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Search results 401 to 492 out of 492 for Pts

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Type Details Score
Protein Domain
IPR001550 | Transcrpt_antitermin_CS
Type: Conserved_site
Description: This is a family of bacterial proteins related to the Escherichia coli BglG protein. E. coli BglG protein mediates the positive regulation of the beta-glucoside (bgl) operon by functioning as a transcriptional antiterminator []. BglG is an RNA-binding protein that recognises a specific sequence located just upstream of two termination sites within the operon. The activity of bglG is suppressed by its phosphorylation []by bglF (EII-bgl), the permease from the beta-glucoside PTS system. BglG is highly similar to other proteins, which also probably act as transcriptional antiterminators.
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Publication
9305644 | -
First Author: van Tilbeurgh H
Year: 1997
Journal: EMBO J
Title: Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis.
Volume: 16
Issue: 16
Pages: 5030-6
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Publication
10610766 | -
First Author: Declerck N
Year: 1999
Journal: J Mol Biol
Title: RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.
Volume: 294
Issue: 2
Pages: 389-402
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Publication
11953318 | -
First Author: Yang Y
Year: 2002
Journal: EMBO J
Title: Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT.
Volume: 21
Issue: 8
Pages: 1987-97
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Publication
1655788 | -
First Author: LiCalsi C
Year: 1991
Journal: J Biol Chem
Title: Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium.
Volume: 266
Issue: 29
Pages: 19519-27
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Publication
8031118 | -
First Author: Lee BR
Year: 1994
Journal: Arch Biochem Biophys
Title: Identification of the N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system produced by proteolytic digestion.
Volume: 312
Issue: 1
Pages: 121-4
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Publication
7686067 | -
First Author: Reizer J
Year: 1993
Journal: Protein Sci
Title: Sequence analyses and evolutionary relationships among the energy-coupling proteins Enzyme I and HPr of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.
Volume: 2
Issue: 4
Pages: 506-21
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Publication
19091015 | J:153381
 
First Author: Mizuno Y
Year: 2008
Journal: BMC Bioinformatics
Title: Predicted mouse peroxisome-targeted proteins and their actual subcellular locations.
Volume: 9 Suppl 12
Pages: S16
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Publication
24141423 | J:203764
First Author: Hasegawa K
Year: 2013
Journal: Nat Med
Title: Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes.
Volume: 19
Issue: 11
Pages: 1496-504
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Publication
22302687 | J:185756
First Author: Noreikat K
Year: 2012
Journal: Biol Reprod
Title: Ciliary activity in the oviduct of cycling, pregnant, and muscarinic receptor knockout mice.
Volume: 86
Issue: 4
Pages: 120
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Publication
36117389 | J:329305
First Author: Abousaad S
Year: 2022
Journal: Physiol Rep
Title: Meprin β expression modulates the interleukin-6 mediated JAK2-STAT3 signaling pathway in ischemia/reperfusion-induced kidney injury.
Volume: 10
Issue: 18
Pages: e15468
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Publication
27930725 | J:255277
First Author: Murtaza G
Year: 2016
Journal: PLoS One
Title: Avertin®, but Not Volatile Anesthetics Addressing the Two-Pore Domain K+ Channel, TASK-1, Slows Down Cilia-Driven Particle Transport in the Mouse Trachea.
Volume: 11
Issue: 12
Pages: e0167919
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Publication
32197346 | J:287355
 
First Author: Plain A
Year: 2020
Journal: Int J Mol Sci
Title: Claudin-12 Knockout Mice Demonstrate Reduced Proximal Tubule Calcium Permeability.
Volume: 21
Issue: 6
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Publication
1481666 | J:4093
First Author: Li HS
Year: 1992
Journal: Acta Otolaryngol
Title: Influence of genotype and age on acute acoustic trauma and recovery in CBA/Ca and C57BL/6J mice.
Volume: 112
Issue: 6
Pages: 956-67
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Publication
10094477 | J:53424
First Author: Mullen RT
Year: 1999
Journal: FEBS Lett
Title: Differential subcellular localization of endogenous and transfected soluble epoxide hydrolase in mammalian cells: evidence for isozyme variants.
Volume: 445
Issue: 2-3
Pages: 301-5
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Publication
10436315 | J:56970
First Author: Ohlemiller KK
Year: 1999
Journal: Audiol Neurootol
Title: Early elevation of cochlear reactive oxygen species following noise exposure.
Volume: 4
Issue: 5
Pages: 229-36
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Publication
10452371 | J:57147
First Author: Davis RR
Year: 1999
Journal: Hear Res
Title: Quantitative measure of genetic differences in susceptibility to noise-induced hearing loss in two strains of mice.
Volume: 134
Issue: 1-2
Pages: 9-15
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Publication
22993068 | J:190099
First Author: Zager RA
Year: 2012
Journal: Am J Physiol Renal Physiol
Title: Renal cortical hemopexin accumulation in response to acute kidney injury.
Volume: 303
Issue: 10
Pages: F1460-72
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Publication
10713498 | J:307974
First Author: Yoshida N
Year: 2000
Journal: Hear Res
Title: Acoustic injury in mice: 129/SvEv is exceptionally resistant to noise-induced hearing loss.
Volume: 141
Issue: 1-2
Pages: 97-106
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Publication
7853396 | -
First Author: van Nuland NA
Year: 1995
Journal: J Mol Biol
Title: High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data.
Volume: 246
Issue: 1
Pages: 180-93
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Publication
1549615 | -
First Author: Herzberg O
Year: 1992
Journal: Proc Natl Acad Sci U S A
Title: Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution.
Volume: 89
Issue: 6
Pages: 2499-503
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Publication
7704530 | -
First Author: Liao DI
Year: 1994
Journal: Structure
Title: Refined structures of the active Ser83-->Cys and impaired Ser46-->Asp histidine-containing phosphocarrier proteins.
Volume: 2
Issue: 12
Pages: 1203-16
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Publication
11054290 | -
First Author: Audette GF
Year: 2000
Journal: J Mol Biol
Title: The 1.9 A resolution structure of phospho-serine 46 HPr from Enterococcus faecalis.
Volume: 303
Issue: 4
Pages: 545-53
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Publication
15713472 | -
First Author: Sridharan S
Year: 2005
Journal: J Mol Biol
Title: The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers.
Volume: 346
Issue: 3
Pages: 919-31
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Publication
16316990 | -
First Author: Schumacher MA
Year: 2006
Journal: J Biol Chem
Title: Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation.
Volume: 281
Issue: 10
Pages: 6793-800
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Publication
9237995 | -
First Author: Galinier A
Year: 1997
Journal: Proc Natl Acad Sci U S A
Title: The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression.
Volume: 94
Issue: 16
Pages: 8439-44
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Publication
8254318 | -
First Author: Schneider KH
Year: 1993
Journal: J Gen Microbiol
Title: Cloning, nucleotide sequence and characterization of the mannitol dehydrogenase gene from Rhodobacter sphaeroides.
Volume: 139
Issue: 10
Pages: 2475-84
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Publication
18421563 | -
First Author: Li X
Year: 2008
Journal: Amino Acids
Title: Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr.
Volume: 35
Issue: 3
Pages: 531-9
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Publication
7496537 | -
 
First Author: de Crécy-Lagard V
Year: 1995
Journal: Microbiology
Title: Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene.
Volume: 141 ( Pt 9)
Pages: 2253-60
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Publication
19091879 | -
First Author: Akashi T
Year: 2009
Journal: Plant Physiol
Title: Molecular cloning and characterization of a cDNA for pterocarpan 4-dimethylallyltransferase catalyzing the key prenylation step in the biosynthesis of glyceollin, a soybean phytoalexin.
Volume: 149
Issue: 2
Pages: 683-93
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Publication
24354545 | -
First Author: Karamat F
Year: 2014
Journal: Plant J
Title: A coumarin-specific prenyltransferase catalyzes the crucial biosynthetic reaction for furanocoumarin formation in parsley.
Volume: 77
Issue: 4
Pages: 627-38
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Publication
18218974 | -
First Author: Sasaki K
Year: 2008
Journal: Plant Physiol
Title: Cloning and characterization of naringenin 8-prenyltransferase, a flavonoid-specific prenyltransferase of Sophora flavescens.
Volume: 146
Issue: 3
Pages: 1075-84
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Publication
20400515 | -
First Author: Sadre R
Year: 2010
Journal: J Biol Chem
Title: Catalytic reactions of the homogentisate prenyl transferase involved in plastoquinone-9 biosynthesis.
Volume: 285
Issue: 24
Pages: 18191-8
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Protein Domain
IPR024113 | PEX5_animals
Type: Family
Description: Two types of peroxisomal targeting signal, PTS1 and PTS2, have been identified as amino acid sequences necessary for peroxisome sorting. The peroxisomal proteins containing PTS are recognised by specific receptors and are delivered to the peroxisomal membrane.Peroxisomal targeting signal 1 receptor (PTS1R, also known as PEX5) binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import [, , ]. Proteins related to PTS1R (generally known as PEX5-related proteins) have been identified in mammals. Based on subcellular localization and binding properties they may function as a regulator in an early step of the PTS1 protein import process []. This entry represents PEX5 (also known as PTS1R) from animals.
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Protein Domain
IPR044502 | AtHST-like
Type: Family
Description: This entry represents a group of plant members of the UbiA family of prenyltransferases, including AtHST from Arabidopsis. AtHST catalyses the prenylation and decarboxylation of homogentisate to form 2-methyl-6-solanesyl-1,4-benzoquinol, the first intermediate in plastoquinone-9 biosynthesis []. This entry also includes naringenin 8-dimethylallyltransferase [], glycinol 4-dimethylallyltransferase []and 2-acylphloroglucinol 4-prenyltransferase [], which share significant homology with homogentisate prenyltransferases.Prenyltransferases (PTs) catalyse the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways. Plant aromatic PTs can be divided into two distinct sub-groups: one is 4-hydroxybenzoate PTs, which are involved in ubiquinone (benzoquinone) and naphthoquinone derivatives localised in mitochondria or the endoplasmic reticulum, and the second sub-group comprises members of the homogentisate PT (HGPT) family, which are involved in vitamin E and plastoquinone biosynthesis [].
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Protein Domain
IPR012735 | DhaK_1b
Type: Family
Description: Two types of dihydroxyacetone kinase (glycerone kinase) are described. In yeast and a few bacteria, e.g. Citrobacter freundii, the enzyme is a single chain that uses ATP as phosphoryl donor and is designated . By contract, Escherichia coli and many other bacterial species have a multisubunit form with a phosphoprotein donor related to PTS transport proteins. This family represents a protein, unique to the firmicutes (low GC Gram-positives), that appears to be a divergent second copy of the K subunit of that complex; its gene is always found in operons with the other three proteins of the complex.This entry also includes DhaKLM operon coactivator DhaQ from Streptococcus lactis. It forms a heterotetramer with DhaS and functions as a transcriptional regulator [].
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Protein Domain
IPR008731 | PTS_EIN
Type: Domain
Description: This sequence identifies proteins which are a component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS), a major carbohydrate active transport system. The PTS system is found throughout the bacterial kingdom, and is responsible for the coupled phosphorylation and translocation of numerous sugars across the cytoplasmic membrane [].This entry represents the N-terminal domain of enzyme I (EIN) which transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) which in turn phosphorylates a group of membrane-associated proteins, known as enzyme II.The N-terminal domain of EI (EIN) extends from residues 1 to 259 and can be phosphorylated in a fully reversible manner by phosphorylated HPr. EIN, however, cannot be autophosphorylated by PEP [, ].
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Protein Domain
IPR006318 | PTS_EI-like
Type: Domain
Description: Most proteins with this domain are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferases (or enzyme I) of PTS sugar transport systems. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). This domain is also found in enzyme I-Ntr, which transfers the phosphoryl group from PEP to the phosphoryl carrier protein NPr, and is involved in regulating nitrogen metabolism [], indicating that not all phosphotransferase system components are associated directly with sugar transport. In Xanthomonas campestris, FruB is a multiphosphoryl transfer protein involved in fructose transport that consists of three domains: a fructose-specific enzyme-IIA-like N-terminal domain, followed by an HPr-like domain and an enzyme-I-like C-terminal domain, represented by this entry [].
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Protein Domain
IPR000032 | HPr-like
Type: Domain
Description: This entry represents a structural domain found in both the histidine-containing phosphocarrier protein HPr, as well as its structural homologues, which includes the catabolite repression protein Crh found in Bacillus subtilis [, ]. This domain has a alpha+beta structure found in two layers with an overall architecture of an open faced β-sandwich in which a β-sheet is packed against three α-helices. The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species [, ]. PTS catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to Enzyme I (EI) of the PTS, which in turn transfers it to the phosphoryl carrier protein (HPr) [, ]. Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII). HPr [, ]is a small cytoplasmic protein of 70 to 90 amino acid residues. In some bacteria, HPr is a domain in a larger protein that includes a EIII(Fru) (IIA) domain and in some cases also the EI domain. A conserved histidine in the N-terminal section of HPr serves as an acceptor for the phosphoryl group of EI. In the central part of HPr, there is a conserved serine which (in Gram-positive bacteria only) is phosphorylated by an ATP-dependent protein kinase; a process which probably play a regulatory role in sugar transport. Regulatory phosphorylation at the conserved Ser residue does not appear to induce large structural changes to the HPr domain, in particular in the region of the active site [, ].
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Protein Domain
IPR035895 | HPr-like_sf
Type: Homologous_superfamily
Description: This entry represents a structural domain found in both the histidine-containing phosphocarrier protein HPr, as well as its structural homologues, which includes the catabolite repression protein Crh found in Bacillus subtilis [, ]. This domain has a alpha+beta structure found in two layers with an overall architecture of an open faced β-sandwich in which a β-sheet is packed against three α-helices. The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species [, ]. PTS catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is as follows: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to Enzyme I (EI) of the PTS, which in turn transfers it to the phosphoryl carrier protein (HPr) [, ]. Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease complex (enzymes EII/EIII). HPr [, ]is a small cytoplasmic protein of 70 to 90 amino acid residues. In some bacteria, HPr is a domain in a larger protein that includes a EIII(Fru) (IIA) domain and in some cases also the EI domain. A conserved histidine in the N-terminal section of HPr serves as an acceptor for the phosphoryl group of EI. In the central part of HPr, there is a conserved serine which (in Gram-positive bacteria only) is phosphorylated by an ATP-dependent protein kinase; a process which probably play a regulatory role in sugar transport. Regulatory phosphorylation at the conserved Ser residue does not appear to induce large structural changes to the HPr domain, in particular in the region of the active site [, ].
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Publication
2176881 | -
First Author: Pocalyko DJ
Year: 1990
Journal: Biochemistry
Title: Analysis of sequence homologies in plant and bacterial pyruvate phosphate dikinase, enzyme I of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and other PEP-utilizing enzymes. Identification of potential catalytic and regulatory motifs.
Volume: 29
Issue: 48
Pages: 10757-65
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Publication
8973315 | -
First Author: Reizer J
Year: 1996
Journal: Gene
Title: Novel phosphotransferase-encoding genes revealed by analysis of the Escherichia coli genome: a chimeric gene encoding an Enzyme I homologue that possesses a putative sensory transduction domain.
Volume: 181
Issue: 1-2
Pages: 103-8
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Publication
29717156 | J:262756
First Author: Umino H
Year: 2018
Journal: Sci Rep
Title: High Basolateral Glucose Increases Sodium-Glucose Cotransporter 2 and Reduces Sirtuin-1 in Renal Tubules through Glucose Transporter-2 Detection.
Volume: 8
Issue: 1
Pages: 6791
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Publication
33737325 | J:306107
 
First Author: Niborski LL
Year: 2021
Journal: Dis Model Mech
Title: Hnf1b haploinsufficiency differentially affects developmental target genes in a new renal cysts and diabetes mouse model.
Volume: 14
Issue: 5
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Publication
10436316 | J:56971
First Author: Ohlemiller KK
Year: 1999
Journal: Audiol Neurootol
Title: Targeted deletion of the cytosolic Cu/Zn-superoxide dismutase gene (Sod1) increases susceptibility to noise-induced hearing loss.
Volume: 4
Issue: 5
Pages: 237-46
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Publication
16985005 | J:119218
First Author: Kedmi M
Year: 2007
Journal: Physiol Genomics
Title: Differential brain transcriptome of beta4 nAChR subunit-deficient mice: is it the effect of the null mutation or the background strain?
Volume: 28
Issue: 2
Pages: 213-22
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Publication
26671181 | J:233851
First Author: Zhu Y
Year: 2016
Journal: Endocrinology
Title: Ablation of the Stimulatory G Protein α-Subunit in Renal Proximal Tubules Leads to Parathyroid Hormone-Resistance With Increased Renal Cyp24a1 mRNA Abundance and Reduced Serum 1,25-Dihydroxyvitamin D.
Volume: 157
Issue: 2
Pages: 497-507
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Publication
11335078 | J:69679
First Author: Davis RR
Year: 2001
Journal: Hear Res
Title: Genetic basis for susceptibility to noise-induced hearing loss in mice.
Volume: 155
Issue: 1-2
Pages: 82-90
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Publication
35001662 | J:334322
First Author: Lee HW
Year: 2022
Journal: Am J Physiol Renal Physiol
Title: Acid-base effects of combined renal deletion of NBCe1-A and NBCe1-B.
Volume: 322
Issue: 2
Pages: F208-F224
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Publication
11756410 | J:75321
First Author: Mukai S
Year: 2002
Journal: J Biol Chem
Title: Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells.
Volume: 277
Issue: 11
Pages: 9548-61
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Publication
18957416 | -
First Author: Zurbriggen A
Year: 2008
Journal: J Biol Chem
Title: X-ray structures of the three Lactococcus lactis dihydroxyacetone kinase subunits and of a transient intersubunit complex.
Volume: 283
Issue: 51
Pages: 35789-96
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HT Experiment
GSE159566 | mRNA sequencing of embryonic kidney at different stages from wild-type and heterozygous mutants of a novel mouse model carrying a human splicing point-mutation in the Hnf1b-gene
 
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
33208952 | J:303218
First Author: Adelmann CH
Year: 2020
Journal: Nature
Title: MFSD12 mediates the import of cysteine into melanosomes and lysosomes.
Volume: 588
Issue: 7839
Pages: 699-704
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Protein
B1ARS3
Organism: Mus musculus/domesticus
Length: 106  
Fragment?: true
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Protein
D6RDD7
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Publication
16760471 | -
First Author: Christen S
Year: 2006
Journal: J Biol Chem
Title: Regulation of the Dha operon of Lactococcus lactis: a deviation from the rule followed by the Tetr family of transcription regulators.
Volume: 281
Issue: 32
Pages: 23129-37
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Publication
2644191 | -
First Author: Poolman B
Year: 1989
Journal: J Bacteriol
Title: Lactose transport system of Streptococcus thermophilus: a hybrid protein with homology to the melibiose carrier and enzyme III of phosphoenolpyruvate-dependent phosphotransferase systems.
Volume: 171
Issue: 1
Pages: 244-53
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Publication
7703254 | -
First Author: Pourcher T
Year: 1995
Journal: Biochemistry
Title: Melibiose permease of Escherichia coli: large scale purification and evidence that H+, Na+, and Li+ sugar symport is catalyzed by a single polypeptide.
Volume: 34
Issue: 13
Pages: 4412-20
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Publication
15774881 | -
First Author: Liang WJ
Year: 2005
Journal: J Bacteriol
Title: The gusBC genes of Escherichia coli encode a glucuronide transport system.
Volume: 187
Issue: 7
Pages: 2377-85
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Publication
9573180 | -
First Author: Chaillou S
Year: 1998
Journal: J Bacteriol
Title: Cloning, sequence analysis, and characterization of the genes involved in isoprimeverose metabolism in Lactobacillus pentosus.
Volume: 180
Issue: 9
Pages: 2312-20
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Protein Domain
IPR012736 | DhaK_1
Type: Domain
Description: In bacteria, dihydroxyacetone is formed by the oxidation of glycerol or the aldol cleavage of fructose-6-phosphate. Dihydroxyacetone kinase converts this compound to the glycolytic intermediate dihydroxyacetone phosphate. Two forms of this enzyme have been shown to exist, using either ATP or a phosphoprotein of the phosphoenolpyruvate: sugar phosphotransferase system (PTS) as phosphate donor. The ATP-dependent kinases () are single-subunit enzymes that are composed of two domains []. The phosphoprotein-dependent kinases are composed of three subunits: DhaK and DhaL, which are homologous to the domains from the ATP-dependent enzyme; and DhaM which is a component of the PTS system [].This entry represents the DhaK subunit of phosphoprotein-dependent dihydroxyacetone kinase. The model excludes the DhaK paralog DhaK2 () encoded in the same operon as DhaK in the firmicutes, with which it sometimes exists as a DhaK/DhaK2 fusion. This subunit is a homodimer which contains the dihydroxyacetone-binding site []. The overall fold consists of two six-stranded mixed β-sheets surrounded by nine α-helices and a β-ribbon covering the exposed edge strand of one sheet.
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Protein Domain
IPR039672 | MFS_2
Type: Family
Description: This family includes lactose permease (LacY) and its homologues that are members of the sodium:galactoside symporter (TC 2.A.2) family. LacY is found in Firmicute bacteria such as Streptococcus thermophilus, and is required for transport of beta-galactosides into the cell. Cations are co-transported. LacY contains a PTS EIIA type-1 domain, which may be regulatory. It is an integral membrane protein with many transmembrane regions []. Other homologues in this family include the melibiose carrier protein (MelB) from Escherichia coli, which is required for the transport of melibiose and other galactosides []; glucuronide carrier protein (UidB or GusB), also from E.coli, which transports glucuronide (but is inactive in some strains) []; and isoprimeverose transporter (XylP) from Lactobacillus pentosus, which transports isoprimeverose []. A human member of this family, MFSD12, has been recently characterised as a transporter that mediates the import of cysteine into melanosomes, thereby regulating skin pigmentation []. In melanosomes, cysteine import is required both for normal levels of cystine, the oxidized dimer of cysteine, and provide cysteine for the production of the cysteinyldopas used in pheomelanin synthesis, thereby regulating skin pigmentation []. In non-pigmented cells, it catalyses the import of cysteine into lysosomes [].
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Publication
15925194 | J:98742
First Author: Harding GW
Year: 2005
Journal: Hear Res
Title: The effect of an age-related hearing loss gene (Ahl) on noise-induced hearing loss and cochlear damage from low-frequency noise.
Volume: 204
Issue: 1-2
Pages: 90-100
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Publication
15276680 | J:117746
First Author: Vázquez AE
Year: 2004
Journal: Hear Res
Title: Evaluating cochlear function and the effects of noise exposure in the B6.CAST+Ahl mouse with distortion product otoacoustic emissions.
Volume: 194
Issue: 1-2
Pages: 87-96
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Publication
1488615 | J:281139
 
First Author: Li HS
Year: 1992
Journal: Scand Audiol Suppl
Title: Genetic influences on susceptibility of the auditory system to aging and environmental factors.
Volume: 36
Pages: 1-39
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Publication
1732212 | -
First Author: el Hassouni M
Year: 1992
Journal: J Bacteriol
Title: Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.
Volume: 174
Issue: 3
Pages: 765-77
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Publication
9045813 | -
First Author: Alpert CA
Year: 1997
Journal: J Bacteriol
Title: The lac operon of Lactobacillus casei contains lacT, a gene coding for a protein of the Bg1G family of transcriptional antiterminators.
Volume: 179
Issue: 5
Pages: 1555-62
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Publication
11751049 | -
First Author: van Tilbeurgh H
Year: 2001
Journal: Curr Opin Struct Biol
Title: Structural insights into the regulation of bacterial signalling proteins containing PRDs.
Volume: 11
Issue: 6
Pages: 685-93
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Publication
11733988 | -
First Author: Declerck N
Year: 2001
Journal: J Mol Biol
Title: Dimer stabilization upon activation of the transcriptional antiterminator LicT.
Volume: 314
Issue: 4
Pages: 671-81
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Publication
15699035 | -
First Author: Graille M
Year: 2005
Journal: J Biol Chem
Title: Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.
Volume: 280
Issue: 15
Pages: 14780-9
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Publication
9202047 | -
First Author: Tortosa P
Year: 1997
Journal: J Biol Chem
Title: Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.
Volume: 272
Issue: 27
Pages: 17230-7
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Publication
9663674 | -
First Author: Stülke J
Year: 1998
Journal: Mol Microbiol
Title: PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria.
Volume: 28
Issue: 5
Pages: 865-74
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Publication
25564559 | -
First Author: Li H
Year: 2015
Journal: Plant Physiol
Title: A heteromeric membrane-bound prenyltransferase complex from hop catalyzes three sequential aromatic prenylations in the bitter acid pathway.
Volume: 167
Issue: 3
Pages: 650-9
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Publication
11606046 | -
First Author: Ito R
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Temperature-sensitive phenotype of Chinese hamster ovary cells defective in PEX5 gene.
Volume: 288
Issue: 2
Pages: 321-7
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Publication
16428307 | -
First Author: Ito R
Year: 2005
Journal: J Biochem
Title: Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA oxidase in CHO cells expressing mutant Pex5p isoforms.
Volume: 138
Issue: 6
Pages: 781-90
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Publication
11865044 | -
First Author: Otera H
Year: 2002
Journal: Mol Cell Biol
Title: Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import.
Volume: 22
Issue: 6
Pages: 1639-55
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Publication
11463335 | J:188908
First Author: Amery L
Year: 2001
Journal: Biochem J
Title: Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals.
Volume: 357
Issue: Pt 3
Pages: 635-46
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Protein Domain
IPR036634 | PRD_sf
Type: Homologous_superfamily
Description: Transcriptional antiterminators and activators containing phosphoenolpyruvate: sugar phosphotransferase system (PTS) regulation domains (PRDs) form a class of bacterial regulatory proteins whose activity is modulated by phosphorylation. These regulators stimulate the expression of genes and operons involved in carbohydrate metabolism.PRD-containing proteins are involved in the regulation of catabolic operons in Gram-positive and Gram-negative bacteria [, ]and are often characterised by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators, ) or DNA (for activators), and a duplicated PRD module which is phosphorylated on conserved histidines by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations are thought to modify the stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain [, , ]. PRDs are characterised by the presence of a duplicated regulatory module of ~100 residues that can be reversibly phosphorylated on histidyl residues by the PTS. PRDs in transcriptional antiterminators and activators are PTS regulatory targets that are (de)phosphorylated in response to the availability of carbon sources [, , , , ].The PRD domain comprises one and often two highly conserved histidines. It forms a compact bundle comprising five helices (alpha1-alpha5). The core of the PRD module consists of two pairs of antiparallel helices making an angle of ~60 degrees. The first pair contains the antiparallel helices alpha1 and alpha4, while the second pair contains alpha2 and alpha5. The third helix (alpha3) is oriented perpendicularly to alpha5 at the periphery of the bundle. The helices are connected by loops of varying length [, , ].
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Protein Domain
IPR011608 | PRD
Type: Domain
Description: Transcriptional antiterminators and activators containing phosphoenolpyruvate: sugar phosphotransferase system (PTS) regulation domains (PRDs) form a class of bacterial regulatory proteins whose activity is modulated by phosphorylation. These regulators stimulate the expression of genes and operons involved in carbohydrate metabolism.PRD-containing proteins are involved in the regulation of catabolic operons in Gram-positive and Gram-negative bacteria [, ]and are often characterised by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators, ) or DNA (for activators), and a duplicated PRD module which is phosphorylated on conserved histidines by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations are thought to modify the stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain [, , ]. PRDs are characterised by the presence of a duplicated regulatory module of ~100 residues that can be reversibly phosphorylated on histidyl residues by the PTS. PRDs in transcriptional antiterminators and activators are PTS regulatory targets that are (de)phosphorylated in response to the availability of carbon sources [, , , , ].The PRD domain comprises one and often two highly conserved histidines. It forms a compact bundle comprising five helices (alpha1-alpha5). The core of the PRD module consists of two pairs of antiparallel helices making an angle of ~60 degrees. The first pair contains the antiparallel helices alpha1 and alpha4, while the second pair contains alpha2 and alpha5. The third helix (alpha3) is oriented perpendicularly to alpha5 at the periphery of the bundle. The helices are connected by loops of varying length [, , ].
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Protein
Q9DA75
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q3T9M1
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
Q3U481
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Protein
B8JK42
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
B8JK43
Organism: Mus musculus/domesticus
Length: 494  
Fragment?: false
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Protein
D6RJ45
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Publication
12813127 | -
First Author: Siebold C
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase.
Volume: 100
Issue: 14
Pages: 8188-92
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Publication
8955298 | -
First Author: Nobelmann B
Year: 1996
Journal: J Bacteriol
Title: Molecular analysis of the gat genes from Escherichia coli and of their roles in galactitol transport and metabolism.
Volume: 178
Issue: 23
Pages: 6790-5
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Publication
8418825 | -
 
First Author: Danchin A
Year: 1993
Journal: Adv Second Messenger Phosphoprotein Res
Title: Phylogeny of adenylyl cyclases.
Volume: 27
Pages: 109-62
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Publication
7863008 | -
 
First Author: Bârzu O
Year: 1994
Journal: Prog Nucleic Acid Res Mol Biol
Title: Adenylyl cyclases: a heterogeneous class of ATP-utilizing enzymes.
Volume: 49
Pages: 241-83
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Protein
O09012
Organism: Mus musculus/domesticus
Length: 639  
Fragment?: false
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Protein
D3Z600
Organism: Mus musculus/domesticus
Length: 632  
Fragment?: false
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Publication
12966101 | -
First Author: Siebold C
Year: 2003
Journal: J Biol Chem
Title: Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain.
Volume: 278
Issue: 48
Pages: 48236-44
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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