ID ARF1_HUMAN STANDARD; PRT; 180 AA. AC P32889; P10947; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE ADP-RIBOSYLATION FACTOR 1. GN ARF1. OS Homo sapiens (Human), Mus musculus (Mouse), Rattus norvegicus (Rat), OS and Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; 10090; 10116; 9913; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=89345613; PubMed=2474826; RA Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J., RA Vaughan M.; RT "Molecular cloning, characterization, and expression of human ADP- RT ribosylation factors: two guanine nucleotide-dependent activators of RT cholera toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=92250494; PubMed=1577740; RA Lee C.M., Haun R.S., Tsai S.C., Moss J., Vaughan M.; RT "Characterization of the human gene encoding ADP-ribosylation factor RT 1, a guanine nucleotide-binding activator of cholera toxin."; RL J. Biol. Chem. 267:9028-9034(1992). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=BRAIN; RX MEDLINE=97264341; PubMed=9110174; RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.; RT "Large-scale concatenation cDNA sequencing."; RL Genome Res. 7:353-358(1997). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Bovine; RX MEDLINE=88262999; PubMed=3133654; RA Sewell J., Kahn R.A.; RT "Sequences of the bovine and yeast ADP-ribosylation factor and RT comparison to other GTP-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4620-4624(1988). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Bovine; RX MEDLINE=91115891; PubMed=1899243; RA Kahn R.A., Kern F.G., Clark J., Gelmann E.P., Rulka C.; RT "Human ADP-ribosylation factors. A functionally conserved family of RT GTP-binding proteins."; RL J. Biol. Chem. 266:2606-2614(1991). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Rat; TISSUE=BRAIN; RA Nightingale M.S., Price S.R., Tsuchiya M., Moss J., Vaughan M.; RL Submitted (XXX-1994) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=ICR; TISSUE=BRAIN; RX MEDLINE=97103475; PubMed=8947846; RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.; RT "Structure and intracellular localization of mouse ADP-ribosylation RT factors type 1 to type 6 (ARF1-ARF6)."; RL J. Biochem. 120:813-819(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=95082952; PubMed=7990966; RA Amor J.C., Harrison D.H., Kahn R.A., Ringe D.; RT "Structure of the human ADP-ribosylation factor 1 complexed with RT GDP."; RL Nature 372:704-708(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RC SPECIES=Rat; RX MEDLINE=96018618; PubMed=7552752; RA Greasley S.E., Jhoti H., Teahan C., Solari R., Fensome A., RA Thomas G.M., Cockcroft S., Bax B.; RT "The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to RT GDP determined from two different crystal forms."; RL Nat. Struct. Biol. 2:797-806(1995). 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 -!- SIMILARITY: BELONGS TO THE ARF FAMILY OF GTP-BINDING PROTEINS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M36340; AAA35552.1; -. DR EMBL; M84326; AAA35512.1; -. DR EMBL; AF052179; AAC28623.1; -. DR EMBL; AF055002; AAC09356.1; -. DR EMBL; M84332; AAA35511.1; -. DR EMBL; J03275; AAA30361.1; -. DR EMBL; L12380; AAA40685.1; -. DR EMBL; D87898; BAA13490.1; -. DR PIR; A33283; A33283. DR PIR; A36167; A36167. DR PIR; A38622; A38622. DR PIR; A40187; A40187. DR PIR; B40187; B40187. DR PDB; 1HUR; 10-JUL-95. DR PDB; 1RRF; 20-JUN-96. DR PDB; 1RRG; 20-JUN-96. DR MIM; 103180; -. DR MGD; MGI:99431; Arf1. DR INTERPRO; IPR000251; -. DR PFAM; PF00025; arf; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family; Myristate; Protein transport; KW Golgi stack; 3D-structure. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (POTENTIAL). FT NP_BIND 23 30 GTP (BY SIMILARITY). FT NP_BIND 66 70 GTP (BY SIMILARITY). FT NP_BIND 125 128 GTP (BY SIMILARITY). SQ SEQUENCE 180 AA; 20565 MW; 117A7399925C0404 CRC64; GNIFANLFKG LFGKKEMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI SFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRERVN EAREELMRML AEDELRDAVL LVFANKQDLP NAMNAAEITD KLGLHSLRHR NWYIQATCAT SGDGLYEGLD WLSNQLRNQK //