ID PUA1_MOUSE STANDARD; PRT; 457 AA. AC P28650; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-NOV-1997 (REL. 35, LAST ANNOTATION UPDATE) DE ADENYLOSUCCINATE SYNTHETASE, MUSCLE ISOZYME (EC 6.3.4.4) (IMP-- DE ASPARTATE LIGASE). GN ADSS1. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; OC RODENTIA; SCIUROGNATHI; MURIDAE; MURINAE; MUS. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MUSCLE; RX MEDLINE; 92042206. RA GUICHERIT O.M., RUDOLPH F.B., KELLEMS R.E., COOPER B.F.; RT "Molecular cloning and expression of a mouse muscle cDNA encoding RT adenylosuccinate synthetase."; RL J. BIOL. CHEM. 266:22582-22587(1991). RN [2] RP REVISIONS. RX MEDLINE; 94140883. RA GUICHERIT O.M., COOPER B.F., RUDOLPH F.B., KELLEMS R.E.; RT "Amplification of an adenylosuccinate synthetase gene in alanosine- RT resistant murine T-lymphoma cells. Molecular cloning of a cDNA RT encoding the 'non-muscle' isozyme."; RL J. BIOL. CHEM. 269:4488-4496(1994). CC -!- FUNCTION: PLAYS AN IMPORTANT ROLE IN THE DE NOVO PATHWAY OF PURINE CC NUCLEOTIDE BIOSYNTHESIS. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-ASPARTATE = GDP + CC ORTHOPHOSPHATE + ADENYLOSUCCINATE. CC -!- PATHWAY: FIRST COMMITTED STEP IN AMP BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC, AND PARTIALLY ASSOCIATED WITH CC PARTICULATE FRACTIONS. CC -!- TISSUE SPECIFICITY: HIGH LEVEL IN MUSCLE. CC -!- SIMILARITY: WITH OTHER ADENYLOSUCCINATE SYNTHETASES. 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 -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M74495; G404751; -. DR PIR; A39317; AJMSDS. DR MGD; MGI:87947; ADSS1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PFAM; PF00709; Adenylsucc_synt; 1. DR HSSP; P12283; 1ADI. KW PURINE BIOSYNTHESIS; LIGASE; GTP-BINDING; MULTIGENE FAMILY. FT NP_BIND 42 48 GTP (POTENTIAL). FT ACT_SITE 174 174 BY SIMILARITY. FT ACT_SITE 181 181 BY SIMILARITY. SQ SEQUENCE 457 AA; 50254 MW; 26D05DAB CRC32; MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF //