PYRG1_MOUSE
ID PYRG1_MOUSE Reviewed; 591 AA.
AC P70698; Q922Y4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=CTP synthase 1 {ECO:0000305};
DE EC=6.3.4.2 {ECO:0000250|UniProtKB:P17812};
DE AltName: Full=CTP synthetase 1;
DE AltName: Full=UTP--ammonia ligase 1;
GN Name=Ctps1; Synonyms=Ctps {ECO:0000312|MGI:MGI:1858304};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Ding J.H., Yang B.Z., Zhang H., Roe C.R.;
RT "Molecular cloning of the mouse liver CTP synthetase cDNA.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-575 AND SER-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=25223282; DOI=10.15252/embr.201438688;
RA Strochlic T.I., Stavrides K.P., Thomas S.V., Nicolas E., O'Reilly A.M.,
RA Peterson J.R.;
RT "Ack kinase regulates CTP synthase filaments during Drosophila oogenesis.";
RL EMBO Rep. 15:1184-1191(2014).
CC -!- FUNCTION: This enzyme is involved in the de novo synthesis of CTP, a
CC precursor of DNA, RNA and phospholipids. Catalyzes the ATP-dependent
CC amination of UTP to CTP with either L-glutamine or ammonia as a source
CC of nitrogen. This enzyme and its product, CTP, play a crucial role in
CC the proliferation of activated lymphocytes and therefore in immunity.
CC {ECO:0000250|UniProtKB:P17812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC Evidence={ECO:0000250|UniProtKB:P17812};
CC -!- ACTIVITY REGULATION: Activated by GTP and inhibited by CTP.
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000250|UniProtKB:P17812}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25223282}.
CC Note=Mainly cytosolic but when active detected in long filamentous
CC structures (By similarity). Co-localizes with TNK2 in the cytosolic
CC filaments (PubMed:25223282). {ECO:0000250|UniProtKB:P17812,
CC ECO:0000269|PubMed:25223282}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; U49350; AAB06942.1; -; mRNA.
DR EMBL; AK148259; BAE28443.1; -; mRNA.
DR EMBL; BC006698; AAH06698.1; -; mRNA.
DR CCDS; CCDS18591.1; -.
DR RefSeq; NP_058028.2; NM_016748.2.
DR RefSeq; XP_006503288.1; XM_006503225.3.
DR PDB; 7MIP; EM; 2.40 A; C/D/G/I=1-591.
DR PDBsum; 7MIP; -.
DR AlphaFoldDB; P70698; -.
DR SMR; P70698; -.
DR BioGRID; 206180; 69.
DR IntAct; P70698; 2.
DR STRING; 10090.ENSMUSP00000030381; -.
DR MEROPS; C26.A36; -.
DR iPTMnet; P70698; -.
DR PhosphoSitePlus; P70698; -.
DR SwissPalm; P70698; -.
DR EPD; P70698; -.
DR jPOST; P70698; -.
DR MaxQB; P70698; -.
DR PaxDb; P70698; -.
DR PeptideAtlas; P70698; -.
DR PRIDE; P70698; -.
DR ProteomicsDB; 300329; -.
DR Antibodypedia; 4476; 181 antibodies from 32 providers.
DR DNASU; 51797; -.
DR Ensembl; ENSMUST00000030381; ENSMUSP00000030381; ENSMUSG00000028633.
DR GeneID; 51797; -.
DR KEGG; mmu:51797; -.
DR UCSC; uc008unj.2; mouse.
DR CTD; 51797; -.
DR MGI; MGI:1858304; Ctps.
DR VEuPathDB; HostDB:ENSMUSG00000028633; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; P70698; -.
DR OMA; EFNNAYR; -.
DR OrthoDB; 810128at2759; -.
DR PhylomeDB; P70698; -.
DR TreeFam; TF300379; -.
DR BRENDA; 6.3.4.2; 3474.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR UniPathway; UPA00159; UER00277.
DR BioGRID-ORCS; 51797; 25 hits in 80 CRISPR screens.
DR ChiTaRS; Ctps; mouse.
DR PRO; PR:P70698; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P70698; protein.
DR Bgee; ENSMUSG00000028633; Expressed in presomitic mesoderm and 264 other tissues.
DR Genevisible; P70698; MM.
DR GO; GO:0097268; C:cytoophidium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
DR GO; GO:0006241; P:CTP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; ISS:UniProtKB.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01227; PyrG; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Glutamine amidotransferase; Immunity; Ligase; Nucleotide-binding;
KW Phosphoprotein; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..591
FT /note="CTP synthase 1"
FT /id="PRO_0000138276"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT REGION 562..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17812"
FT CONFLICT 37
FT /note="I -> F (in Ref. 1; AAB06942)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="T -> P (in Ref. 1; AAB06942)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="A -> S (in Ref. 1; AAB06942)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="M -> I (in Ref. 1; AAB06942)"
FT /evidence="ECO:0000305"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 262..269
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 298..307
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 447..457
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 472..484
FT /evidence="ECO:0007829|PDB:7MIP"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 489..494
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 506..518
FT /evidence="ECO:0007829|PDB:7MIP"
FT STRAND 520..525
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 538..547
FT /evidence="ECO:0007829|PDB:7MIP"
FT HELIX 551..556
FT /evidence="ECO:0007829|PDB:7MIP"
SQ SEQUENCE 591 AA; 66682 MW; 81083429870BF0DE CRC64;
MKYILVTGGV ISGIGKGVIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV
LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK ERKGDYLGKT VQVVPHITDA
IQEWVMRQAL IPVDEDGLEP QVCVIELGGT VGDIESMPFI EAFRQFQFKV KRENFCNIHV
SLVPQPSSTG EQKTKPTQNS VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ
VICVHDVSSI YRVPLLLEEQ GVVDYFLRRL DLPIERQSRK MLMKWKEMAD RYDRLLETCS
IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDST DLEPSTLQEE PVRYHEAWQK
LCSAHGVLVP GGFGVRGTEG KIQAIAWARK QKKPFLGVCL GMQLAVVEFS RNVLGWQDAN
STEFDPKTSH PVVIDMPEHN PGQMGGTMRL GKRRTLFQTK NSVMRKLYGD TDYLEERHRH
RFEVNPVLKK CLEEQGLKFV GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY
FGLLLASVGR LPHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSISQ D
