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Search results 601 to 700 out of 711 for Furin

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Type Details Score
Protein
Q547J8
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
Q32MU0
Organism: Mus musculus/domesticus
Length: 753  
Fragment?: false
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Protein
Q3UZV3
Organism: Mus musculus/domesticus
Length: 619  
Fragment?: false
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Protein
Q3TT48
Organism: Mus musculus/domesticus
Length: 736  
Fragment?: true
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Protein
H3BJL4
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: true
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Protein
F6XJP7
Organism: Mus musculus/domesticus
Length: 959  
Fragment?: false
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Protein
Q62030
Organism: Mus musculus/domesticus
Length: 932  
Fragment?: true
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Protein
Q3TYM6
Organism: Mus musculus/domesticus
Length: 637  
Fragment?: false
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Protein
Q91VK0
Organism: Mus musculus/domesticus
Length: 915  
Fragment?: false
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Protein
E9Q4D0
Organism: Mus musculus/domesticus
Length: 946  
Fragment?: false
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Protein
Q8BI61
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
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Protein
A0A1L1STL8
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
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Publication
2984314 | -
 
First Author: Binns MM
Year: 1985
Journal: J Gen Virol
Title: Cloning and sequencing of the gene encoding the spike protein of the coronavirus IBV.
Volume: 66 ( Pt 4)
Pages: 719-26
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Publication
29458023 | -
First Author: Zhang W
Year: 2018
Journal: Biochem Biophys Res Commun
Title: Structural characterization of the HCoV-229E fusion core.
Volume: 497
Issue: 2
Pages: 705-712
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Publication
30198895 | -
First Author: Yan L
Year: 2018
Journal: Acta Crystallogr D Struct Biol
Title: Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Volume: 74
Issue: Pt 9
Pages: 841-851
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Protein Domain
IPR000209 | Peptidase_S8/S53_dom
Type: Domain
Description: These proteins contain a domain found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin) and S53 (sedolisin), both of which are members of clan SB [].The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence []. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses []. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [, ]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [, ]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [].The proprotein-processing endopeptidases kexin, furin and related enzymesform a distinct subfamily known as the kexin subfamily (S8B). These preferentially cleave C-terminally to paired basic amino acids. Members of this subfamily can be identified by subtly different motifs around the active site [, ]. Members of the kexin subfamily, along with endopeptidases R, T and K from the yeast Tritirachium and cuticle-degrading peptidase from Metarhizium, require thiol activation. This can be attributed to the presence of a cysteine near to the active site histidine []. Only one viral member of the subtilisin family is known, a 56kDa protease from herpes virus 1, which infects the channel catfish []. Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus sp. MN-32. Mutations in the human gene leads to a fatal neurodegenerative disease [].
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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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Protein Domain
IPR036852 | Peptidase_S8/S53_dom_sf
Type: Homologous_superfamily
Description: These proteins contain a domain superfamily found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin) and S53 (sedolisin), both of which are members of clan SB [].The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence []. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses []. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [, ]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [, ]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [].The proprotein-processing endopeptidases kexin, furin and related enzymesform a distinct subfamily known as the kexin subfamily (S8B). These preferentially cleave C-terminally to paired basic amino acids. Members of this subfamily can be identified by subtly different motifs around the active site [, ]. Members of the kexin subfamily, along with endopeptidases R, T and K from the yeast Tritirachium and cuticle-degrading peptidase from Metarhizium, require thiol activation. This can be attributed to the presence of a cysteine near to the active site histidine []. Only one viral member of the subtilisin family is known, a 56kDa protease from herpes virus 1, which infects the channel catfish []. Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus sp. MN-32. Mutations in the human gene leads to a fatal neurodegenerative disease [].
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Protein
Q3V3M8
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
A0A1Y7VJY7
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: true
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Protein
M0QW95
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Protein
Q3V451
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
Q8BNF3
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: false
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Protein
Q5PYH4
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Publication
10627571 | -
First Author: Godeke GJ
Year: 2000
Journal: J Virol
Title: Assembly of spikes into coronavirus particles is mediated by the carboxy-terminal domain of the spike protein.
Volume: 74
Issue: 3
Pages: 1566-71
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Publication
10725213 | -
First Author: Chang KW
Year: 2000
Journal: Virology
Title: Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein.
Volume: 269
Issue: 1
Pages: 212-24
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Publication
19321428 | -
First Author: Belouzard S
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites.
Volume: 106
Issue: 14
Pages: 5871-6
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Publication
25445340 | -
 
First Author: Millet JK
Year: 2015
Journal: Virus Res
Title: Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis.
Volume: 202
Pages: 120-34
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Publication
26206723 | -
First Author: Lu G
Year: 2015
Journal: Trends Microbiol
Title: Bat-to-human: spike features determining 'host jump' of coronaviruses SARS-CoV, MERS-CoV, and beyond.
Volume: 23
Issue: 8
Pages: 468-78
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Publication
32057769 | -
 
First Author: Coutard B
Year: 2020
Journal: Antiviral Res
Title: The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade.
Volume: 176
Pages: 104742
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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
19801669 | -
First Author: Shulla A
Year: 2009
Journal: J Biol Chem
Title: Role of spike protein endodomains in regulating coronavirus entry.
Volume: 284
Issue: 47
Pages: 32725-34
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Protein Domain
IPR043614 | Spike_S2_CoV_C
Type: Domain
Description: The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM or cytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the cysteine rich intravirion region found at the C-terminal of coronavirus spike proteins (S) []. These cysteine residues are targets for palmitoylation, necessary for efficiently S incorporation into virions and S-mediated membrane fusions.
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Protein Domain
IPR044873 | Spike_S2_CoV_HR1
Type: Domain
Description: The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM or cytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the heptad repeat 1 (HR1) from coronavirus Spike glycoprotein, S2 subunit. This region forms a long trimeric helical coiled-coil structure with peptides from the HR2 region packing in an oblique antiparallel manner on the grooves of the HR1 trimer in a mixed extended and helical conformation. Packing of the helical parts of HR2 on the HR1 trimer grooves and formation of a six-helical bundle plays an important role in the formation of a stable post-fusion structure. In contrast to their extended helical conformations in the post-fusion state, the HR1 motifs within S2 form several shorter helices in their pre-fusion state [, ].
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Protein Domain
IPR044874 | Spike_S2_CoV_HR2
Type: Domain
Description: The type I glycoprotein S of Coronavirus, trimers of which constitute the typical viral spikes, is assembled into virions through noncovalent interactions with the M protein. The spike glycoprotein is translated as a large polypeptide that is subsequently cleaved to S1 () and S2 []. The cleavage of S can occur at two distinct sites: S2 or S2' []. The spike is present in two very different forms: pre-fusion (the form on mature virions) and post-fusion (the form after membrane fusion has been completed). The spike is cleaved sequentially by host proteases at two sites: first at the S1/S2 boundary (i.e. S1/S2 site) and second within S2 (i.e. S2' site). After the cleavages, S1 dissociates from S2, allowing S2 to transition to the post-fusion structure []. Both chimeric S proteins appeared to cause cell fusion when expressed individually, suggesting that they were biologically fully active []. The spike is a type I membrane glycoprotein that possesses a conserved transmembrane anchor and an unusual cysteine-rich (cys) domain that bridges the putative junction of the anchor and the cytoplasmic tail [].SARS-CoV S is largely uncleaved after biosynthesis. It can be later processed by endosomal cathepsin L, trypsin, thermolysin, and elastase, which are shown to induce syncytia formation and virus entry. Other proteases that are of potential biological relevance in potentiating SARS-CoV S include TMPRSS2, TMPRSS11a, and HAT which are localized on the cell surface and are highly expressed in the human airway []. The furin-like S2' cleavage site at KR/SF with P1 and P2 basic residues and a P2' hydrophobic Phe downstream of the IFP is identical between the SARS-CoV-2 and SARS-CoV. One or more furin-like enzymes would cleave the S2' site at KR/SF [, ]. Deletion of SARS-CoV-2 furin cleavage site suggests that it may not be required for viral entry but may affect replication kinetics and altered sites have been still seen proteolytically cleaved. Several substitutions within the S2' cleavage domain of SARS-COV-2 have been reported, including P812L/S/T, S813I/G, F817L, I818S/V, but further experimental study of their consequences and the replication properties of the altered viruses are required to understand the role of furin cleavage in SARS-CoV-2 infection and virulence []. The S2 subunit normally contains multiple key components, including one or more fusion peptides (FP), a second proteolytic site (S2') and two conserved heptad repeats (HRs), driving membrane penetration and virus-cell fusion. The HRs can trimerize into a coiled-coil structure built of three HR1-HR2 helical hairpins presenting as a canonical six-helix bundle and drag the virus envelope and the host cell bilayer into close proximity, preparing for fusion to occur []. The fusion core is composed of HR1 and HR2 and at least three membranotropic regions that are denoted as the fusion peptide (FP), internal fusion peptide (IFP), and pretransmembrane domain (PTM). The HR regions are further flanked by the three membranotropic components. Both FP and IFP are located upstream of HR1, while PTM is distally downstream of HR2 and directly precedes the transmembrane domain of SARS-CoV S. All of these three components are able to partition into the phospholipid bilayer to disturb membrane integrity. []. During the pandemic, many conservative amino acid changes in FP segment of SARS-CoV-2 have been reported (i.e., L821I, L822F, K825R, V826L, T827I, L828P, A829T, D830G/A, A831V/S/T, G832C/S, F833S, I834T), although their impact is not known as the active conformation and mode of insertion of SARS-CoV-2 fusion peptide have not been experimentally characterised. Differences in HR1 sequences between SARS-CoV and SARS-CoV-2 suggest that SARS-CoV-2 HR2 makes stronger interactions with HR1. However, the substitutions observed in the solvent accessible surface of the HR1 domain (e.g., D936Y, S943P, S939F) of SARS-CoV-2 do not seem to be involved in stabilizing interactions with HR2. Substitutions in HR2 (e.g., K1073N, V1176F) or the TM orcytoplasmic tail domains have also been observed, but further experimental work is required to determine the effects of these changes [].This entry represents the heptad repeat 2 (HR2) from coronavirus Spike glycoprotein, S2 subunit. It adopts a mixed conformation: the central part fold into a nine-turn α-helix, while the residues on either side of the helix adopt an extended conformation. Packing of the helical parts of HR2 on the HR1 trimer grooves and formation of a six-helical bundle plays an important role in the formation of a stable post-fusion structure [, ].
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Protein
Q6PHU5
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
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Protein
O89023
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
Q80UF6
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q3U2Z6
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
Q3U2X9
Organism: Mus musculus/domesticus
Length: 780  
Fragment?: true
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Protein
Q3TDY6
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Publication
2106512 | -
First Author: Sloma A
Year: 1990
Journal: J Bacteriol
Title: Bacillopeptidase F of Bacillus subtilis: purification of the protein and cloning of the gene.
Volume: 172
Issue: 3
Pages: 1470-7
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Publication
26497454 | -
First Author: Meng D
Year: 2015
Journal: Appl Environ Microbiol
Title: Maturation of Fibrinolytic Bacillopeptidase F Involves both Hetero- and Autocatalytic Processes.
Volume: 82
Issue: 1
Pages: 318-27
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Protein Domain
IPR033857 | Bacillopeptidase_F
Type: Domain
Description: Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth []. The ones that make up this group are known as bacillopeptidase F (MEROPS identifier S08.017), encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF []. Bacillopeptidase F is fibrinolytic and is synthesized as a precursor, which is either activated autocatalytically or by another, unidentified B. subtilis peptidase []. Like other members of the peptidases S8 family these have a Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity [].These proteins contain a domain found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin) and S53 (sedolisin), both of which are members of clan SB [].The subtilisin family is one of the largest serine peptidase families characterised to date. Over 200 subtilises are presently known, more than 170 of which with their complete amino acid sequence []. It is widespread, being found in eubacteria, archaebacteria, eukaryotes and viruses []. The vast majority of the family are endopeptidases, although there is an exopeptidase, tripeptidyl peptidase [, ]. Structures have been determined for several members of the subtilisin family: they exploit the same catalytic triad as the chymotrypsins, although the residues occur in a different order (HDS in chymotrypsin and DHS in subtilisin), but the structures show no other similarity [, ]. Some subtilisins are mosaic proteins, while others contain N- and C-terminal extensions that show no sequence similarity to any other known protein [].The proprotein-processing endopeptidases kexin, furin and related enzymesform a distinct subfamily known as the kexin subfamily (S8B). These preferentially cleave C-terminally to paired basic amino acids. Members of this subfamily can be identified by subtly different motifs around the active site [, ]. Members of the kexin subfamily, along with endopeptidases R, T and K from the yeast Tritirachium and cuticle-degrading peptidase from Metarhizium, require thiol activation. This can be attributed to the presence of a cysteine near to the active site histidine []. Only one viral member of the subtilisin family is known, a 56kDa protease from herpes virus 1, which infects the channel catfish []. Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus sp. MN-32. Mutations in the human gene leads to a fatal neurodegenerative disease [].
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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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Protein
Q05DJ9
Organism: Mus musculus/domesticus
Length: 607  
Fragment?: false
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Protein
M0QWG0
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: false
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Protein
Q8BRQ2
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
Q3U4M7
Organism: Mus musculus/domesticus
Length: 1249  
Fragment?: false
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Protein
H3BLN2
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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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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Publication
21458307 | J:171379
First Author: Shi C
Year: 2011
Journal: Immunity
Title: Bone marrow mesenchymal stem and progenitor cells induce monocyte emigration in response to circulating toll-like receptor ligands.
Volume: 34
Issue: 4
Pages: 590-601
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Publication
38014224 | J:350002
     
First Author: James RE
Year: 2023
Journal: bioRxiv
Title: Semaphorin 6A in Retinal Ganglion Cells Regulates Functional Specialization of the Inner Retina.
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Protein
Q80W65
Organism: Mus musculus/domesticus
Length: 694  
Fragment?: false
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Protein
Q9WTZ2
Organism: Mus musculus/domesticus
Length: 1052  
Fragment?: false
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Protein
O89001
Organism: Mus musculus/domesticus
Length: 1377  
Fragment?: false
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Protein
Q64514
Organism: Mus musculus/domesticus
Length: 1262  
Fragment?: false
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Protein
Q3TB11
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: true
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Publication
32150576 | J:296119
First Author: Shang J
Year: 2020
Journal: PLoS Pathog
Title: Structure of mouse coronavirus spike protein complexed with receptor reveals mechanism for viral entry.
Volume: 16
Issue: 3
Pages: e1008392
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Protein
Q3TW28
Organism: Mus musculus/domesticus
Length: 1249  
Fragment?: false
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Protein
A0A087WRC0
Organism: Mus musculus/domesticus
Length: 883  
Fragment?: false
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Protein
Q80U80
Organism: Mus musculus/domesticus
Length: 1055  
Fragment?: true
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Protein
Q3UHA7
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: false
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Protein
A3QWY0
Organism: Mus musculus/domesticus
Length: 1052  
Fragment?: false
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Publication
8420571 | -
First Author: Van de Ven WJ
Year: 1993
Journal: Crit Rev Oncog
Title: Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases.
Volume: 4
Issue: 2
Pages: 115-36
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Publication
9070434 | -
First Author: Siezen RJ
Year: 1997
Journal: Protein Sci
Title: Subtilases: the superfamily of subtilisin-like serine proteases.
Volume: 6
Issue: 3
Pages: 501-23
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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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Protein
Q9R0X2
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
Q9EPR5
Organism: Mus musculus/domesticus
Length: 1159  
Fragment?: false
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Protein
Q8VI51
Organism: Mus musculus/domesticus
Length: 1219  
Fragment?: false
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Protein
Q9JLC4
Organism: Mus musculus/domesticus
Length: 1167  
Fragment?: false
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Protein
Q1HL23
Organism: Mus musculus/domesticus
Length: 1148  
Fragment?: false
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Protein
Q8BSV0
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
E9QQ02
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
E9PYT6
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
A0A1B0GRB7
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
A0A1B0GT94
Organism: Mus musculus/domesticus
Length: 1148  
Fragment?: false
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Protein
A0A1B0GRN1
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
Q1HL24
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
Q1HL22
Organism: Mus musculus/domesticus
Length: 1219  
Fragment?: false
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Protein
A0A1B0GRC4
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
Q3U0T4
Organism: Mus musculus/domesticus
Length: 467  
Fragment?: false
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Protein
E9QQ63
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
Q1HL25
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
Q8CHA4
Organism: Mus musculus/domesticus
Length: 1185  
Fragment?: true
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Publication
12673349 | -
First Author: Wlodawer A
Year: 2003
Journal: Acta Biochim Pol
Title: Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.
Volume: 50
Issue: 1
Pages: 81-102
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Protein
O88839
Organism: Mus musculus/domesticus
Length: 864  
Fragment?: false
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Protein
Q3TD57
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
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Protein
Q8CA82
Organism: Mus musculus/domesticus
Length: 809  
Fragment?: true
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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
34580920 | -
First Author: Lubin JH
Year: 2022
Journal: Proteins
Title: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic.
Volume: 90
Issue: 5
Pages: 1054-1080
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Protein
O35674
Organism: Mus musculus/domesticus
Length: 920  
Fragment?: false
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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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