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Search results 301 to 400 out of 432 for Arf1

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Type Details Score
Publication
9111317 | -
First Author: Santos B
Year: 1997
Journal: Mol Cell Biol
Title: CHS5, a gene involved in chitin synthesis and mating in Saccharomyces cerevisiae.
Volume: 17
Issue: 5
Pages: 2485-96
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Publication
16855022 | -
First Author: Sanchatjate S
Year: 2006
Journal: Mol Biol Cell
Title: Chs5/6 complex: a multiprotein complex that interacts with and conveys chitin synthase III from the trans-Golgi network to the cell surface.
Volume: 17
Issue: 10
Pages: 4157-66
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Publication
12058076 | -
First Author: Liu Y
Year: 2002
Journal: Mol Biol Cell
Title: The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly.
Volume: 13
Issue: 6
Pages: 2147-56
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Publication
11062263 | -
First Author: Jackson TR
Year: 2000
Journal: J Cell Biol
Title: ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.
Volume: 151
Issue: 3
Pages: 627-38
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Publication
15520000 | -
First Author: Amor JC
Year: 2005
Journal: J Biol Chem
Title: The structure of RalF, an ADP-ribosylation factor guanine nucleotide exchange factor from Legionella pneumophila, reveals the presence of a cap over the active site.
Volume: 280
Issue: 2
Pages: 1392-400
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Protein Domain
IPR031673 | Chs5_N
Type: Domain
Description: This domain is found at the N terminus of fungal chitin biosynthesis protein Chs5 []. It functions as a dimerisation domain [].Chs5/6 is a multi-protein complex conserved in fungi that interacts with chitin synthase III (Chs3p) and is involved in its transport to the cell surface from the trans-Golgi network, functioning as an exomer cargo adapter. Chs5p appears to form a complex with Chs6p and its paralogues Bch1p, Bud7p, and Bch2p. In this complex, Chs5p may act as a central scaffold []. The N-terminal domain characterized by this model forms a homodimer and has been shown to interact with Chs6p and Bch1p. It may function as a flexible hinge domain that allows the exomer to interact with both proteins and the Golgi membrane as the latter undergoes changes in curvature during the formation of transport vesicles []. The dimerization domain sits N-terminally to a conserved FBE (FN3-BRCT) unit, which binds Arf1 an is involved in the recruitment of the exomer to the membrane [].
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Protein Domain
IPR006689 | Small_GTPase_ARF/SAR
Type: Family
Description: Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [, ]. Sequence comparisons of small G proteins from various species have revealed that they are conserved in primary structures at the level of 30-55% similarity [].Crystallographic analysis of various small G proteins revealed the presence of a 20kDa catalytic domain that is unique for the whole superfamily [, ]. The domain is built of five alpha helices (A1-A5), six β-strands (B1-B6) and five polypeptide loops (G1-G5). A structural comparison of the GTP- and GDP-bound form, allows one to distinguish two functional loop regions: switch I and switch II that surround the gamma-phosphate group of the nucleotide. The G1 loop (also called the P-loop) that connects the B1 strand and the A1 helix is responsible for the binding of the phosphate groups. The G3 loop provides residues for Mg2 and phosphate binding and is located at the N terminus of the A2 helix. The G1 and G3 loops are sequentially similar to Walker A and Walker B boxes that are found in other nucleotide binding motifs. The G2 loop connects the A1 helix and the B2 strand and contains a conserved Thr residue responsible for Mg2 binding. The guanine base is recognised by the G4 and G5 loops. The consensus sequence NKXD of the G4 loop contains Lys and Asp residues directly interacting with the nucleotide. Part of the G5 loop located between B6 and A5 acts as a recognition site for the guanine base [].The small GTPase superfamily can be divided into at least 8 different families, including:Arf small GTPases. GTP-binding proteins involved in protein trafficking by modulating vesicle budding and uncoating within the Golgi apparatus.Ran small GTPases. GTP-binding proteins involved in nucleocytoplasmic transport. Required for the import of proteins into the nucleus and also for RNA export.Rab small GTPases. GTP-binding proteins involved in vesicular traffic.Rho small GTPases. GTP-binding proteins that control cytoskeleton reorganisation.Ras small GTPases. GTP-binding proteins involved in signalling pathways.Sar1 small GTPases. Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER).Mitochondrial Rho (Miro). Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking.Roc small GTPases domain. Small GTPase domain always found associated with the COR domain.This entry represents a branch of the small GTPase superfamily that includes the ADP ribosylation factor Arf, Arl (Arf-like), Arp(Arf-related proteins) and the remotely related Sar (Secretion-associated and Ras-related) proteins. Arf proteins are major regulators of vesicle biogenesis in intracellular traffic []. They cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterised by conformational changes at the so-called switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes, they depart from other small GTP-binding proteins in that they use an additional, unique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2-beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N terminus. In GDP-boundArf1 and Arf6, the interswitch is retracted and forms a pocket to which the N-terminal helix binds, the latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP. In this conformation, the interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.
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Protein Domain
IPR024156 | Small_GTPase_ARF
Type: Family
Description: Small GTPases form an independent superfamily within the larger class of regulatory GTP hydrolases. This superfamily contains proteins that control a vast number of important processes and possess a common, structurally preserved GTP-binding domain [, ]. Sequence comparisons of small G proteins from various species have revealed that they are conserved in primary structures at the level of 30-55% similarity [].Crystallographic analysis of various small G proteins revealed the presence of a 20kDa catalytic domain that is unique for the whole superfamily [, ]. The domain is built of five alpha helices (A1-A5), six β-strands (B1-B6) and five polypeptide loops (G1-G5). A structural comparison of the GTP- and GDP-bound form, allows one to distinguish two functional loop regions: switch I and switch II that surround the gamma-phosphate group of the nucleotide. The G1 loop (also called the P-loop) that connects the B1 strand and the A1 helix is responsible for the binding of the phosphate groups. The G3 loop provides residues for Mg2 and phosphate binding and is located at the N terminus of the A2 helix. The G1 and G3 loops are sequentially similar to Walker A and Walker B boxes that are found in other nucleotide binding motifs. The G2 loop connects the A1 helix and the B2 strand and contains a conserved Thr residue responsible for Mg2 binding. The guanine base is recognised by the G4 and G5 loops. The consensus sequence NKXD of the G4 loop contains Lys and Asp residues directly interacting with the nucleotide. Part of the G5 loop located between B6 and A5 acts as a recognition site for the guanine base [].The small GTPase superfamily can be divided into at least 8 different families, including:Arf small GTPases. GTP-binding proteins involved in protein trafficking by modulating vesicle budding and uncoating within the Golgi apparatus.Ran small GTPases. GTP-binding proteins involved in nucleocytoplasmic transport. Required for the import of proteins into the nucleus and also for RNA export.Rab small GTPases. GTP-binding proteins involved in vesicular traffic.Rho small GTPases. GTP-binding proteins that control cytoskeleton reorganisation.Ras small GTPases. GTP-binding proteins involved in signalling pathways.Sar1 small GTPases. Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER).Mitochondrial Rho (Miro). Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking.Roc small GTPases domain. Small GTPase domain always found associated with the COR domain.This entry represents a branch of the small GTPase superfamily that includes the ADP ribosylation factor Arf, Arl (Arf-like), and Arp(Arf-related proteins). Arf proteins are major regulators of vesicle biogenesis in intracellular traffic []. They cycle between inactive GDP-bound and active GTP-bound forms that bind selectively to effectors. The classical structural GDP/GTP switch is characterised by conformational changes at the so-called switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide. Structural studies of Arf1 and Arf6 have revealed that although these proteins feature the switch 1 and 2 conformational changes, they depart from other small GTP-binding proteins in that they use an additional, unique switch to propagate structural information from one side of the protein to the other. The GDP/GTP structural cycles of human Arf1 and Arf6 feature a unique conformational change that affects the beta2-beta3 strands connecting switch 1 and switch 2 (interswitch) and also the amphipathic helical N terminus. In GDP-boundArf1 and Arf6, the interswitch is retracted and forms a pocket to which the N-terminal helix binds, the latter serving as a molecular hasp to maintain the inactive conformation. In the GTP-bound form of these proteins, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP. In this conformation, the interswitch projects out of the protein and extrudes the N-terminal hasp by occluding its binding pocket.
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Publication
12429613 | -
First Author: Pasqualato S
Year: 2002
Journal: EMBO Rep
Title: Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication.
Volume: 3
Issue: 11
Pages: 1035-41
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Publication
17850229 | -
First Author: Casanova JE
Year: 2007
Journal: Traffic
Title: Regulation of Arf activation: the Sec7 family of guanine nucleotide exchange factors.
Volume: 8
Issue: 11
Pages: 1476-85
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Protein
P61750
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
P84084
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
Q8BSL7
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
P61205
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
P84078
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q9DD04
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q3U344
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q14BR4
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
P62331
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
P61208
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
Q99PE9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
P61213
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
Q80ZU0
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q6P068
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q6P3A9
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: false
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Protein
P61211
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q9D4P0
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q3UGY8
Organism: Mus musculus/domesticus
Length: 2170  
Fragment?: false
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Protein
Q3SXC5
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
O88848
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q8BV33
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
Q3TIR2
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q3U0D7
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
Q4V9U3
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
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Protein
G3UVX1
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Protein
Q8BLF9
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
Q14AC7
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
F6UFB9
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
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Protein
E9Q2C2
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Protein
F8WIB1
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: true
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Protein
Q810L2
Organism: Mus musculus/domesticus
Length: 262  
Fragment?: true
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Protein
S4R1T9
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
Q3U6U3
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
E9Q798
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
A2A6T9
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: true
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Protein
Q99PN1
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: true
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Protein
Q3TE09
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
D6RJJ6
Organism: Mus musculus/domesticus
Length: 39  
Fragment?: false
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Protein
A0A0A6YXH4
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
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Protein
D3YV25
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
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Protein
Q8VCV3
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
E9Q006
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
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Protein
Q9D2Y8
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
A0A1N9M5I8
Organism: Mus musculus/domesticus
Length: 1709  
Fragment?: false
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Protein
D3Z067
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
Q3UUY4
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
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Protein
Q1LZJ1
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: true
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Protein
A2A541
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
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Protein
Q9D7H9
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
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Protein
Q3TUM2
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q498A0
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q6NXZ5
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
G3X9K3
Organism: Mus musculus/domesticus
Length: 1846  
Fragment?: false
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Protein
Q9D416
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein
Q8VEH3
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q9CQW2
Organism: Mus musculus/domesticus
Length: 186  
Fragment?: false
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Protein
Q9QXJ4
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
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Protein
Q8BGR6
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: false
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Protein
Q640N2
Organism: Mus musculus/domesticus
Length: 427  
Fragment?: false
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Protein
A2A5R2
Organism: Mus musculus/domesticus
Length: 1792  
Fragment?: false
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Protein
Q8BWY3
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
Q8BXL7
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
Q3U6V5
Organism: Mus musculus/domesticus
Length: 387  
Fragment?: false
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Protein
Q6IMB2
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
B1ATY8
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
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Protein
D3Z4X7
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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Protein
P70199
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: true
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Protein
Q3TF02
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
F7BE40
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
Q9DAB3
Organism: Mus musculus/domesticus
Length: 166  
Fragment?: false
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Protein
E9PZK7
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
F6ZTU1
Organism: Mus musculus/domesticus
Length: 54  
Fragment?: true
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Protein
F6QKK2
Organism: Mus musculus/domesticus
Length: 165  
Fragment?: true
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Protein
A0A338P6Z3
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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Protein
A0A0N4SVB8
Organism: Mus musculus/domesticus
Length: 138  
Fragment?: false
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Protein
F6Y333
Organism: Mus musculus/domesticus
Length: 31  
Fragment?: true
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Protein
Q9CUD0
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: true
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Protein
Q3TDF8
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
Q3TL10
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
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Protein
Q9D1Z5
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
Q3V3L8
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: false
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Protein
V9GX20
Organism: Mus musculus/domesticus
Length: 62  
Fragment?: false
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Protein
B7ZN40
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: false
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Protein
Q80SX7
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
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Protein
Q3U2F2
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: true
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Protein
Q8BYH5
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: true
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Protein
Q9WUL7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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Protein
Q9D0J4
Organism: Mus musculus/domesticus
Length: 184  
Fragment?: false
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Protein
Q543P7
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
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•
Protein
A0A494BAJ6
Organism: Mus musculus/domesticus
Length: 180  
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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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Cambridge CB2 3EH, United Kingdom