The domain within your query sequence starts at position 326 and ends at position 508; the E-value for the ARF domain shown below is 1.15e-78.
IPVTFTKDNRVHIGPKMEIRVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYK NLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVVDSSHRDRISEAHSELAKLLTEKELRDA LLLIFANKQDVAGALSVEEITELLSLHKLCCGRSWYIQGCDARSGMGLYEGLDWLSRQLV AAG
ARFARF-like small GTPases; ARF, ADP-ribosylation factor |
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SMART accession number: | SM00177 |
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Description: | Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop). |
Family alignment: |
There are 12028 ARF domains in 11995 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing ARF domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with ARF domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing ARF domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
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Binding / catalysis: GTP hydrolysis
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Luo JQ et al.
- Functional association between Arf and RalA in active phospholipase D complex.
- Proc Natl Acad Sci U S A. 1998; 95: 3632-7
- Display abstract
Activation of phospholipase D1 (PLD1) by Arf has been implicated in vesicle transport and membrane trafficking. PLD1 has also been shown to be associated with the small GTPase RalA, which functions downstream from Ras in a Ras-RalA GTPase cascade that facilitates intracellular signal transduction. Although PLD1 associates directly with RalA, RalA has no effect upon the activity of PLD1. However, PLD1 precipitated from cell lysates with immobilized glutathione S-transferase-RalA fusion protein is active. This suggests the presence of an additional activating factor in the active RalA-PLD1 complexes. Because Arf stimulates PLD1, we looked for the presence of Arf in the active RalA-PLD1 complexes isolated from v-Src- and v-Ras-transformed cell lysates. Low levels of Arf protein were detected in RalA-PLD1 complexes; however, if guanosine 5'-[gamma-thio]triphosphate was added to activate Arf and stimulate translocation to the membrane, high levels of Arf were precipitated by RalA from cell lysates. Interestingly, deletion of 11 amino-terminal amino acids unique to Ral GTPases, which abolished the ability of RalA to precipitate PLD activity, prevented the association between RalA and Arf. Brefeldin A, which inhibits Arf GDP-GTP exchange, inhibited PLD activity in v-Src- and v-Ras-transformed cells but not in the nontransformed cells, suggesting that the association of Arf with RalA is required for the increased PLD activity induced by v-Src and v-Ras. These data implicate Arf in the transduction of intracellular signals activated by v-Src and mediated by the Ras-RalA GTPase cascade. Because both Arf and PLD1 stimulate vesicle formation in the Golgi, these data raise the possibility that vesicle formation and trafficking may play a role in the transduction of intracellular signals.
- Exton JH
- New developments in phospholipase D.
- J Biol Chem. 1997; 272: 15579-82
- Boman AL, Kahn RA
- Arf proteins: the membrane traffic police?
- Trends Biochem Sci. 1995; 20: 147-50
- Display abstract
Cofactor for cholera toxin; activator of phospholipase D; regulator of coat-protein assembly; inhibitor of membrane traffic; ability to cause expansion of the endoplasmic reticulum and vesiculation of the Golgi; sensitivity to membrane phospholipids--each of these activities has been attributed to Arf proteins. Can a single molecular mechanism link them all?
- Greasley SE et al.
- The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms.
- Nat Struct Biol. 1995; 2: 797-806
- Display abstract
The ARFs are a family of 21,000 M(r) proteins with biological roles in constitutive secretion and activation of phospholipase D. The structure of ARF-1 complexed to GDP determined from two crystal forms reveals a topology that is similar to that of the protein p21 ras with two differences: an additional amino-terminal helix and an extra beta-strand. The Mg2+ ion in ARF-1 displays a five-coordination sphere; this feature is not seen in p21 ras, due to a shift in the relative position of the DXXG motif between the two proteins. The occurrence of a dimer in one crystal form suggests that ARF-1 may dimerize during its biological function. The dimer interface involves a region of the ARF-1 molecule that is analogous to the effector domain in p21 ras and may mediate interactions with its effectors.
- Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C
- Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins.
- J Biol Chem. 1991; 266: 2606-14
- Display abstract
A new member, hARF4, of the ADP-ribosylation factor (ARF) family, a subset of the superfamily of regulatory GTP-binding proteins, has been cloned from a cDNA expression library. Two other human ARF cDNA sequences, designated human ARF1 and ARF3, have been reported previously and are 96% identical in amino acid sequence. A human ARF1 cDNA, significantly longer than previously described clones, was obtained, by cross-species hybridization using a bovine ARF1 cDNA probe. Bovine ARF1p and human ARF1p are 100% identical while each is only 80% identical to hARF4p. Thus, hARF4p is the most divergent of the mammalian ARF proteins identified. Northern blot analysis revealed the expression of at least three different ARF messages in human placenta and adrenal carcinoma cells. Both hARF1 and hARF4 encode GTP-binding proteins with predicted molecular masses of 20,000-21,000 Da. Biochemical analysis of the purified recombinant proteins revealed a high degree of conservation of nucleotide binding properties and in vitro ARF activities. ARF is an essential gene in the yeast, Saccharomyces cerevisiae, and is encoded by two genes. Expression of either hARF1p or hARF4p in yeast was found to rescue the lethal double mutant, arf1-arf2-, thus demonstrating the functional conservation of ARF functions between yeast and man. The combination of in vivo and in vitro assays for ARF function provides a specific and unambiguous means of determining bona fide ARF proteins from divergent species from among the rapidly increasing number of structurally related, small molecular weight GTP-binding proteins.
- Structure (3D structures containing this domain)
3D Structures of ARF domains in PDB
PDB code Main view Title 1e0s small G protein Arf6-GDP 1fzq CRYSTAL STRUCTURE OF MURINE ARL3-GDP 1hur HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED 1j2j Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form 1ksg Complex of Arl2 and PDE delta, Crystal Form 1 1ksh Complex of Arl2 and PDE delta, Crystal Form 2 (native) 1ksj Complex of Arl2 and PDE delta, Crystal Form 2 (SeMet) 1moz ADP-ribosylation factor-like 1 (ARL1) from Saccharomyces cerevisiae 1mr3 Saccharomyces cerevisiae ADP-ribosylation Factor 2 (ScArf2) complexed with GDP-3'P at 1.6A resolution 1o3y Crystal structure of mouse ARF1 (delta17-Q71L), GTP form 1r4a Crystal Structure of GTP-bound ADP-ribosylation Factor Like Protein 1 (Arl1) and GRIP Domain of Golgin245 COMPLEX 1r8q FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN 1r8s ARF1[DELTA1-17]-GDP IN COMPLEX WITH A SEC7 DOMAIN CARRYING THE MUTATION OF THE CATALYTIC GLUTAMATE TO LYSINE 1re0 Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A 1rrf NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM 1rrg NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM 1s9d ARF1[DELTA 1-17]-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN 1u81 Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP 1upt Structure of a complex of the golgin-245 GRIP domain with Arl1 1yzg Structure of Human ADP-ribosylation factor-like 8 1z6x Structure Of Human ADP-Ribosylation Factor 4 1z6y Structure Of Human ADP-Ribosylation Factor-Like 5 1zj6 Crystal structure of human ARL5 2a5d Structural basis for the activation of cholera toxin by human ARF6-GTP 2a5f Cholera toxin A1 subunit bound to its substrate, NAD+, and its human protein activator, ARF6 2a5g Cholera toxin A1 subunit bound to ARF6(Q67L) 2b6h Structure of human ADP-ribosylation factor 5 2h16 Structure of human ADP-ribosylation factor-like 5 (ARL5) 2h17 Structure of human ADP-ribosylation factor-like 5 (ARL5) (CASP Target) 2h57 Crystal structure of human ADP-ribosylation factor-like 6 2j59 Crystal structure of the ARF1:ARHGAP10-ArfBD complex 2j5x STRUCTURE OF THE SMALL G PROTEIN ARF6 IN COMPLEX WITH GTPGAMMAS 2k5u Solution structure of myirstoylated yeast ARF1 protein, GDP-bound 2ksq The myristoylated yeast ARF1 in a GTP and bicelle bound conformation 2w83 Crystal structure of the ARF6 GTPase in complex with a specific effector, JIP4 2x77 Crystal Structure of Leishmania major ADP ribosylation factor-like 1. 3aq4 Molecular insights into plant cell proliferation disturbance by Agrobacterium protein 6b 3bh6 Crystal structure of the RP2-Arl3 complex bound to GppNHp 3bh7 Crystal structure of the RP2-Arl3 complex bound to GDP-AlF4 3doe Complex of ARL2 and BART, Crystal Form 1 3dof Complex of ARL2 and BART, Crystal Form 2 3lrp Crystal Structure of Plasmodium falciparum ADP-Ribosylation Factor 1 3lvq The crystal structure of ASAP3 in complex with Arf6 in transition state 3lvr The crystal structure of ASAP3 in complex with Arf6 in transition state soaked with Calcium 3n5c Crystal Structure of Arf6DELTA13 complexed with GDP 3o47 Crystal structure of ARFGAP1-ARF1 fusion protein 3pcr Structure of EspG-Arf6 complex 3tjz Crystal Structure of Arf1 Bound to the gamma/zeta-COP Core Complex 3vhx The crystal structure of Arf6-MKLP1 (Mitotic kinesin-like protein 1) complex 4bas Structure of the Arl6 BBS3 Small GTPase from Trypanosoma brucei with bound nucleotide analogue GppNp 4c0a Arf1(Delta1-17)in complex with BRAG2 Sec7-PH domain 4dcn Crystal Structure Analysis of the Arfaptin2 BAR domain in Complex with ARL1 4fme EspG-Rab1-Arf6 complex 4goj The Crystal Structure of full length Arl3GppNHp in complex with UNC119a 4gok The Crystal structure of Arl2GppNHp in complex with UNC119a 4hmy Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1 4kax Crystal structure of the Grp1 PH domain in complex with Arf6-GTP 4q66 4Q66 4v0k 4V0K 4v0l 4V0L 4v0m 4V0M 4v0n 4V0N 4v0o 4V0O 4y0v 4Y0V 4ylg 4YLG 4zi2 4ZI2 4zi3 4ZI3 5a1u 5A1U 5a1v 5A1V 5a1w 5A1W 5a1x 5A1X 5a1y 5A1Y 5de3 5DE3 5di3 5DI3 5ee5 5EE5 5j5c 5J5C - Links (links to other resources describing this domain)
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PFAM arf