ID ARF4_HUMAN STANDARD; PRT; 179 AA. AC P18085; P21371; DT 01-MAY-1991 (Rel. 18, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE ADP-RIBOSYLATION FACTOR 4. GN ARF4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90192776; PubMed=2107548; RA Monaco L., Murtagh J.J. Jr., Newman K.B., Tsai S.-C., Moss J., RA Vaughan M.; RT "Selective amplification of an mRNA and related pseudogene for a human RT ADP-ribosylation factor, a guanine nucleotide-dependent protein RT activator of cholera toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2206-2210(1990). RN [2] RP SEQUENCE FROM N.A. 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). 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 -!- CAUTION: WAS ORIGINALLY THOUGHT TO BE ARF2. 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; M36341; AAA53081.1; -. DR PIR; A35091; A35091. DR PIR; B38622; B38622. DR HSSP; P32889; 1HUR. DR MIM; 601177; -. DR INTERPRO; IPR000251; -. DR PFAM; PF00025; arf; 1. DR PROSITE; PS01019; ARF; 1. KW GTP-binding; Multigene family; Myristate; Protein transport; KW Golgi stack. 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 179 AA; 20379 MW; D743A62B6A2AA912 CRC64; GLTISSLFSR LFGKKQMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI CFTVWDVGGQ DRIRPLWKHY FQNTQGLIFV VDSNDRERIQ EVADELQKML LVDELRDAVL LLFANKQDLP NAMAISEMTD KLGLQSLRNR TWYVQATCAT QGTGLYEGLD WLSNELSKR //