The domain within your query sequence starts at position 4 and ends at position 171; the E-value for the ARF domain shown below is 4.8e-58.

GHYAEHKVIIVGLDNAGKTTILYQFLMNEVVHTSPTIGSNVEEIVVKNTHFLMWDIGGQE
SLRSSWNTYYSNTEFIILVVDSIDRERLAITKEELYRMLAHEDLRKAAVLIFANKQDMKG
CMTAAEISKYLTLSSIKDHPWHIQSCCALTGEGLCQGLEWMTSRIGVR

ARF

ARF-like small GTPases; ARF, ADP-ribosylation factor

• SMART accession number: SM00177
• 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).

There are 12028 ARF domains in 11995 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Binding / catalysis: GTP hydrolysis

Literature (relevant references for this domain)

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

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

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

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

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	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)

• PFAM: arf