ID ARF6_HUMAN Reviewed; 175 AA. AC P62330; P26438; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 25-NOV-2008, entry version 57. DE RecName: Full=ADP-ribosylation factor 6; GN Name=ARF6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91131565; PubMed=1993656; RA Tsuchiya M., Price S.R., Tsai S.-C., Moss J., Vaughan M.; RT "Molecular identification of ADP-ribosylation factor mRNAs and their RT expression in mammalian cells."; RL J. Biol. Chem. 266:2772-2777(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX MEDLINE=98318631; PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full- RT length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP MYRISTOYLATION AT GLY-2, FUNCTION, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF GLY-2. RX MEDLINE=96042026; PubMed=7589240; DOI=10.1006/excr.1995.1362; RA D'Souza-Schorey C., Stahl P.D.; RT "Myristoylation is required for the intracellular localization and RT endocytic function of ARF6."; RL Exp. Cell Res. 221:153-159(1995). RN [6] RP INTERACTION WITH PIP5K1C. RX PubMed=12847086; DOI=10.1083/jcb.200301006; RA Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.; RT "ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by RT activating phosphatidylinositol phosphate kinase type Igamma."; RL J. Cell Biol. 162:113-124(2003). RN [7] RP INTERACTION WITH HERC1. RX PubMed=15642342; DOI=10.1016/j.febslet.2004.11.095; RA Garcia-Gonzalo F.R., Bartrons R., Ventura F., Rosa J.L.; RT "Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1- RT mediated guanine nucleotide release from ARF proteins."; RL FEBS Lett. 579:343-348(2005). RN [8] RP INTERACTION WITH ARHGAP21. RX PubMed=15793564; DOI=10.1038/ncb1244; RA Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B., RA De Matteis M.A., Franco M., Chavrier P.; RT "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control RT Arp2/3 complex and F-actin dynamics."; RL Nat. Cell Biol. 7:353-364(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND FUNCTION. RX MEDLINE=21174504; PubMed=11266366; DOI=10.1093/embo-reports/kve043; RA Pasqualato S., Menetrey J., Franco M., Cherfils J.; RT "The structural GDP/GTP cycle of human Arf6."; RL EMBO Rep. 2:234-238(2001). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SUBUNIT: Interacts with ARHGAP21, DDEF2, HERC1, PIP5K1C and UACA. CC -!- INTERACTION: CC P53365:ARFIP2; NbExp=1; IntAct=EBI-638181, EBI-638194; CC P21283:ATP6V1C1; NbExp=4; IntAct=EBI-638181, EBI-988663; CC P49366:DHPS; NbExp=1; IntAct=EBI-638181, EBI-741925; CC Q14204:DYNC1H1; NbExp=1; IntAct=EBI-638181, EBI-356015; CC P56537:EIF6; NbExp=1; IntAct=EBI-638181, EBI-372243; CC P58107:EPPK1; NbExp=1; IntAct=EBI-638181, EBI-297954; CC P22102:GART; NbExp=1; IntAct=EBI-638181, EBI-356297; CC P46940:IQGAP1; NbExp=1; IntAct=EBI-638181, EBI-297509; CC P42704:LRPPRC; NbExp=1; IntAct=EBI-638181, EBI-1050853; CC Q13310:PABPC4; NbExp=1; IntAct=EBI-638181, EBI-372844; CC P54577:YARS; NbExp=1; IntAct=EBI-638181, EBI-1048893; CC -!- SUBCELLULAR LOCATION: Golgi apparatus. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M57763; AAA90928.1; -; mRNA. DR EMBL; AF047432; AAC39877.1; -; mRNA. DR EMBL; AF493885; AAM12599.1; -; mRNA. DR EMBL; BC002952; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC008918; AAH08918.1; -; mRNA. DR PIR; B23741; B23741. DR RefSeq; NP_001654.1; -. DR UniGene; Hs.525330; -. DR UniGene; Hs.593068; -. DR PDB; 1E0S; X-ray; 2.28 A; A=1-175. DR PDB; 2A5D; X-ray; 1.80 A; A=1-175. DR PDB; 2A5F; X-ray; 2.02 A; A=1-175. DR PDB; 2A5G; X-ray; 2.66 A; A=1-175. DR PDB; 2J5X; X-ray; 2.80 A; A/B=1-175. DR PDBsum; 1E0S; -. DR PDBsum; 2A5D; -. DR PDBsum; 2A5F; -. DR PDBsum; 2A5G; -. DR PDBsum; 2J5X; -. DR IntAct; P62330; -. DR PhosphoSite; P62330; -. DR PeptideAtlas; P62330; -. DR Ensembl; ENSG00000165527; Homo sapiens. DR GeneID; 382; -. DR KEGG; hsa:382; -. DR H-InvDB; HIX0011635; -. DR HGNC; HGNC:659; ARF6. DR HPA; CAB002778; -. DR MIM; 600464; gene. DR PharmGKB; PA24942; -. DR HOGENOM; P62330; -. DR HOVERGEN; P62330; -. DR LinkHub; P62330; -. DR NextBio; 1599; -. DR ArrayExpress; P62330; -. DR CleanEx; HS_ARF6; -. DR GermOnline; ENSG00000165527; Homo sapiens. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; TAS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW. DR GO; GO:0005624; C:membrane fraction; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0001726; C:ruffle; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB. DR GO; GO:0006928; P:cell motion; TAS:UniProtKB. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0048261; P:negative regulation of receptor-mediated en...; TAS:UniProtKB. DR GO; GO:0030838; P:positive regulation of actin filament polym...; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:UniProtKB. DR GO; GO:0031529; P:ruffle organization; IDA:UniProtKB. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PANTHER; PTHR11711; ARF/SAR; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. PE 1: Evidence at protein level; KW 3D-structure; ER-Golgi transport; Golgi apparatus; GTP-binding; KW Lipoprotein; Myristate; Nucleotide-binding; Protein transport; KW Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 175 ADP-ribosylation factor 6. FT /FTId=PRO_0000207400. FT NP_BIND 20 27 GTP (By similarity). FT NP_BIND 63 67 GTP (By similarity). FT NP_BIND 122 125 GTP (By similarity). FT LIPID 2 2 N-myristoyl glycine. FT MUTAGEN 2 2 G->A: Fails to associate with membranes. FT HELIX 3 9 FT STRAND 14 21 FT HELIX 26 32 FT STRAND 39 44 FT STRAND 47 54 FT STRAND 57 65 FT HELIX 68 70 FT HELIX 71 74 FT HELIX 75 77 FT TURN 78 80 FT STRAND 83 89 FT HELIX 93 95 FT HELIX 96 107 FT HELIX 110 112 FT STRAND 116 122 FT HELIX 132 138 FT HELIX 141 143 FT STRAND 149 153 FT TURN 156 159 FT HELIX 162 172 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 //