ARF6_XENLA
ID ARF6_XENLA Reviewed; 175 AA.
AC P51645;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ADP-ribosylation factor 6;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P62330};
GN Name=arf6;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Boman A.L.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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}. Golgi apparatus
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 -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; U31469; AAA74952.1; -; mRNA.
DR RefSeq; NP_001084094.1; NM_001090625.1.
DR AlphaFoldDB; P51645; -.
DR SMR; P51645; -.
DR DNASU; 399300; -.
DR GeneID; 399300; -.
DR KEGG; xla:399300; -.
DR CTD; 399300; -.
DR Xenbase; XB-GENE-17343122; arf6.2.S.
DR OrthoDB; 1362554at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 399300; Expressed in testis and 19 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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 ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Lipoprotein;
KW Membrane; Myristate; Neurogenesis; Nucleotide-binding; Protein transport;
KW 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_0000207404"
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; 20187 MW; 2468FE6FE4AC8F11 CRC64;
MGKMFSKIFG NKEMRILMRG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC PDRDRIDEAR QELHRIINDR EMRDAIILIF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCAASGD GLYEGLTWLT SNYKS
