ID C4MQ03_PIG Unreviewed; 175 AA.
AC C4MQ03;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=ADP-ribosylation factor 6 {ECO:0000256|ARBA:ARBA00017741};
GN Name=ARF6 {ECO:0000313|EMBL:ACI15389.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|EMBL:ACI15389.1};
RN [1] {ECO:0000313|EMBL:ACI15389.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang R.R., Yang Z.Q.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI15389.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20662810; DOI=10.1111/j.1740-0929.2010.00765.x;
RA Zhang R., Lei T., Qi Y., Lei P., Chen Z., Chen X., Yang Z.;
RT "Molecular cloning, chromosomal localization and expression pattern of
RT porcine ADP-ribosylation factor(Arf) gene family.";
RL Anim. Sci. J. 81:425-431(2010).
RN [3] {ECO:0000313|EMBL:HCZ83879.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30723633; DOI=.7717/peerj.6374;
RA Gilbert D.G.;
RT "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL PeerJ 7:E6374-E6374(2019).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell projection,
CC filopodium membrane {ECO:0000256|ARBA:ARBA00004527}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004527}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cleavage furrow
CC {ECO:0000256|ARBA:ARBA00004626}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004455}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004455}. Midbody, Midbody ring
CC {ECO:0000256|ARBA:ARBA00004476}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004139}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004139}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000256|RuleBase:RU003925}.
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DR EMBL; EU753432; ACI15389.1; -; Genomic_DNA.
DR EMBL; DQIR01028404; HCZ83879.1; -; Transcribed_RNA.
DR RefSeq; NP_001072145.1; NM_001078677.1.
DR RefSeq; XP_005659996.1; XM_005659939.2.
DR AlphaFoldDB; C4MQ03; -.
DR SMR; C4MQ03; -.
DR GeneID; 780425; -.
DR KEGG; ssc:780425; -.
DR CTD; 382; -.
DR HOGENOM; CLU_040729_9_4_1; -.
DR OMA; GGQISKM; -.
DR OrthoDB; 5474610at2759; -.
DR ExpressionAtlas; C4MQ03; baseline and differential.
DR Genevisible; C4MQ03; SS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR GO; GO:0031996; F:thioesterase binding; IEA:Ensembl.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
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:0001889; P:liver development; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
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:0010976; P:positive regulation of neuron projection development; 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; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0060998; P:regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR CDD; cd04149; Arf6; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR041838; Arf6.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1.
DR PANTHER; PTHR11711:SF322; ADP-RIBOSYLATION FACTOR 6; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU003925};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003925}.
SQ SEQUENCE 175 AA; 20082 MW; 49E38E59AEA52B98 CRC64;
MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF
ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS
//
