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beta2b-tubulin + H2O
?
-
incubation with isoform CCP5 causes decreases of the peaks corresponding to multi- and monoglutamylated beta2b-tubulin and a dramatic increase of the peak corresponding to beta2b-tubulin without Glu on the side chain
-
?
biotin-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
biotin-Glu-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
biotin-Glu-Glu-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
biotin-Glu-Glu-Glu-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
biotin-Glu-Glu-Glu-Gly-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
biotin-Glu-Glu-Gly-Glu-Glu-Glu + H2O
?
Nna1 can metabolized substrates with two or more glutamate residues. It is more active against longer chain substrates
-
-
?
DATAEEEGEMYE(gamma-(E)2)-DDDEESEAQGPK + 2 H2O
DATAEEEGEMYEDDDEESEAQGPK + 2 L-Glu
synthetic beta3-tubulin-based 24-residue C-terminal peptide with two side chain Glu residues
about 30% removal of Glu side chains
-
?
DATAEEEGEMYE(gamma-(E)3)-DDDEESEAQGPK + 3 H2O
DATAEEEGEMYEDDDEESEAQGPK + 3 L-Glu
synthetic beta3-tubulin-based 24-residue C-terminal peptide with three side chain Glu residues
-
-
?
DATAEEEGEMYE(gamma-(E)4)-DDDEESEAQGPK + 4 H2O
DATAEEEGEMYEDDDEESEAQGPK + 4 L-Glu
synthetic beta3-tubulin-based 24-residue C-terminal peptide with four side chain Glu residues
-
-
?
DATAEEEGEMYE(gamma-E)-DDDEESEAQGPK + H2O
DATAEEEGEMYEDDDEESEAQGPK + L-Glu
synthetic beta3-tubulin-based 24-residue C-terminal peptide with one side chain Glu residue
complete removal of Glu side chain
-
?
DELTA2-tubulin + H2O
DELTA3-tubulin + L-glutamate
i.e. tubulin lacking two C-terminal amino acids
i.e. tubulin lacking two C-terminal amino acids
-
?
detyrosinated alpha-tubulin + H2O
DELTA2-tubulin + L-glutamate
monoglutamyl alpha-tubulin + H2O
alpha-tubulin + L-Glu
-
-
-
r
monoglutamyl beta-tubulin + H2O
beta-tubulin + L-Glu
-
-
-
r
polyglutamated tubulin + H2O
?
CCP5 specifically metabolizes the gamma-carboxyl linked, branch point glutamate. It metabolized gamma-carboxyl-linked glutamate of synthetic substrates and tubulin
-
-
?
polymerized microtubules + H2O
?
polymerized microtubules prepared from MDA-MB-231 cells grown on a coverslip. Isoform CCP5 eliminates GT335 signals and diminishes poly(E) signals on polymerized tubulin
-
-
?
polymerized microtubules + H2O
DELTA2-tubulin + ?
tubulin + H2O
?
porcine brain tubulin. Isoform CCP5 can process paclitaxel-treated tubulin, and the activity of CCP5 in the presence of paclitaxel is comparable with the activity in the absence of the drug
-
-
?
tubulin-polyglutamate + H2O
?
the enzyme (Nna1) metabolizes the polyglutamate side chain of tubulin. It removes the C-terminal glutamate from substrates with two or more glutamates. The enzyme exhibits a monoglutamase activity when aspartic acid precedes a single glutamate
-
-
?
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDEEED + H2O
[40S ribosomal protein S9]-KNAKKGQGGAGAGDD + Glu-Glu-Glu-Asp
-
-
-
?
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDEEED + H2O
[40S ribosomal protein S9]-KNAKKGQGGAGAGDDE + Glu-Glu-Asp
-
-
-
?
[alpha-tubulin 1A/1B]-EDMAALEKDYEEVGVDSVEGEGEEEGEE + H2O
[alpha-tubulin 1A/1B]-EDMAALEKDYEEVGVDSVEGEGEEEG + Glu-Glu
in the case of alpha-tubulin, it is considered that CCP1 uses as substrate the pool of detyrosinated tubulin naturally present in the cell
-
-
?
[alpha-tubulin 1C]-EDMAALEKDYEEVGADSADGEDEGEE + H2O
[alpha-tubulin 1C]-EDMAALEKDYEEVGADSADGEDEG + Glu-Glu
in the case of alpha-tubulin, it is considered that CCP1 uses as substrate the pool of detyrosinated tubulin naturally present in the cell
-
-
?
[eukaryotic translation initiation factor 4H]-EEVVQKEQE + H2O
[eukaryotic translation initiation factor 4H]-EEVVQKEQ + Glu
-
-
-
?
[high mobility group protein B1]-EEEEDEEDEEDEEEEEDEEDEDEEEDDDDE + H2O
[high mobility group protein B1] + EEEEDEEDEEDEEEEEDEEDEDEEEDDDDE
-
-
-
?
[high mobility group protein B2]-EDEEEEEEEEDEDEEEEDEDEE + H2O
[high mobility group protein B2] + EDEEEEEEEEDEDEEEEDEDEE
-
-
-
?
[high mobility group protein B3]-KKVEEEDEEEEEEEEEEEEEEDE + H2O
[high mobility group protein B3]-KKVEEED + EEEEEEEEEEEEEEDE
-
-
-
?
[high mobility group protein B3]-KKVEEEDEEEEEEEEEEEEEEDE + H2O
[high mobility group protein B3]-KKVEEEDE + EEEEEEEEEEEEEDE
-
-
-
?
[myosin light chain kinase 1/telokinc]-EEEEEE + H2O
[myosin light chain kinase 1/telokinc] + EEEEEE
-
-
-
?
[stathmin]-KNKESKDPADETEAD + H2O
[stathmin]-KNKESKDPADETEA + Asp
-
-
-
?
[TRAF-type zinc finger domain-containing protein]-TAKAKPSKQQGAGDAEEEEEE + H2O
[TRAF-type zinc finger domain-containing protein]-TAKAKPSKQQGAGDA + Glu-Glu-Glu-Glu-Glu-Glu
-
-
-
?
additional information
?
-
detyrosinated alpha-tubulin + H2O
DELTA2-tubulin + L-glutamate
-
porcine brain tubulin
i.e. tubulin lacking two C-terminal amino acids
-
?
detyrosinated alpha-tubulin + H2O
DELTA2-tubulin + L-glutamate
-
treatment with isoform CCP5 leads to a decrease in the peak intensities of the multi- as well as monoglutamylated alpha-tubulin forms and an increase in the peak intensity of the form lacking all Glu residues on the side chain
-
?
detyrosinated alpha-tubulin + H2O
DELTA2-tubulin + L-glutamate
porcine brain tubulin
i.e. tubulin lacking two C-terminal amino acids
-
?
polymerized microtubules + H2O
DELTA2-tubulin + ?
-
-
i.e. tubulin lacking two C-terminal amino acids
-
?
polymerized microtubules + H2O
DELTA2-tubulin + ?
-
i.e. tubulin lacking two C-terminal amino acids
-
?
additional information
?
-
-
isoform CCP1 removes Glu residues from the polyglutamyl side chains of porcine brain alpha- and beta-tubulin and also generates a form of alpha-tubulin with two C-terminal Glu residues removed
-
-
?
additional information
?
-
isoform CCP5 is a deglutamylase that specifically removes branching point glutamates. CCP5 is the only enzyme that is able to remove tubulin-tyrosine ligase-like protein TTLL4-dependent monoglutamylation. CCP5 removes glutamylation not only from tubulin but also from other substrates that are monoglutamylated by TTLL4. Active CCP5 completely removes monoglutamylation and strongly reduces polyglutamylation of tubulin by TTLL6. Only short side chains are removed, and CCP5 does not generate DELTA2-tubulin
-
-
?
additional information
?
-
CCP1 processes both glutamates as well as C-terminal aspartates
-
-
-
additional information
?
-
CCP5 does not have detyrosinase activity
-
-
?
additional information
?
-
-
CCP5 does not have detyrosinase activity
-
-
?
additional information
?
-
isoform CCP1 removes Glu residues from the polyglutamyl side chains of porcine brain alpha- and beta-tubulin and also generates a form of alpha-tubulin with two C-terminal Glu residues removed
-
-
?
additional information
?
-
-
isoform CCP1 removes Glu residues from the polyglutamyl side chains of porcine brain alpha- and beta-tubulin and also generates a form of alpha-tubulin with two C-terminal Glu residues removed
-
-
?
additional information
?
-
isoform CCP5 removes multiple glutamate residues and the branch point glutamate from the side chains of porcine brain alpha- and beta-tubulin. CCP5 excises C-terminal glutamates from detyrosinated alpha-tubulin. The enzyme also removes multiple glutamate residues from side chains and C-termini of paclitaxel-stabilized microtubules. CCP5 both shortens and removes side chain glutamates from synthetic peptides corresponding to the C-terminal region of beta3-tubulin
-
-
?
additional information
?
-
-
isoform CCP5 removes multiple glutamate residues and the branch point glutamate from the side chains of porcine brain alpha- and beta-tubulin. CCP5 excises C-terminal glutamates from detyrosinated alpha-tubulin. The enzyme also removes multiple glutamate residues from side chains and C-termini of paclitaxel-stabilized microtubules. CCP5 both shortens and removes side chain glutamates from synthetic peptides corresponding to the C-terminal region of beta3-tubulin
-
-
?
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Alstrom Syndrome
Birt-Hogg-Dubé syndrome associated with chorioretinopathy and nyctalopia: a case report and review of the literature.
Ataxia
Alteration of Neural Stem Cell Functions in Ataxia and Male Sterility Mice: A Possible Role of ?-Tubulin Glutamylation in Neurodegeneration.
Carcinoma
Reduced cytosolic carboxypeptidase 6 (CCP6) level leads to accumulation of serum polyglutamylated DNAJC7 protein: A potential biomarker for renal cell carcinoma early detection.
Carcinoma, Renal Cell
Reduced cytosolic carboxypeptidase 6 (CCP6) level leads to accumulation of serum polyglutamylated DNAJC7 protein: A potential biomarker for renal cell carcinoma early detection.
Ciliopathies
Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function.
Cysts
Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function.
Hydrocephalus
Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function.
Infertility
Lack of Cytosolic Carboxypeptidase 1 Leads to Subfertility due to the Reduced Number of Antral Follicles in pcd3J-/- Females.
Infertility, Male
Alteration of Neural Stem Cell Functions in Ataxia and Male Sterility Mice: A Possible Role of ?-Tubulin Glutamylation in Neurodegeneration.
Infertility, Male
Loss of the deglutamylase CCP5 perturbs multiple steps of spermatogenesis and leads to male infertility.
Retinitis Pigmentosa
Birt-Hogg-Dubé syndrome associated with chorioretinopathy and nyctalopia: a case report and review of the literature.
Retinitis Pigmentosa
Establishing the involvement of the novel gene AGBL5 in retinitis pigmentosa by whole genome sequencing.
Retinitis Pigmentosa
Exome Sequencing Reveals AGBL5 as Novel Candidate Gene and Additional Variants for Retinitis Pigmentosa in Five Turkish Families.
Retinitis Pigmentosa
Mutations in AGBL5, Encoding ?-Tubulin Deglutamylase, Are Associated With Autosomal Recessive Retinitis Pigmentosa.
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malfunction
CCP5 deficiency does cause male infertility
malfunction
knockdown of CCP1 and CCP5 results in similar defects including severe hydrocephalus and axial curvature
malfunction
loss of CCP1 in mice causes cerebellar Purkinje cell degeneration. Neuronal degeneration caused by loss of CCP1 in mammals may represent a novel ciliopathy in which cilia are formed but not maintained, depriving the cell of cilia-based signal transduction
physiological function
isoform ccp5 knockdown increases cilia tubulin glutamylation, induces ciliopathy phenotypes, including axis curvature, hydrocephalus, and pronephric cysts, and disrupts multicilia motility. ccp5 knockdown restores tubulin glutamylation and promotes multicilia assembly in intraflagellar transport-deficient zebrafish
physiological function
loss of ccpp-6 gene function, which encodes one of two cytosolic carboxypeptidases, results in elevated levels of ciliary microtubule polyglutamylation. Overexpression of this gene in ciliated cells decreases polyglutamylation signals
physiological function
overexpression of murine CCP5 causes a dramatic loss of microtubule polyglutamylation in cultured mammalian cells. Recombinantly expressed Myc-tagged CCP5 exhibits deglutamylase biochemical activities
physiological function
-
overexpression or knockdown (8090%) of isoform CCP1 in human embryonic kidney 293T cells does not affect the levels of most intracellular peptides but alters the levels of alpha-tubulin lacking two C-terminal amino acids more than 5fold, suggesting that tubulin processing is the primary function of CCP1
physiological function
the Purkinje cell degeneration (pcd) mouse has a disruption in the gene encoding cytosolic carboxypeptidase 1. Pcd mutant mouse brain shows hyperglutamylation of both alpha- and beta-tubulin
physiological function
CCP1 and CCP5 play important roles in zebrafish embryonic development, particularly the development and functioning of cilia. Loss of the deglutamylating enzymes causes developmental defects in zebrafish
physiological function
CCP1-mediated shortening of acidic protein tails might regulate protein-protein and protein-DNA interactions
physiological function
CCP5 is not essential for neuronal survival in mouse. CCP5 is involved in spermatogenesis
physiological function
CCPP-1 acts as a tubulin deglutamylase that regulates the localization and velocity of kinesin motors, and the structural integrity of microtubules in sensory cilia of a multicellular, living animal
physiological function
the C-terminal regions of tubulins undergo multiple forms of post-translational modifications, which, in addition to polyglutamylation, include removal and addition of a C-terminal tyrosine residue, addition and trimming of polyglycine side chains, and proteolytic processing to yield DELTA2 tubulin. The enzyme (Nna1) is involved in several of these processes, as it not only removes polyglutamate chains from tubulin, but also cleaves synthetic substrates that mimic the detyrosinated and DELTA2 forms of the C terminus of alpha-tubulin the enzyme is involved in the posttranslational process of polyglutamylation, where they catalyze the removal of polyglutamate side chains
physiological function
the enzyme regulates the ciliary localization of the kinesin-3 KLP-6 and the polycystin PKD-2 in male-specific sensory neurons in Caenorhabditis elegans. CCPP-1 activity is required for ciliary maintenance but not ciliogenesi
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Rogowski, K.; van Dijk, J.; Magiera, M.M.; Bosc, C.; Deloulme, J.C.; Bosson, A.; Peris, L.; Gold, N.D.; Lacroix, B.; Bosch Grau, M.; Bec, N.; Larroque, C.; Desagher, S.; Holzer, M.; Andrieux, A.; Moutin, M.J.; Janke, C.
A family of protein-deglutamylating enzymes associated with neurodegeneration
Cell
143
564-578
2010
Homo sapiens (Q8NDL9)
brenda
Kimura, Y.; Kurabe, N.; Ikegami, K.; Tsutsumi, K.; Konishi, Y.; Kaplan, O.I.; Kunitomo, H.; Iino, Y.; Blacque, O.E.; Setou, M.
Identification of tubulin deglutamylase among Caenorhabditis elegans and mammalian cytosolic carboxypeptidases (CCPs)
J. Biol. Chem.
285
22936-22941
2010
Caenorhabditis elegans (Q09296), Caenorhabditis elegans, Mus musculus (Q09M02), Mus musculus
brenda
Berezniuk, I.; Vu, H.; Lyons, P.; Sironi, J.; Xiao, H.; Burd, B.; Setou, M.; Angeletti, R.; Ikegami, K.; Fricker, L.
Cytosolic carboxypeptidase 1 is involved in processing alpha- and beta-tubulin
J. Biol. Chem.
287
6503-6517
2012
Homo sapiens, Mus musculus (Q09M02), Mus musculus
brenda
Berezniuk, I.; Lyons, P.J.; Sironi, J.J.; Xiao, H.; Setou, M.; Angeletti, R.H.; Ikegami, K.; Fricker, L.D.
Cytosolic carboxypeptidase 5 removes alpha- and gamma-linked glutamates from tubulin
J. Biol. Chem.
288
30445-30453
2013
Mus musculus (Q09M02), Mus musculus
brenda
Pathak, N.; Austin-Tse, C.A.; Liu, Y.; Vasilyev, A.; Drummond, I.A.
Cytoplasmic carboxypeptidase 5 regulates tubulin glutamylation and zebrafish cilia formation and function
Mol. Biol. Cell
25
1836-1844
2014
Danio rerio (Q68EI3), Danio rerio
brenda
O'Hagan, R.; Piasecki, B.P.; Silva, M.; Phirke, P.; Nguyen, K.C.; Hall, D.H.; Swoboda, P.; Barr, M.M.
The tubulin deglutamylase CCPP-1 regulates the function and stability of sensory cilia in C. elegans
Curr. Biol.
21
1685-1694
2011
Caenorhabditis elegans (O76373), Mus musculus (Q641K1)
brenda
Kalinina, E.; Biswas, R.; Berezniuk, I.; Hermoso, A.; Aviles, F.X.; Fricker, L.D.
A novel subfamily of mouse cytosolic carboxypeptidases
FASEB J.
21
836-850
2007
Mus musculus (Q09M02)
brenda
Lyons, P.J.; Sapio, M.R.; Fricker, L.D.
Zebrafish cytosolic carboxypeptidases 1 and 5 are essential for embryonic development
J. Biol. Chem.
288
30454-30462
2013
Danio rerio (Q4U2V3), Danio rerio (Q68EI3)
brenda
Wu, H.Y.; Rong, Y.; Correia, K.; Min, J.; Morgan, J.I.
Comparison of the enzymatic and functional properties of three cytosolic carboxypeptidase family members
J. Biol. Chem.
290
1222-1232
2015
Mus musculus (Q641K1)
brenda
Tanco, S.; Tort, O.; Demol, H.; Aviles, F.X.; Gevaert, K.; Van Damme, P.; Lorenzo, J.
C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini
Mol. Cell. Proteomics
14
177-190
2015
Homo sapiens (Q9UPW5)
brenda
Wu, H.Y.; Wei, P.; Morgan, J.I.
Role of cytosolic carboxypeptidase 5 in neuronal survival and spermatogenesis
Sci. Rep.
7
41428
2017
Mus musculus (Q09M02), Mus musculus
brenda
3.4.17.24 tubulin-glutamate carboxypeptidase
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