ID PUA1_MOUSE STANDARD; PRT; 457 AA. AC P28650; Q8CHQ1; DT 01-DEC-1992 (Rel. 24, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Adenylosuccinate synthetase, muscle isozyme (EC 6.3.4.4) (IMP-- DE aspartate ligase 1) (AdSS 1) (AMPSase 1). GN ADSS1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RC TISSUE=Muscle; RX MEDLINE=92042206; PubMed=1939273; 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; PubMed=8308018; 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). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC STRAIN=Czech II; TISSUE=Breast tumor; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=12004071; RA Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.; RT "IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle RT adenylosuccinate synthetase."; RL J. Biol. Chem. 277:26779-26787(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=12186864; RA Iancu C.V., Borza T., Fromm H.J., Honzatko R.B.; RT "Feedback inhibition and product complexes of recombinant mouse muscle RT adenylosuccinate synthetase."; RL J. Biol. Chem. 277:40536-40543(2002). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + CC adenylosuccinate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit. CC -!- PATHWAY: AMP biosynthesis; first committed step. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic, and partially associated with CC particulate fractions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P28650-1; Sequence=Displayed; CC Name=2; CC IsoId=P28650-2; Sequence=VSP_008422; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: High levels in muscle. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. 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; AAA82870.1; -. DR EMBL; BC039943; AAH39943.1; -. DR PIR; A39317; AJMSDS. DR PDB; 1IWE; 28-AUG-02. DR PDB; 1J4B; 21-NOV-01. DR PDB; 1LNY; 28-AUG-02. DR PDB; 1LON; 28-AUG-02. DR PDB; 1LOO; 28-AUG-02. DR PDB; 1MEZ; 30-OCT-02. DR PDB; 1MF0; 30-OCT-02. DR PDB; 1MF1; 30-OCT-02. DR MGD; MGI:87947; Adss1. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IDA. DR GO; GO:0005515; F:protein binding activity; IPI. DR InterPro; IPR001114; Asucc_synthtase. DR Pfam; PF00709; Adenylsucc_synt; 1. DR ProDom; PD001188; Asucc_synthtase; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. KW Purine biosynthesis; Ligase; GTP-binding; Metal-binding; Magnesium; KW 3D-structure; Alternative splicing. FT NP_BIND 42 48 GTP (POTENTIAL). FT ACT_SITE 174 174 BY SIMILARITY. FT ACT_SITE 181 181 BY SIMILARITY. FT METAL 43 43 MAGNESIUM. FT METAL 70 70 MAGNESIUM (VIA CARBONYL OXYGEN). FT VARSPLIC 136 136 L -> LENEVPHEPLPSASLLPMCWLLAP (in FT isoform 2). FT /FTId=VSP_008422. SQ SEQUENCE 457 AA; 50254 MW; EBEC85BF907B7FED CRC64; 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 //