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 05-JUL-2004 (Rel. 44, Last annotation update) DE Adenylosuccinate synthetase, muscle isozyme (EC 6.3.4.4) (IMP-- DE aspartate ligase 1) (AdSS 1) (AMPSase 1). GN Name=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; DOI=10.1073/pnas.242603899; 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 MEDLINE=22128853; PubMed=12004071; DOI=10.1074/jbc.M203730200; 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 MEDLINE=22287400; PubMed=12186864; DOI=10.1074/jbc.M204952200; 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; IPI. DR GO; GO:0006164; P:purine nucleotide biosynthesis; IDA. DR InterPro; IPR001114; Asucc_synthtase. DR Pfam; PF00709; Adenylsucc_synt; 1. DR ProDom; PD001188; Asucc_synthtase; 1. DR TIGRFAMs; TIGR00184; purA; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1. KW 3D-structure; Alternative splicing; GTP-binding; Ligase; Magnesium; KW Metal-binding; Purine biosynthesis. 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 isoform FT 2). FT /FTId=VSP_008422. FT STRAND 33 38 FT HELIX 46 54 FT TURN 55 56 FT STRAND 59 62 FT STRAND 65 65 FT TURN 67 68 FT STRAND 71 74 FT STRAND 79 82 FT HELIX 87 90 FT TURN 92 93 FT STRAND 95 98 FT TURN 100 101 FT STRAND 102 104 FT HELIX 106 117 FT TURN 118 120 FT HELIX 124 126 FT STRAND 128 131 FT TURN 132 133 FT STRAND 135 136 FT HELIX 139 155 FT HELIX 167 176 FT TURN 177 177 FT STRAND 181 181 FT HELIX 182 185 FT TURN 186 186 FT HELIX 189 205 FT TURN 208 209 FT HELIX 214 228 FT HELIX 229 231 FT STRAND 232 233 FT HELIX 235 244 FT STRAND 250 253 FT HELIX 258 260 FT TURN 262 264 FT TURN 267 268 FT TURN 277 277 FT HELIX 278 284 FT TURN 285 285 FT HELIX 288 290 FT STRAND 291 299 FT STRAND 302 304 FT TURN 311 312 FT STRAND 313 313 FT HELIX 317 325 FT TURN 326 327 FT STRAND 329 329 FT TURN 331 333 FT STRAND 336 336 FT STRAND 338 340 FT STRAND 342 343 FT HELIX 344 354 FT STRAND 358 362 FT HELIX 364 367 FT TURN 368 369 FT STRAND 372 381 FT TURN 382 383 FT STRAND 384 385 FT TURN 393 394 FT HELIX 395 398 FT STRAND 400 407 FT TURN 414 415 FT HELIX 419 421 FT HELIX 424 437 FT TURN 438 438 FT STRAND 441 445 FT TURN 450 452 FT STRAND 453 455 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 //