ARF6_CHICK
ID ARF6_CHICK Reviewed; 175 AA.
AC P26990;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ADP-ribosylation factor 6;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62330};
GN Name=ARF6; Synonyms=CPS1 {ECO:0000303|PubMed:3083400};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=3083400; DOI=10.1093/nar/14.5.2123;
RA Alsip G.R., Konkel D.A.;
RT "A processed chicken pseudogene (CPS1) related to the ras oncogene
RT superfamily.";
RL Nucleic Acids Res. 14:2123-2138(1986).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking;
CC regulates endocytic recycling and cytoskeleton remodeling. May modulate
CC vesicle budding and uncoating within the Golgi apparatus. May
CC contribute to the regulation of dendritic branching, filopodia
CC extension and dendritic spine development (By similarity).
CC {ECO:0000250|UniProtKB:P62330}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P62330};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P62330};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P62330}. Cell membrane
CC {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62330}. Endosome membrane
CC {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62330}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62331}. Cell projection, filopodium membrane
CC {ECO:0000250|UniProtKB:P62331}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62331}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P62330}. Cleavage furrow
CC {ECO:0000250|UniProtKB:P62330}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:P62331}. Note=Distributed uniformly on the
CC plasma membrane, as well as throughout the cytoplasm during metaphase.
CC Subsequently concentrated at patches in the equatorial region at the
CC onset of cytokinesis, and becomes distributed in the equatorial region
CC concurrent with cleavage furrow ingression. In late stages of
CC cytokinesis, concentrates at the midbody ring/Flemming body. After
CC abscission of the intercellular bridge, incorporated into one of the
CC daughter cells as a midbody remnant and localizes to punctate
CC structures beneath the plasma membrane (By similarity). Recruited to
CC the cell membrane in association with CYTH2 and ARL4C. Colocalizes with
CC DAB2IP at the plasma membrane and endocytic vesicles. Myristoylation is
CC required for proper localization to membranes (By similarity).
CC {ECO:0000250|UniProtKB:P62330, ECO:0000250|UniProtKB:P62331}.
CC -!- DEVELOPMENTAL STAGE: In 3 days embryos. {ECO:0000269|PubMed:3083400}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; X03682; CAA27317.1; -; Genomic_DNA.
DR PIR; I50632; I50632.
DR RefSeq; NP_001075174.1; NM_001081705.1.
DR AlphaFoldDB; P26990; -.
DR SMR; P26990; -.
DR IntAct; P26990; 2.
DR MINT; P26990; -.
DR STRING; 9031.ENSGALP00000041604; -.
DR Ensembl; ENSGALT00000045497; ENSGALP00000041604; ENSGALG00000026944.
DR GeneID; 428927; -.
DR KEGG; gga:428927; -.
DR CTD; 382; -.
DR VEuPathDB; HostDB:geneid_428927; -.
DR eggNOG; KOG0071; Eukaryota.
DR GeneTree; ENSGT00940000156593; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P26990; -.
DR OMA; WSVIPTI; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P26990; -.
DR PRO; PR:P26990; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000026944; Expressed in granulocyte and 12 other tissues.
DR ExpressionAtlas; P26990; baseline.
DR GO; GO:0005938; C:cell cortex; ISS:AgBase.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISS:AgBase.
DR GO; GO:0032587; C:ruffle membrane; IDA:AgBase.
DR GO; GO:0003925; F:G protein activity; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0031996; F:thioesterase binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:AgBase.
DR GO; GO:0032456; P:endocytic recycling; IEA:Ensembl.
DR GO; GO:1902217; P:erythrocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:AgBase.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0036010; P:protein localization to endosome; IBA:GO_Central.
DR GO; GO:0060998; P:regulation of dendritic spine development; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISS:AgBase.
DR GO; GO:0097178; P:ruffle assembly; ISS:AgBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041838; Arf6.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Differentiation; Endosome;
KW GTP-binding; Hydrolase; Lipoprotein; Membrane; Myristate; Neurogenesis;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT CHAIN 2..175
FT /note="ADP-ribosylation factor 6"
FT /id="PRO_0000207403"
FT BINDING 23..28
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT BINDING 41..44
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT BINDING 63..67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT BINDING 155..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P62330"
FT LIPID 3
FT /note="N6-myristoyl lysine"
FT /evidence="ECO:0000250|UniProtKB:P62330"
SQ SEQUENCE 175 AA; 20096 MW; 49E68E09AEA52B98 CRC64;
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATTGD GLYEGLTWLT SNYKS
