PYRG2_MOUSE
ID PYRG2_MOUSE Reviewed; 586 AA.
AC P70303; Q3TPQ2; Q3TT59;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=CTP synthase 2;
DE EC=6.3.4.2;
DE AltName: Full=CTP synthetase 2;
DE Short=CTPsH;
DE AltName: Full=UTP--ammonia ligase 2;
GN Name=Ctps2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J X CBA/J; TISSUE=Liver;
RA Yang B.Z., Ding J.H., Roe C.R., Zhang H., Cooney D.A., Roller P.P.,
RA Johns D.G.;
RT "Identification and characterization of a novel gene (CTPsH) homologous to
RT murine CTP synthetase gene.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Heart, Hippocampus, and Medulla oblongata;
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] (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 AND SER-574, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
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).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Constitutes
CC the rate-limiting enzyme in the synthesis of cytosine nucleotides (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P70303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70303-2; Sequence=VSP_019894;
CC Name=3;
CC IsoId=P70303-3; Sequence=VSP_019893, VSP_019895, VSP_019896;
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}.
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DR EMBL; U49385; AAB17729.1; -; mRNA.
DR EMBL; AK032018; BAC27651.1; -; mRNA.
DR EMBL; AK052854; BAC35174.1; -; mRNA.
DR EMBL; AK084595; BAC39223.1; -; mRNA.
DR EMBL; AK150966; BAE29997.1; -; mRNA.
DR EMBL; AK151597; BAE30537.1; -; mRNA.
DR EMBL; AK161564; BAE36466.1; -; mRNA.
DR EMBL; AK164206; BAE37683.1; -; mRNA.
DR EMBL; BC003257; AAH03257.1; -; mRNA.
DR CCDS; CCDS41202.1; -. [P70303-1]
DR CCDS; CCDS53240.1; -. [P70303-2]
DR RefSeq; NP_001162040.1; NM_001168568.1. [P70303-1]
DR RefSeq; NP_001162041.1; NM_001168569.1. [P70303-1]
DR RefSeq; NP_001162043.1; NM_001168571.1. [P70303-2]
DR RefSeq; NP_061207.1; NM_018737.5. [P70303-1]
DR RefSeq; XP_006528975.1; XM_006528912.2. [P70303-1]
DR RefSeq; XP_006528976.1; XM_006528913.2. [P70303-1]
DR PDB; 7MIU; EM; 2.60 A; C/D/G/H=1-586.
DR PDB; 7MIV; EM; 2.80 A; C/D/G/H=1-586.
DR PDBsum; 7MIU; -.
DR PDBsum; 7MIV; -.
DR AlphaFoldDB; P70303; -.
DR SMR; P70303; -.
DR BioGRID; 207735; 23.
DR STRING; 10090.ENSMUSP00000033727; -.
DR MEROPS; C26.A36; -.
DR iPTMnet; P70303; -.
DR PhosphoSitePlus; P70303; -.
DR EPD; P70303; -.
DR MaxQB; P70303; -.
DR PaxDb; P70303; -.
DR PeptideAtlas; P70303; -.
DR PRIDE; P70303; -.
DR ProteomicsDB; 300214; -. [P70303-1]
DR ProteomicsDB; 300215; -. [P70303-2]
DR ProteomicsDB; 300216; -. [P70303-3]
DR Antibodypedia; 337; 209 antibodies from 27 providers.
DR DNASU; 55936; -.
DR Ensembl; ENSMUST00000033727; ENSMUSP00000033727; ENSMUSG00000031360. [P70303-1]
DR Ensembl; ENSMUST00000101095; ENSMUSP00000098656; ENSMUSG00000031360. [P70303-3]
DR Ensembl; ENSMUST00000112301; ENSMUSP00000107920; ENSMUSG00000031360. [P70303-1]
DR Ensembl; ENSMUST00000112302; ENSMUSP00000107921; ENSMUSG00000031360. [P70303-2]
DR Ensembl; ENSMUST00000112303; ENSMUSP00000107922; ENSMUSG00000031360. [P70303-1]
DR GeneID; 55936; -.
DR KEGG; mmu:55936; -.
DR UCSC; uc009uuo.2; mouse. [P70303-1]
DR UCSC; uc012hrk.1; mouse. [P70303-2]
DR CTD; 56474; -.
DR MGI; MGI:1933185; Ctps2.
DR VEuPathDB; HostDB:ENSMUSG00000031360; -.
DR eggNOG; KOG2387; Eukaryota.
DR GeneTree; ENSGT00910000144179; -.
DR HOGENOM; CLU_011675_5_0_1; -.
DR InParanoid; P70303; -.
DR OMA; FKPGTEW; -.
DR OrthoDB; 810128at2759; -.
DR PhylomeDB; P70303; -.
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; 55936; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Ctps2; mouse.
DR PRO; PR:P70303; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70303; protein.
DR Bgee; ENSMUSG00000031360; Expressed in granulocyte and 263 other tissues.
DR ExpressionAtlas; P70303; baseline and differential.
DR Genevisible; P70303; MM.
DR GO; GO:0097268; C:cytoophidium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IBA:GO_Central.
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:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
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 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; Alternative splicing; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Phosphoprotein;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..586
FT /note="CTP synthase 2"
FT /id="PRO_0000247034"
FT DOMAIN 300..554
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 399
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 526
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 528
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1
FT /note="M -> MGSELLGKNSALFSSFPTFCGGGPLGCTVADGQTFMIASGYWQSPIR
FT PPM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019893"
FT VAR_SEQ 465..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019894"
FT VAR_SEQ 465..472
FT /note="KKLYGDVP -> SLYLQCSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019895"
FT VAR_SEQ 473..586
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019896"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 311..314
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 351..362
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 378..390
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 400..413
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 449..457
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 463..467
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 472..484
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:7MIU"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 527..530
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 538..547
FT /evidence="ECO:0007829|PDB:7MIU"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:7MIU"
FT HELIX 551..556
FT /evidence="ECO:0007829|PDB:7MIU"
SQ SEQUENCE 586 AA; 65514 MW; 52EC0237B84A05F9 CRC64;
MKYILVTGGV ISGIGKGIIA SSIGTILKSC GLRVTAIKID PYINIDAGTF SPYEHGEVFV
LNDGGEVDLD LGNYERFLDI NLYKDNNITT GKIYQHVINK ERRGDYLGKT VQVVPHITDA
IQEWVMNQAK VSVDGNKEDP QICVIELGGT IGDIEGMAFV EAFRQFQFKA KKENFYNIHV
SLVPQPSATG EQKTKPTQNS VRALRGLGLS PDLIVCRSST PIEMAVKEKI SMFCHVNPEQ
VICIHDVSSI YRVPLLLEEQ GVVKYFQERL GLPINDCSSN LLFKWKAMAD RYERLQKICS
IALVGKYTKL RDCYASVFKA LEHSALAINH KLNLMYIDSI DLEPVTKAED PVKFHEAWQK
LCLADGILVP GGFGIRGTLG KLQAISWART KKIPFLGICL GMQLAVIEFA RNCLNLKDAN
STEFEPNTPV PLVIDMPEHN PGDLGGTMRL GLRRTVFTTE NSILKKLYGD VPYIEERHRH
RYEVNPNLIN QFENKDLCFV GEDVDGKRME IVELTSHPYF IGVQFHPEFS SRPMKPSPPY
LGLLLAATGN LNAHLQQMNK LPYSDGYSDA SDDSFPEAKL AELDLN
