Primary Information
BoMiProt ID	Bomi224
Protein Name	ADP-ribosylation factor 1
Organism	Bos taurus
Uniprot ID	P84080
Milk Fraction	MFGM, Exosome
Ref Sequence ID	NP_788826.1
Aminoacid Length	181
Molecular Weight	20697
FASTA Sequence	Download
Gene Name	ARF1
Gene ID	338058
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Presence in other biological fluids/tissue/cells	localized to the Golgi apparatu; found in every eukaryotic cell; present in high abundance (-1% of cell protein) in brain tissue; highly enriched in coated vesicles as compared with parental Golgi cisternae
Protein Function	Arf family of GTP-binding (G) proteins, including the Arf-like (Arl) proteins and Sar1, regulate membrane traffic and organelle structure through the membrane recruitment of cargo-sorting coat proteins; and interacts with regulators of other G proteins; activity of the ADP-ribosylation factor (ARF) is that of a cofactor,which is in turn regulated by GTP; may modulate vesicle budding and uncoating through controlled GTP hydrolysis; Arfs have several important functions,including the recruitment of coat proteins that promote sorting of cargo into vesicles, the recruitment and activation of enzymes such as the phosphatidylinositol kinases that alter membrane lipid composition, and interaction with cytoskeletal factors; Arfs can also recruit and activate enzymes that alter membrane lipid composition. ARF1 stimulated proliferation and migration of osteoclast precursors while suppressing their fusion, suggesting that ARF1 may be a plausible inter-player that mediates the transition to osteoclast fusion at multiple steps during osteoclast differentiation.
Biochemical Properties	ARF and ARLs function is under tight spatial control, mediated by guanine nucleotide-exchange factors (GEFs) and GTPase activating proteins (GAPs) that catalyse GTP exchange and hydrolysis; Asp-26 of ARF corresponds to Gly-12 of ras proteins, which is an important determinant of GTPase activity and transformation potency- lack of a glycine at this position may explain the lack of GTPase activity of purified ARF; ARF, as purified from cytosol, is accompanied by a bound GDP molecule and has no measurable GTPase activity (upper estimate of 0.0015/min), nor will it readily exchange GTP for endogenous GDP- However, exchange can be accomplished under conditions of high ionic strength or denaturation/renaturation
PTMs	all Arf proteins are myristoylated at the amino terminus-consensus sequence for aminoterminal myristoylation (Metiit-Gly-Xaa-Xaa-Xaa-Ser/Ala/ Thr); Some Arl proteins are myristoylated but most appear to lack this modification
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
SCOP	Class : Alpha and beta proteins (a/b) Fold : G domain-like Superfamily : Ras-like P-loop GTPases Family : Ras-like monodomain GTPases Domain Name : 1R8S A:18-177
CATH	Matched CATH superfamily 3.40.50.300
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	This cotranslational modification is required for membrane recruitment and biological activity
PDB ID	1R8Q, 1R8S, 1S9D, 4C0A,
Additional Comments	ARF1 deficiency resulted in reduced osteoclast precursor proliferation and migration as well as increasing cell-cell fusion.
Bibliography	1. Sewell, J. L. and Kahn, R. A. (1988) ‘Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins.’, Proceedings of the National Academy of Sciences of the United States of America, 85(13), pp. 4620–4. doi: 10.1073/pnas.85.13.4620. 2. Stearns, T. et al. (1990) ‘ADP-ribosylation factor is functionally and physically associated with the Golgi complex.’, Proceedings of the National Academy of Sciences, 87(3), pp. 1238–1242. doi: 10.1073/pnas.87.3.1238. 3. Serafini, T. et al. (1991) ‘ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.’, Cell, 67(2), pp. 239–53. doi: 10.1016/0092-8674(91)90176-y. 4.Kim MJ, Kim H, Lee SH, Gu DR, Lee SY, Lee K, Jeong D. ADP-Ribosylation Factor 1 Regulates Proliferation, Migration, and Fusion in Early Stage of Osteoclast Differentiation. Int J Mol Sci. 2015 Dec 9;16(12):29305-14. doi: 10.3390/ijms161226168. PMID: 26690137; PMCID: PMC4691111.