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Search results 201 to 253 out of 253 for Cpd

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Type Details Score
Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
21858120 | J:176363
First Author: Chaves I
Year: 2011
Journal: PLoS One
Title: The Potorous CPD photolyase rescues a cryptochrome-deficient mammalian circadian clock.
Volume: 6
Issue: 8
Pages: e23447
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Allele
Sharpin<cpdm> | MGI:1856699
 
Name: SHANK-associated RH domain interacting protein; chronic proliferative dermatitis
Allele Type: Spontaneous
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Publication
35422806 | J:323995
 
First Author: Kajitani GS
Year: 2022
Journal: Front Immunol
Title: Photorepair of Either CPD or 6-4PP DNA Lesions in Basal Keratinocytes Attenuates Ultraviolet-Induced Skin Effects in Nucleotide Excision Repair Deficient Mice.
Volume: 13
Pages: 800606
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Allele
Cpd<em1Smoc> | MGI:7289117
Name: carboxypeptidase D; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Ontology Term
- | Joubert syndrome
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Protein Coding Gene
MGI:1347354 | Homer2
Type: protein_coding_gene
Organism: mouse, laboratory
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GO Term
GO:0003904 | deoxyribodipyrimidine photo-lyase activity
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Protein Domain
IPR034224 | M14_CPD_II
Type: Domain
Description: This entry represents the second carboxypeptidase (CP)-like domain of carboxypeptidase D (CPD; EC 3.4.17.22; MEROPS M14.016).Carboxypeptidase D (CPD) differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains []. CPD belongs to the N/E-like subfamily (subfamily M14B) of the M14 family of metallocarboxypeptidases (MCPs) []. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys [, , ]. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila[]. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles []. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors []. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop [].The carboxypeptidase A family can be divided into four subfamilies: M14A(carboxypeptidase A or digestive), M14B (carboxypeptidase H or regulatory), M14C (gamma-D-glutamyl-L-diamino acid peptidase I) and M14D (AGTPBP-1/Nna1-like proteins) [, ]. Members of subfamily M14B have longer C-termini than those of subfamily M14A [], and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble []. The zinc ligands have been determined as two histidines and a glutamate,and the catalytic residue has been identified as a C-terminal glutamate,but these do not form the characteristic metalloprotease HEXXH motif [, ]. Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended α-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [, ].
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Publication
10545093 | -
First Author: Gomis-Rüth FX
Year: 1999
Journal: EMBO J
Title: Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily.
Volume: 18
Issue: 21
Pages: 5817-26
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Publication
11278909 | -
First Author: Aloy P
Year: 2001
Journal: J Biol Chem
Title: The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases.
Volume: 276
Issue: 19
Pages: 16177-84
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Publication
20386952 | -
First Author: Sidyelyeva G
Year: 2010
Journal: Cell Mol Life Sci
Title: Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior.
Volume: 67
Issue: 17
Pages: 2991-3004
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Publication
17641957 | -
First Author: Hoff NP
Year: 2007
Journal: J Clin Immunol
Title: Carboxypeptidase D: a novel TGF-beta target gene dysregulated in patients with lupus erythematosus.
Volume: 27
Issue: 6
Pages: 568-79
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Publication
11148133 | -
First Author: Varlamov O
Year: 2001
Journal: J Cell Sci
Title: Protein phosphatase 2A binds to the cytoplasmic tail of carboxypeptidase D and regulates post-trans-Golgi network trafficking.
Volume: 114
Issue: Pt 2
Pages: 311-22
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Publication
18845756 | -
First Author: Lupardus PJ
Year: 2008
Journal: Science
Title: Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain.
Volume: 322
Issue: 5899
Pages: 265-8
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Publication
19465933 | -
First Author: Shen A
Year: 2009
Journal: Nat Chem Biol
Title: Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin.
Volume: 5
Issue: 7
Pages: 469-78
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Publication
20628577 | -
First Author: Egerer M
Year: 2010
Journal: PLoS Pathog
Title: Inositol hexakisphosphate-induced autoprocessing of large bacterial protein toxins.
Volume: 6
Issue: 7
Pages: e1000942
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Publication
21543324 | -
First Author: Guo B
Year: 2011
Journal: J Biol Chem
Title: Structure of the autocatalytic cysteine protease domain of potyvirus helper-component proteinase.
Volume: 286
Issue: 24
Pages: 21937-43
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Protein Domain
IPR033848 | M14_CPD_III
Type: Domain
Description: This entry represents the third carboxypeptidase (CP)-like domain of Carboxypeptidase D (CPD; MEROPS identifier XM14.001; EC 3.4.17.22)(MEROPS identifier M14.950). Carboxypeptidase D (CPD) differs from all other metallocarboxypeptidases in that it contains multiple CP-like domains []. CPD belongs to the N/E-like subfamily (subfamily M14B) of the M14 family of metallocarboxypeptidases (MCPs) []. CPD is a single-chain protein containing a signal peptide, three tandem repeats of CP-like domains separated by short bridge regions, followed by a transmembrane domain, and a C-terminal cytosolic tail. The first two CP-like domains of CPD contain all of the essential active site and substrate-binding residues, while the third CP-like domain lacks critical residues necessary for enzymatic activity and is inactive towards standard CP substrates. Domain I is optimally active at pH 6.3-7.5 and prefers substrates with C-terminal Arg, whereas domain II is active at pH 5.0-6.5 and prefers substrates with C-terminal Lys [, , ]. CPD functions in the processing of proteins that transit the secretory pathway, and is present in all vertebrates as well as Drosophila[]. It is broadly distributed in all tissue types. Within cells, CPD is present in the trans-Golgi network and immature secretory vesicles, but is excluded from mature vesicles []. It is thought to play a role in the processing of proteins that are initially processed by furin or related endopeptidases present in the trans-Golgi network, such as growth factors and receptors []. CPD is implicated in the pathogenesis of lupus erythematosus (LE), it is regulated by TGF-beta in various cell types of murine and human origin and is significantly down-regulated in CD14 positive cells isolated from patients with LE. As down-regulation of CPD leads to down-modulation of TGF-beta, CPD may have a role in a positive feedback loop [].The carboxypeptidase A family can be divided into four subfamilies: M14A(carboxypeptidase A or digestive), M14B (carboxypeptidase H or regulatory), M14C (gamma-D-glutamyl-L-diamino acid peptidase I) and M14D (AGTPBP-1/Nna1-like proteins) [, ]. Members of subfamily M14B have longer C-termini than those of subfamily M14A [], and carboxypeptidase M (a member of the H family) is bound to the membrane by a glycosylphosphatidylinositol anchor, unlike the majority of the M14 family, which are soluble []. The zinc ligands have been determined as two histidines and a glutamate,and the catalytic residue has been identified as a C-terminal glutamate,but these do not form the characteristic metalloprotease HEXXH motif [, ]. Members of the carboxypeptidase A family are synthesised as inactive molecules with propeptides that must be cleaved to activate the enzyme. Structural studies of carboxypeptidases A and B reveal the propeptide to exist as a globular domain, followed by an extended α-helix; this shields the catalytic site, without specifically binding to it, while the substrate-binding site is blocked by making specific contacts [, ].
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Publication
10506132 | -
First Author: Novikova EG
Year: 1999
Journal: J Biol Chem
Title: Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D.
Volume: 274
Issue: 41
Pages: 28887-92
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Publication
9355738 | -
 
First Author: Tan F
Year: 1997
Journal: Biochem J
Title: Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains.
Volume: 327 ( Pt 1)
Pages: 81-7
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Publication
10329672 | -
First Author: Varlamov O
Year: 1999
Journal: J Biol Chem
Title: Localization of metallocarboxypeptidase D in AtT-20 cells. Potential role in prohormone processing.
Volume: 274
Issue: 21
Pages: 14759-67
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Protein Domain
IPR042308 | HC_PRO_CPD_sf
Type: Homologous_superfamily
Description: Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side [].This superfamily represents the CPD domain of the HC-Pro protein.
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Protein Domain
IPR031159 | HC_PRO_CPD_dom
Type: Domain
Description: This entry represents the CPD domain of the HC-Pro protein. Potyviruses form one of the most numerous groups of plant viruses and are a major cause of crop loss worldwide. The helper-component proteinase (HC-Pro) is an indispensable, multifunctional protein of members of the genus Potyvirus and other viruses of the family Potyviridae. It is directly involved in diverse steps of viral infection, such as aphid plant-to-plant transmission, polyprotein processing, and suppression of host antiviral RNA silencing. HC-Pro is generally divided into three functional domains: a N-terminal domain, a central region, and a cysteine protease domain (CPD) in the C-terminal region. The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. Cysteine and histidine residues form the catalytic dyad at the active site. The HC-Pro CPD domain constitutes the peptidase family C6 of the CA clan [].The HC-Pro CPD domain adopts a compact oval-shaped alpha/beta fold. The secondary structure elements include four α-helices (alpha1-alpha4) and two short β-strands (beta1 and beta2) arranged in the order alpha1-alpha2-alpha3-beta1-beta2-alpha4. In addition, two 3(10) helices are located between alpha3 and beta1 and downstream of alpha4. The four helices form a helix bundle packed against one face of a short β-hairpin formed by strands beta1 and beta2. The catalytic residue Cys is located at the N terminus of helix alpha1, and the other catalytic residue His is located on strand beta2. The substrate binding cleft is lined by the loop connecting helices alpha2 and alpha3 and the N-terminal region of helix alpha1 on one side and by strand beta2 on the other side [].
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Protein Domain
IPR038383 | CPD_dom_sf
Type: Homologous_superfamily
Description: Large bacterial protein toxins autotranslocate functional effector domains tothe eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms of post-translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is regulated by a unique allosteric activation mechanism. Binding of the eukaryotic-specific small molecule inositol hexakisphosphate (InsP(6)) to a basic cleft within the CPD induces a structural rearrangement that exposes the protease active site to its substrates. Proteins containing this domain belong to the peptidase family C80 of clan CD [, , , ].The CGT/MARTX CPD domain consists of a central β-sheet that is surrounded by α-helices. Additional β-strands at the C terminus form a subdomain known as the β-flap, that is loosely attached to the core protease. The CGT/MARTX CPD catalytic dyad is composed of one His and one Cys residue. The distance between the catalytic residues indicates that the Cys is not activated by protonation from His, but rather suggests that the Cys is substrate-activated by close alignment of the scissile bond, while the His functions solely to protonate the leaving group [, , ].
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Protein Domain
IPR020974 | CPD_dom
Type: Domain
Description: Large bacterial protein toxins autotranslocate functional effector domains tothe eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms of post-translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is regulated by a unique allosteric activation mechanism. Binding of the eukaryotic-specific small molecule inositol hexakisphosphate (InsP(6)) to a basic cleft within the CPD induces a structural rearrangement that exposes the protease active site to its substrates. Proteins containing this domain belong to the peptidase family C80 of clan CD [, , , ].The CGT/MARTX CPD domain consists of a central β-sheet that is surrounded by α-helices. Additional β-strands at the C terminus form a subdomain known as the β-flap, that is loosely attached to the core protease. The CGT/MARTX CPD catalytic dyad is composed of one His and one Cys residue. The distance between the catalytic residues indicates that the Cys is not activated by protonation from His, but rather suggests that the Cys is substrate-activated by close alignment of the scissile bond, while the His functions solely to protonate the leaving group [, , ].
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Publication
17464284 | -
First Author: Sheahan KL
Year: 2007
Journal: EMBO J
Title: Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain.
Volume: 26
Issue: 10
Pages: 2552-61
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Protein
O89001
Organism: Mus musculus/domesticus
Length: 1377  
Fragment?: false
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Publication
34341345 | J:323035
First Author: Wright MB
Year: 2021
Journal: Nat Commun
Title: Compounds targeting OSBPL7 increase ABCA1-dependent cholesterol efflux preserving kidney function in two models of kidney disease.
Volume: 12
Issue: 1
Pages: 4662
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Publication
6887246 | -
First Author: Rees DC
Year: 1983
Journal: J Mol Biol
Title: Refined crystal structure of carboxypeptidase A at 1.54 A resolution.
Volume: 168
Issue: 2
Pages: 367-87
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Publication
1449602 | -
First Author: Osterman AL
Year: 1992
Journal: J Protein Chem
Title: Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family.
Volume: 11
Issue: 5
Pages: 561-70
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Publication
33937266 | J:314115
 
First Author: Zhang Y
Year: 2021
Journal: Front Cell Dev Biol
Title: USP44 Stabilizes DDB2 to Facilitate Nucleotide Excision Repair and Prevent Tumors.
Volume: 9
Pages: 663411
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Publication
17127714 | J:120007
First Author: Nijhof JG
Year: 2007
Journal: Carcinogenesis
Title: Epidermal stem and progenitor cells in murine epidermis accumulate UV damage despite NER proficiency.
Volume: 28
Issue: 4
Pages: 792-800
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Publication
24820417 | J:223684
First Author: Kitagawa K
Year: 2014
Journal: Mol Cell Biol
Title: Fbw7 targets GATA3 through cyclin-dependent kinase 2-dependent proteolysis and contributes to regulation of T-cell development.
Volume: 34
Issue: 14
Pages: 2732-44
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Publication
25670854 | J:278427
First Author: Nakajima T
Year: 2015
Journal: J Biol Chem
Title: Regulation of GATA-binding protein 2 levels via ubiquitin-dependent degradation by Fbw7: involvement of cyclin B-cyclin-dependent kinase 1-mediated phosphorylation of THR176 in GATA-binding protein 2.
Volume: 290
Issue: 16
Pages: 10368-81
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Publication
15191564 | J:90498
First Author: Yamazaki F
Year: 2004
Journal: J Invest Dermatol
Title: XPA gene-deficient, SCF-transgenic mice with epidermal melanin are resistant to UV-induced carcinogenesis.
Volume: 123
Issue: 1
Pages: 220-8
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Publication
16117798 | J:100666
First Author: Itoh T
Year: 2005
Journal: J Invest Dermatol
Title: The photocarcinogenesis of antibiotic lomefloxacin and UVA radiation is enhanced in xeroderma pigmentosum group A gene-deficient mice.
Volume: 125
Issue: 3
Pages: 554-9
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Publication
26239054 | J:249446
First Author: Forbes S
Year: 2015
Journal: Diabetes
Title: Selective FFA2 Agonism Appears to Act via Intestinal PYY to Reduce Transit and Food Intake but Does Not Improve Glucose Tolerance in Mouse Models.
Volume: 64
Issue: 11
Pages: 3763-71
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Publication
11062176 | J:65369
First Author: You YH
Year: 2000
Journal: Carcinogenesis
Title: Cyclobutane pyrimidine dimers form preferentially at the major p53 mutational hotspot in UVB-induced mouse skin tumors.
Volume: 21
Issue: 11
Pages: 2113-7
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Publication
8453636 | J:4316
First Author: Ruven HJ
Year: 1993
Journal: Cancer Res
Title: Ultraviolet-induced cyclobutane pyrimidine dimers are selectively removed from transcriptionally active genes in the epidermis of the hairless mouse.
Volume: 53
Issue: 7
Pages: 1642-5
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Publication
8158968 | J:16782
First Author: Sayama K
Year: 1994
Journal: Lab Anim
Title: Pregnancy dependence of mammary tumours in DDD mice congenic for Mtv-2, DDD/1-Mtv-2/Mtv-2.
Volume: 28
Issue: 1
Pages: 44-9
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Publication
12198174 | J:78938
First Author: Schul W
Year: 2002
Journal: EMBO J
Title: Enhanced repair of cyclobutane pyrimidine dimers and improved UV resistance in photolyase transgenic mice.
Volume: 21
Issue: 17
Pages: 4719-29
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Publication
17687389 | J:127312
First Author: Kunisada M
Year: 2007
Journal: J Invest Dermatol
Title: Narrow-band UVB induces more carcinogenic skin tumors than broad-band UVB through the formation of cyclobutane pyrimidine dimer.
Volume: 127
Issue: 12
Pages: 2865-71
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Publication
22166495 | J:181514
First Author: Roy S
Year: 2012
Journal: Carcinogenesis
Title: Silibinin prevents ultraviolet B radiation-induced epidermal damages in JB6 cells and mouse skin in a p53-GADD45α-dependent manner.
Volume: 33
Issue: 3
Pages: 629-36
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Publication
24326454 | J:210555
First Author: Ahmad I
Year: 2014
Journal: J Invest Dermatol
Title: Toll-like receptor-4 deficiency enhances repair of UVR-induced cutaneous DNA damage by nucleotide excision repair mechanism.
Volume: 134
Issue: 6
Pages: 1710-1717
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Publication
24940652 | J:215930
First Author: Kamo A
Year: 2014
Journal: J Invest Dermatol
Title: The excimer lamp induces cutaneous nerve degeneration and reduces scratching in a dry-skin mouse model.
Volume: 134
Issue: 12
Pages: 2977-2984
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Publication
17244818 | J:168198
First Author: Kalinina E
Year: 2007
Journal: FASEB J
Title: A novel subfamily of mouse cytosolic carboxypeptidases.
Volume: 21
Issue: 3
Pages: 836-50
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Publication
1548696 | -
First Author: Guasch A
Year: 1992
Journal: J Mol Biol
Title: Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.
Volume: 224
Issue: 1
Pages: 141-57
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Publication
23873023 | J:212621
First Author: Xu Y
Year: 2014
Journal: Oncogene
Title: Fbw7-dependent cyclin E regulation ensures terminal maturation of bone marrow erythroid cells by restraining oxidative metabolism.
Volume: 33
Issue: 24
Pages: 3161-71
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Publication
11062172 | J:65370
First Author: Budiyanto A
Year: 2000
Journal: Carcinogenesis
Title: Protective effect of topically applied olive oil against photocarcinogenesis following UVB exposure of mice.
Volume: 21
Issue: 11
Pages: 2085-90
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Publication
16307655 | J:107035
First Author: Takahashi H
Year: 2005
Journal: Br J Dermatol
Title: ATX-S10(Na)-photodynamic therapy is less carcinogenic for mouse skin compared with ultraviolet B irradiation.
Volume: 153
Issue: 6
Pages: 1182-6
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Publication
26898828 | J:318312
First Author: Hernandez MA
Year: 2016
Journal: Cell Signal
Title: Regulation of BRAF protein stability by a negative feedback loop involving the MEK-ERK pathway but not the FBXW7 tumour suppressor.
Volume: 28
Issue: 6
Pages: 561-71
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Publication
7674922 | -
 
First Author: Rawlings ND
Year: 1995
Journal: Methods Enzymol
Title: Evolutionary families of metallopeptidases.
Volume: 248
Pages: 183-228
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