BRENDA team
Galas, M.C.; Dourlen, P.; Begard, S.; Ando, K.; Blum, D.; Hamdane, M.; Buee, L.
The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease
J. Biol. Chem.
281
19296-19304
2006
Rattus norvegicus (B0BNL2)
Manually annotated by BRENDA team
Kim, J.; Choi, T.G.; Ding, Y.; Kim, Y.; Ha, K.S.; Lee, K.H.; Kang, I.; Ha, J.; Kaufman, R.J.; Lee, J.; Choe, W.; Kim, S.S.
Overexpressed cyclophilin B suppresses apoptosis associated with ROS and Ca2+ homeostasis after ER stress
J. Cell Sci.
121
3636-3648
2008
Rattus norvegicus
Manually annotated by BRENDA team
Rudrabhatla, P.; Pant, H.C.
Phosphorylation-specific peptidyl-prolyl isomerization of neuronal cytoskeletal proteins by Pin1: implications for therapeutics in neurodegeneration
J. Alzheimers Dis.
19
389-403
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Rudrabhatla, P.; Albers, W.; Pant, H.C.
Peptidyl-prolyl isomerase 1 regulates protein phosphatase 2A-mediated topographic phosphorylation of neurofilament proteins
J. Neurosci.
29
14869-14880
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Shim, S.; Yuan, J.P.; Kim, J.Y.; Zeng, W.; Huang, G.; Milshteyn, A.; Kern, D.; Muallem, S.; Ming, G.L.; Worley, P.F.
Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal growth cones via regulation of TRPC1 channel opening
Neuron
64
471-483
2009
Rattus norvegicus (O42123), Xenopus laevis (Q62658)
Manually annotated by BRENDA team