ID ARF4_MOUSE STANDARD; PRT; 179 AA. AC P36403; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE ADP-RIBOSYLATION FACTOR 4. GN ARF4. OS Mus musculus (Mouse), and Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; 10116; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Rat; TISSUE=TESTIS; RX MEDLINE=93054784; PubMed=1358888; RA Mishima K., Price S.R., Nightingale M.S., Kousvelari E., Moss J., RA Vaughan M.; RT "Regulation of ADP-ribosylation factor (ARF) expression. Cross-species RT conservation of the developmental and tissue-specific alternative RT polyadenylation of ARF 4 mRNA."; RL J. Biol. Chem. 267:24109-24116(1992). RN [2] 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 [3] 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). 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; L12383; AAA40688.1; -. DR EMBL; D87901; BAA13493.1; -. DR HSSP; P32889; 1RRF. DR MGD; MGI:99433; Arf4. 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; 20265 MW; E4116423854CA71D CRC64; GLTISSLFSR LFGKKQMRIL MVGLDAAGKT TILYKLKLGE IVTTIPTIGF NVETVEYKNI CFTVWDVGGQ DKIRPLWRHY FQNTQGLIFV VDSNDRERIQ EGAAVLQKML LEDELQDAVL LLFANKQDLP NAMAISEMTD KLGLQSLRNR TWYVQATCAT QGTGLYEGLD WLSNELSKR //