Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
Not Specified |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chicken |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
zebrafish |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This domain can be found in many bacterial hypothetical proteins. The structures of , PDB:3hsa, and , PDB:3dcx, show similarities to the PH or pleckstrin homology domain. First evidence of PH-like domains in bacteria suggests role in cell envelope stress response []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Xu Q |
Year: |
2010 |
Journal: |
J Mol Biol |
Title: |
Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain. |
Volume: |
396 |
Issue: |
1 |
Pages: |
31-46 |
|
•
•
•
•
•
|
Ontology Term |
|
•
•
•
•
•
|
Author |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang LF |
Year: |
2020 |
Journal: |
Nucleic Acids Res |
Title: |
PHB regulates meiotic recombination via JAK2-mediated histone modifications in spermatogenesis. |
Volume: |
48 |
Issue: |
9 |
Pages: |
4780-4796 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the C terminus of bacterial poly(3-hydroxybutyrate) (PHB) de-polymerase. This degrades PHB granules to oligomers and monomers of 3-hydroxy-butyric acid. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
399
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
282
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Prieto MA |
Year: |
1999 |
Journal: |
J Bacteriol |
Title: |
PhaF, a polyhydroxyalkanoate-granule-associated protein of Pseudomonas oleovorans GPo1 involved in the regulatory expression system for pha genes. |
Volume: |
181 |
Issue: |
3 |
Pages: |
858-68 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gordillo F |
Year: |
2006 |
Journal: |
Mycol Res |
Title: |
Penicillium purpurogenum produces a family 1 acetyl xylan esterase containing a carbohydrate-binding module: characterization of the protein and its gene. |
Volume: |
110 |
Issue: |
Pt 10 |
Pages: |
1129-39 |
|
•
•
•
•
•
|
Publication |
First Author: |
Garcia-Conesa MT |
Year: |
2004 |
Journal: |
J Biotechnol |
Title: |
The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity. |
Volume: |
108 |
Issue: |
3 |
Pages: |
227-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Saito T |
Year: |
1989 |
Journal: |
J Bacteriol |
Title: |
Cloning, nucleotide sequence, and expression in Escherichia coli of the gene for poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis. |
Volume: |
171 |
Issue: |
1 |
Pages: |
184-9 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry describes a group of lipases, including bacterial depolymerases for poly(3-hydroxybutyrate) (PHB) []and related polyhydroxyalkanoates (PHA), as well as acetyl xylan esterases [], and feruloyl esterases from fungi []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The proteins this domain is found in are typically involved in regulating polymer accumulation in bacteria, for example the production of poly-beta-hydroxybutyrate (PHB) which is formed via the polymerisation of D(-)-3-hydroxybutyryl-CoA []. The function ofthis domain is unknown. |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
272
|
Fragment?: |
false |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Sugiyama A |
Year: |
2004 |
Journal: |
Curr Microbiol |
Title: |
Roles of poly(3-hydroxybutyrate) depolymerase and 3HB-oligomer hydrolase in bacterial PHB metabolism. |
Volume: |
48 |
Issue: |
6 |
Pages: |
424-7 |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Publication |
First Author: |
Cai GQ |
Year: |
2000 |
Journal: |
J Bacteriol |
Title: |
Requirement for the enzymes acetoacetyl coenzyme A synthetase and poly-3-hydroxybutyrate (PHB) synthase for growth of Sinorhizobium meliloti on PHB cycle intermediates. |
Volume: |
182 |
Issue: |
8 |
Pages: |
2113-8 |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
GO Term |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion KL287, GENSAT Project at Rockefeller University |
Allele Type: |
Transgenic |
Attribute String: |
Reporter |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant stock, transgenic |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Members of this family are transcriptional regulatory proteins found in the vicinity of poly-beta-hydroxybutyrate (PHB) operons in several species of Bacillus. This protein appears to have repressor activity modulated by PHB itself. This protein belongs to the larger PadR family. |
|
•
•
•
•
•
|
Publication |
First Author: |
Garzia L |
Year: |
2018 |
Journal: |
Cell |
Title: |
A Hematogenous Route for Medulloblastoma Leptomeningeal Metastases. |
Volume: |
172 |
Issue: |
5 |
Pages: |
1050-1062.e14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Richter-Dennerlein R |
Year: |
2014 |
Journal: |
Cell Metab |
Title: |
DNAJC19, a mitochondrial cochaperone associated with cardiomyopathy, forms a complex with prohibitins to regulate cardiolipin remodeling. |
Volume: |
20 |
Issue: |
1 |
Pages: |
158-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Fernandez DC |
Year: |
2018 |
Journal: |
Cell |
Title: |
Light Affects Mood and Learning through Distinct Retina-Brain Pathways. |
Volume: |
175 |
Issue: |
1 |
Pages: |
71-84.e18 |
|
•
•
•
•
•
|
Publication |
First Author: |
Weil T |
Year: |
2022 |
Journal: |
Sci Adv |
Title: |
Daily changes in light influence mood via inhibitory networks within the thalamic perihabenular nucleus. |
Volume: |
8 |
Issue: |
23 |
Pages: |
eabn3567 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li Y |
Year: |
2016 |
Journal: |
Immunity |
Title: |
Analysis of the Rab GTPase Interactome in Dendritic Cells Reveals Anti-microbial Functions of the Rab32 Complex in Bacterial Containment. |
Volume: |
44 |
Issue: |
2 |
Pages: |
422-37 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ande SR |
Year: |
2009 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Prohibitin interacts with phosphatidylinositol 3,4,5-triphosphate (PIP3) and modulates insulin signaling. |
Volume: |
390 |
Issue: |
3 |
Pages: |
1023-8 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
The band-7 protein family comprises a diverse set of membrane-bound proteins characterised by the presence of a conserved domain, the band-7 domain, also known as SPFH or PHB domain []. The exact function of the band-7 domain is not known, but examples from animal and bacterial stomatin-type proteins demonstrate binding to lipids and the ability to assemble into membrane-bound oligomers that form putative scaffolds []. A variety of proteins belong to this family. These include the prohibitins, cytoplasmic anti-proliferative proteins and stomatin, an erythrocyte membrane protein. Bacterial HflC protein also belongs to this family.Note: Band 4.1 and Band 7 proteins refer to human erythrocyte membrane proteins separated by SDS polyacrylamide gels and stained with coomassie blue []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
340
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
348
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
158
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
185
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
220
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Ande SR |
Year: |
2014 |
Journal: |
Diabetes |
Title: |
Prohibitin overexpression in adipocytes induces mitochondrial biogenesis, leads to obesity development, and affects glucose homeostasis in a sex-specific manner. |
Volume: |
63 |
Issue: |
11 |
Pages: |
3734-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
He B |
Year: |
2008 |
Journal: |
Mol Endocrinol |
Title: |
A repressive role for prohibitin in estrogen signaling. |
Volume: |
22 |
Issue: |
2 |
Pages: |
344-60 |
|
•
•
•
•
•
|
Publication |
First Author: |
He B |
Year: |
2011 |
Journal: |
Endocrinology |
Title: |
Estrogen-regulated prohibitin is required for mouse uterine development and adult function. |
Volume: |
152 |
Issue: |
3 |
Pages: |
1047-56 |
|
•
•
•
•
•
|
Publication |
First Author: |
Savulescu D |
Year: |
2013 |
Journal: |
Mol Endocrinol |
Title: |
Gonadotropin-releasing hormone-regulated prohibitin mediates apoptosis of the gonadotrope cells. |
Volume: |
27 |
Issue: |
11 |
Pages: |
1856-70 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yang C |
Year: |
2012 |
Journal: |
Genetics |
Title: |
Targeting of >1.5 Mb of human DNA into the mouse X chromosome reveals presence of cis-acting regulators of epigenetic silencing. |
Volume: |
192 |
Issue: |
4 |
Pages: |
1281-93 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nguyen KH |
Year: |
2016 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Obesity-related abnormalities couple environmental triggers with genetic susceptibility in adult-onset T1D. |
Volume: |
470 |
Issue: |
1 |
Pages: |
94-100 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rao CV |
Year: |
2020 |
Journal: |
Aging Cell |
Title: |
GSK3-ARC/Arg3.1 and GSK3-Wnt signaling axes trigger amyloid-β accumulation and neuroinflammation in middle-aged Shugoshin 1 mice. |
Volume: |
19 |
Issue: |
10 |
Pages: |
e13221 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kathiria AS |
Year: |
2013 |
Journal: |
Am J Physiol Gastrointest Liver Physiol |
Title: |
Nrf2 is not required for epithelial prohibitin-dependent attenuation of experimental colitis. |
Volume: |
304 |
Issue: |
10 |
Pages: |
G885-96 |
|
•
•
•
•
•
|
Publication |
First Author: |
Goo HG |
Year: |
2014 |
Journal: |
Exp Cell Res |
Title: |
HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis. |
Volume: |
328 |
Issue: |
2 |
Pages: |
456-65 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ande SR |
Year: |
2016 |
Journal: |
Oncogene |
Title: |
Expression of a mutant prohibitin from the aP2 gene promoter leads to obesity-linked tumor development in insulin resistance-dependent manner. |
Volume: |
35 |
Issue: |
34 |
Pages: |
4459-70 |
|
•
•
•
•
•
|
Publication |
First Author: |
Morrow IC |
Year: |
2002 |
Journal: |
J Biol Chem |
Title: |
Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. |
Volume: |
277 |
Issue: |
50 |
Pages: |
48834-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Laviola G |
Year: |
1994 |
Journal: |
Psychopharmacology (Berl) |
Title: |
A mouse model of early social interactions after prenatal drug exposure: a genetic investigation. |
Volume: |
113 |
Issue: |
3-4 |
Pages: |
388-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huber TB |
Year: |
2006 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Podocin and MEC-2 bind cholesterol to regulate the activity of associated ion channels. |
Volume: |
103 |
Issue: |
46 |
Pages: |
17079-86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Theiss AL |
Year: |
2007 |
Journal: |
J Biol Chem |
Title: |
Interleukin-6 transcriptionally regulates prohibitin expression in intestinal epithelial cells. |
Volume: |
282 |
Issue: |
17 |
Pages: |
12804-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
Theiss AL |
Year: |
2009 |
Journal: |
Mol Biol Cell |
Title: |
Prohibitin inhibits tumor necrosis factor alpha-induced nuclear factor-kappa B nuclear translocation via the novel mechanism of decreasing importin alpha3 expression. |
Volume: |
20 |
Issue: |
20 |
Pages: |
4412-23 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kathiria AS |
Year: |
2012 |
Journal: |
Cancer Res |
Title: |
Prohibitin attenuates colitis-associated tumorigenesis in mice by modulating p53 and STAT3 apoptotic responses. |
Volume: |
72 |
Issue: |
22 |
Pages: |
5778-89 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zi Xu YX |
Year: |
2018 |
Journal: |
Cancer Lett |
Title: |
Prohibitin: A new player in immunometabolism and in linking obesity and inflammation with cancer. |
Volume: |
415 |
|
Pages: |
208-216 |
|
•
•
•
•
•
|
Publication |
First Author: |
Theiss AL |
Year: |
2009 |
Journal: |
Gastroenterology |
Title: |
Prohibitin is a novel regulator of antioxidant response that attenuates colonic inflammation in mice. |
Volume: |
137 |
Issue: |
1 |
Pages: |
199-208, 208.e1-6 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
353
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
212
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
286
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
287
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
299
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
241
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
104
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
207
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
217
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
196
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
271
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
299
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
192
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Too IHK |
Year: |
2018 |
Journal: |
PLoS Pathog |
Title: |
Prohibitin plays a critical role in Enterovirus 71 neuropathogenesis. |
Volume: |
14 |
Issue: |
1 |
Pages: |
e1006778 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
385
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
395
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
85
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
385
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
150
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
395
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
265
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
159
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
395
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
251
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Gehl B |
Year: |
2014 |
Journal: |
Front Plant Sci |
Title: |
Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly? |
Volume: |
5 |
|
Pages: |
141 |
|
•
•
•
•
•
|
Publication |
First Author: |
de Almeida A |
Year: |
2007 |
Journal: |
Appl Environ Microbiol |
Title: |
Effects of granule-associated protein PhaP on glycerol-dependent growth and polymer production in poly(3-hydroxybutyrate)-producing Escherichia coli. |
Volume: |
73 |
Issue: |
24 |
Pages: |
7912-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Neumann L |
Year: |
2008 |
Journal: |
J Bacteriol |
Title: |
Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules. |
Volume: |
190 |
Issue: |
8 |
Pages: |
2911-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pötter M |
Year: |
2004 |
Journal: |
Microbiology |
Title: |
The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha. |
Volume: |
150 |
Issue: |
Pt 7 |
Pages: |
2301-11 |
|
•
•
•
•
•
|
Publication |
First Author: |
Korotkova N |
Year: |
2002 |
Journal: |
J Bacteriol |
Title: |
Poly-beta-hydroxybutyrate biosynthesis in the facultative methylotroph methylobacterium extorquens AM1: identification and mutation of gap11, gap20, and phaR. |
Volume: |
184 |
Issue: |
22 |
Pages: |
6174-81 |
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Protein Domain |
Type: |
Domain |
Description: |
Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry describes a group of phasins that associate with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). |
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Protein Domain |
Type: |
Family |
Description: |
Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. Members of this entry are encoded in polyhydroxyalkanoic acid storage system regions in a number of Vibrio species, including Vibrio cholerae V52, Photobacterium profundum SS9, Acinetobacter sp., and Aeromonas hydrophila. Members appear distantly related to the phasin family, see: and . |
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Protein Domain |
Type: |
Family |
Description: |
Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry describes a group of phasins associated with polyhydroxyalkanoate (PHA) inclusions, the most common of which consist of polyhydroxybutyrate (PHB). However, the member from Magnetospirillum sp. (strain AMB-1) is called a magnetic particle membrane-specific GTPase. |
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Protein Domain |
Type: |
Family |
Description: |
Phasins (or granule-associate proteins) are surface proteins found covering Polyhydroxyalkanoate (PHA) storage granules in bacteria. Polyhydroxyalkanoates are linear polyesters produced by bacterial fermentation of sugar or lipids for the purpose of storing carbon and energy, and are accumulated as intracellular granules by many bacteria under unfavorable conditions, enhancing their fitness and stress resistance []. The layer of phasins stabilises the granules and prevents coalescence of separated granules in the cytoplasm and nonspecific binding of other proteins to the hydrophobic surfaces of the granules. For example, in Ralstonia eutropha (strain ATCC 17699/H16/DSM 428/Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)), the major surface protein of polyhydroxybutyrate (PHB) granules is phasin PhaP1(Reu), which occurs along with three homologues (PhaP2, PhaP3, and PhaP4) that have the capacity to bind to PHB granules but are present at minor levels [, ]. These four phasins lack a highly conserved domain but share homologous hydrophobic regions. This entry represents a family of phasins that are part of the polyhydroxyalkanoate synthesis machinery []. Members of this family are related to . |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
428
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Fragment?: |
false |
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