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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Xenopus laevis and UniProt Accession O42123
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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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- 5.2.1.8
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cyclosporine
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immunophilins
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isomerization
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genorm
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voltage-dependent
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phosphorylation-dependent
- ns5a
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ca2+-induced
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direct-acting
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bestkeeper
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excitation-contraction
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emmprin
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normfinder
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ribosome-associated
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The taxonomic range for the selected organisms is: Xenopus laevis
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
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12.6 kDa FKBP
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13 kDa FKBP
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15 kDa FKBP
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19 kDa FK506-binding protein
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22 kDa FK506-binding protein
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25 kDa FKBP
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27 kDa membrane protein
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36 kDa FK506 binding protein
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40 kDa thylakoid lumen PPIase
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40 kDa thylakoid lumen rotamase
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51 kDa FK506-binding protein
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52 kDa FK506 binding protein
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54 kDa progesterone receptor-associated immunophilin
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65 kDa FK506-binding protein
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CGI-124
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Chl-Mip
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CPH
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Cyclophilin
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Cyclophilin 18
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Cyclophilin 33
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Cyclophilin A
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Cyclophilin B
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Cyclophilin C
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Cyclophilin cyp2
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Cyclophilin homolog
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Cyclophilin ScCypA
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Cyclophilin ScCypB
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Cyclophilin-10
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Cyclophilin-11
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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
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CYP-40
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CYP-S1
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Cyp3 PPIase
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CyPA
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CyPB
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Estrogen receptor binding cyclophilin
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FF1 antigen
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FKBP
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FKBP-12
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FKBP-12.6
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FKBP-13
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FKBP-15
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FKBP-19
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FKBP-21
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FKBP-22
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FKBP-23
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FKBP-25
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FKBP-36
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FKBP-51
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FKBP-70
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FKBP22
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FKBP52 protein
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FKBP54
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FKBP59
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FKBP65
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FKBP65RS
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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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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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Macrolide binding protein
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Macrophage infectivity potentiator
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MtFK
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Nucleolar proline isomerase
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p17.7
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P31
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P54
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p59 protein
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Par14
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Parvulin
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Parvulin 14
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Peptide bond isomerase
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Peptidyl-prolyl cis-trans isomerase
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
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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
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Proteins, specific or class, cyclophilins
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Rapamycin-binding protein
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Rapamycin-selective 25 kDa immunophilin
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Rotamase
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Rotamase Pin1
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Rotamase Pin4
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Rotamase plp
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S-cyclophilin
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S1205-06
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SCYLP
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SmCYP A
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SmCYP B
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Smp17.7
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SP18
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WHP
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Peptidyl-prolyl cis-trans isomerase
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PPIase
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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
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
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
additional information
?
-
FKBP12 and FKBP52 catalyze cis/trans isomerization of regions of TRPC1 implicated in controlling channel opening, molecular mechanism of FKBP52 in TRPC1 channel opening, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
FKBP52 mediates stimulus-dependent TRPC1 gating through isomerization, which is required for chemotropic turning of neuronal growth cones to netrin-1 and myelin-associated glycoprotein and for netrin-1/DCC-dependent midline axon guidance of commissural interneurons in the developing spinal cord. By contrast, FKBP12 mediates spontaneous opening of TRPC1 through isomerization and is not required for growth cone responses to netrin-1, PPIase-dependent molecular mechanism, overview. PPIase-dependent regulation of netrin-1-induced Ca2+ influx by FKBP52. FKBP52 and its regulation of TRPC1 are essential for commissural axon guidance in vivo. The PPIase activity of FKBP52 is required for MAG-induced, but not for Sema3-induced, growth cone repulsion
physiological function
-
Xenopus peptidyl-prolyl cis-trans isomerase FKBP1B induces ectopic secondary axis and is involved in eye formation during Xenopus embryogenesis
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). FKB1A_XENLA
108
0
11912
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
overexpression of mutant FKBP52-FD67DV, but not of wild-type FKBP52, leads to similar midline targeting errors and premature fasciculation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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