ADP-ribosylation factor 1 (ARF1)

The protein contains 181 amino acids for an estimated molecular weight of 20697 Da.

 

GTP-binding protein involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasicity of excitatory synapses and spine shrinkage during long-term depression (LTD).', '(Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. (updated: Dec. 5, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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VariantDescription
PVNH8
PVNH8; unknown pathological significance
PVNH8

The reference OMIM entry for this protein is 103180

Adp-ribosylation factor 1; arf1

DESCRIPTION

ADP-ribosylation factors (ARFs), such as ARF1, are small guanine nucleotide-binding proteins that enhance the enzymatic activities of cholera toxin. ARFs are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as activators of phospholipase D. The functions of ARF proteins in membrane traffic and organelle integrity are intimately tied to their reversible association with membranes and specific interactions with membrane phospholipids. A common feature of these functions is their regulation by the binding and hydrolysis of GTP (summary by Bobak et al. (1989) and Amor et al. (1994)).

CLONING

Bobak et al. (1989) cloned 2 ARF cDNAs, ARF1 and ARF3 (103190), from a human cerebellum library. Based on deduced amino acid sequences and patterns of hybridization of cDNA and oligonucleotide probes with mammalian brain poly(A)+ RNA, human ARF1 is the homolog of bovine ARF1. Human ARF3, however, appeared to represent a newly identified, third type of ARF, which differs from bovine ARF1 and bovine ARF2. Peng et al. (1989) also reported cloning of ADP-ribosylation factor. Lee et al. (1992) found that human ARF1 is identical to its bovine counterpart, has a distinctive pattern of tissue and developmental expression, and is encoded by an mRNA of approximately 1.9 kb.

GENE FUNCTION

Coatomer, or COPI (see 601924), is a heptameric protein recruited to membranes by ARF1. Coat assembly helps in the transport of budding off membrane between the endoplasmic reticulum (ER) and Golgi apparatus. Using fluorescence microscopy, Presley et al. (2002) showed that guanine nucleotide exchange-activated ARF1 at the Golgi membrane recruits and binds cytoplasmic COPI to the membranes. Photobleaching experiments demonstrated that COPI remains at the membranes after ARF1-GTP has been hydrolyzed by ARFGAP1 (608377). COPI binds to membrane cargo, soluble-cargo receptors, or other Golgi proteins. Uncoating, or the release of COPI from Golgi membranes to the cytoplasm, then occurs, which can be inhibited by aluminum fluoride. Presley et al. (2002) concluded from their kinetic and biochemical analyses that COPI and ARF1 continuously bind and release from Golgi membranes, allowing the membrane at these sites to recruit cargo, alter their phospholipid composition, and become larger, phase-separated domains. Endocytosis of glycosylphosphatidyl inositol (GPI)-anchored proteins and the fluid phase takes place primarily through a dynamin (see DNM1; 602377)- and clathrin (see CLTC; 118955)-independent, CDC42 (116952)-regulated pinocytic mechanism. In Chinese hamster ovary cells, Kumari and Mayor (2008) found that reduced activity or levels of Arf1 inhibited GPI-anchored protein and fluid-phase endocytosis without affecting other clathrin-dependent or -independent endocytic pathways. Arf1 was activated at distinct sites on the plasma membrane, and it recruited the CDC42 GTPase-activating protein Arhgap10 (609746) to the plasma membrane, thereby modulating cell surface Cdc42 dynamics. Kumari and Mayor (2008) concluded that ARF1 regulates both endocytosis and secretion and may provide a mechanism for crosstalk between these processes. Using a yeast genetic screen for substrates of the Shigella flexneri type III effector protein IpaJ, Burnaevskiy et al. (2013) identified Arf1 and Arf2 (ARF4; 601177). Mass spectrometric analysis showed that IpaJ cleaved the peptide bond between myristoylated gly2 and asn3 ... More on the omim web site

Subscribe to this protein entry history

Dec. 9, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for ARF1

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 103180 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed