ARF6
entrez
382
canonical
uniprot
P62330
canonical
ensembl
ENSG00000165527
resolver
ensp
ENSP00000298316
resolver
ensp
ENSP00000510419
resolver
ensp
ENSP00000565870
resolver
ensp
ENSP00000565871
resolver
enst
ENST00000298316
resolver
enst
ENST00000693319
resolver
enst
ENST00000895811
resolver
enst
ENST00000895812
resolver
genesymbol
ARF6
resolver
hgnc
HGNC:659
resolver
uniprot
P26438
resolver
uniprot
Q6FGZ2
resolver
uniprot_entry
ARF6_HUMAN
resolver
uniprot_sec
P26438
resolver
uniprot_sec
Q6FGZ2
resolver
activity_regulation
ACTIVITY REGULATION: Activation is generally mediated by a guanine exchange factor (GEF), while inactivation through hydrolysis of bound GTP is catalyzed by a GTPase activating protein (GAP). Activated by ASAP3. Inactivated by ACAP1 and ACAP2. Activated by NGF via NTRK1 (By similarity). Activated by PRKAA2 through its C-terminal regulatory domain (PubMed:36017701). {ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11062263, ECO:0000269|PubMed:18400762, ECO:0000269|PubMed:36017701}.
uniprot
proteins
amino_acid_sequence
MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling (PubMed:11266366, PubMed:16737952, PubMed:18400762, PubMed:21170023, PubMed:32103017, PubMed:7589240). GTP-bound form plays an important role in the transport of multiple palmitoylated proteins form the Golgi to the plasma membrane (PubMed:37461827). Required for normal completion of mitotic cytokinesis (By similarity). Plays a role in the reorganization of the actin cytoskeleton and the formation of stress fibers (By similarity). Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension (PubMed:14978216). Potentiates the neurite outgrowth in primary neurons by interacting with the molecular adapter APBB1 (PubMed:36250347). Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization (PubMed:36017701). Regulates surface levels of adherens junction proteins such as CDH1 (By similarity). Required for NTRK1 sorting to the recycling pathway from early endosomes (By similarity). {ECO:0000250|UniProtKB:P62331, ECO:0000250|UniProtKB:P62332, ECO:0000269|PubMed:11266366, ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16099990, ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:18400762, ECO:0000269|PubMed:21170023, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:36017701, ECO:0000269|PubMed:36250347, ECO:0000269|PubMed:37461827, ECO:0000269|PubMed:7589240}.; FUNCTION: (Microbial infection) Functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. {ECO:0000269|PubMed:16099990}.; FUNCTION: (Microbial infection) Plays a key role in the endocytosis of enterovirus 71 and thus viral entry into brain microvascular endothelial cells. {ECO:0000269|PubMed:37417384}.
uniprot
proteins
mass_dalton
20082
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Fails to associate with membranes."; /evidence="ECO:0000269|PubMed:7589240"; MUTAGEN 3; /note="K->R: Abolished lysine-myristoylation, leading to decreased localization to membranes."; /evidence="ECO:0000269|PubMed:32103017"; MUTAGEN 27; /note="T->N: Constitutively inactivated. Fails to associate with membranes. Does not inhibit filopodia formation."; /evidence="ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:17398095, ECO:0000269|PubMed:32103017"; MUTAGEN 67; /note="Q->L: Constitutively active. Inhibits filopodia formation and dendritic branching."; /evidence="ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:32103017
uniprot
proteins
post_translational_modification
PTM: GTP-bound form is myristoylated on Lys-3 by NMT1 and NMT2, allowing ARF6 to remain on membranes during the GTPase cycle, thereby promoting its activity (PubMed:32103017). GDP-bound inactive form is demyristoylated on Lys-3 by SIRT2 at early endosomes or endocytic recycling compartment to allow its efficient activation by a guanine exchange factor (GEF) after GDP release (PubMed:32103017). {ECO:0000269|PubMed:32103017}.
uniprot
proteins
protein_family
Arf family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10881192
uniprot
proteins
pubmed
11062263
uniprot
proteins
pubmed
11266366
uniprot
proteins
pubmed
11950392
uniprot
proteins
pubmed
12847086
uniprot
proteins
pubmed
14659046
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14978216
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509780
uniprot
proteins
pubmed
15642342
uniprot
proteins
pubmed
15793564
uniprot
proteins
pubmed
16099990
uniprot
proteins
pubmed
16148947
uniprot
proteins
pubmed
16737952
uniprot
proteins
pubmed
16839550
uniprot
proteins
pubmed
17030804
uniprot
proteins
pubmed
17398095
uniprot
proteins
pubmed
17555535
uniprot
proteins
pubmed
17628206
uniprot
proteins
pubmed
18400762
uniprot
proteins
pubmed
19644450
uniprot
proteins
pubmed
1993656
uniprot
proteins
pubmed
19948740
uniprot
proteins
pubmed
20510928
uniprot
proteins
pubmed
20682791
uniprot
proteins
pubmed
20727515
uniprot
proteins
pubmed
21170023
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21951725
uniprot
proteins
pubmed
22939626
uniprot
proteins
pubmed
23603394
uniprot
proteins
pubmed
23940353
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32004315
uniprot
proteins
pubmed
32103017
uniprot
proteins
pubmed
36017701
uniprot
proteins
pubmed
36250347
uniprot
proteins
pubmed
37417384
uniprot
proteins
pubmed
37461827
uniprot
proteins
pubmed
7589240
uniprot
proteins
pubmed
9653160
uniprot
proteins
sequence_length
175
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:23603394, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:36017701, ECO:0000269|PubMed:7589240}. Cell membrane {ECO:0000269|PubMed:16737952, ECO:0000269|PubMed:17398095, ECO:0000269|PubMed:17555535, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:36017701, ECO:0000269|PubMed:37417384}; Lipid-anchor {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Endosome membrane {ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:20682791, ECO:0000269|PubMed:21951725}; Lipid-anchor {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Recycling endosome membrane {ECO:0000269|PubMed:21951725}; Lipid-anchor {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Cell projection, filopodium membrane {ECO:0000269|PubMed:14978216}; Lipid-anchor {ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}. Cell projection, ruffle {ECO:0000269|PubMed:16737952}. Cleavage furrow {ECO:0000269|PubMed:23603394}. Midbody, Midbody ring {ECO:0000269|PubMed:23603394}. Early endosome membrane {ECO:0000250|UniProtKB:P62331}; Lipid-anchor {ECO:0000250|UniProtKB:P62331}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P62331}; Lipid-anchor {ECO:0000250|UniProtKB:P62331}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase. Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression. In late stages of cytokinesis, concentrates at the midbody ring/Flemming body (PubMed:23603394). Recruitment to the midbody ring requires both activation by PSD/EFA6A and interaction with KIF23/MKLP1 (PubMed:23603394). After abscission of the intercellular bridge, incorporated into one of the daughter cells as a midbody remnant and localizes to punctate structures beneath the plasma membrane (PubMed:23603394). Recruited to the cell membrane in association with CYTH2 and ARL4C (PubMed:17398095). Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles (PubMed:19948740). Myristoylation is required for proper localization to membranes: myristoylation on Lys-3 allows ARF6 to remain on membranes during the GTPase cycle (PubMed:32103017, PubMed:7589240). {ECO:0000269|PubMed:17398095, ECO:0000269|PubMed:19948740, ECO:0000269|PubMed:23603394, ECO:0000269|PubMed:32103017, ECO:0000269|PubMed:7589240}.
uniprot
proteins