PRPS2_MOUSE
ID PRPS2_MOUSE Reviewed; 318 AA.
AC Q9CS42; Q9CZA9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 2;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase II;
DE Short=PRS-II;
GN Name=Prps2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 244-260, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP)
CC that is essential for nucleotide synthesis.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by magnesium and inorganic phosphate.
CC Competitively or non-competitively inhibited by ADP, 2,3-
CC bisphosphoglyceride or GDP (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC -!- SUBUNIT: Homodimer. The active form is probably a hexamer composed of 3
CC homodimers (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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; AK012819; BAB28492.1; -; mRNA.
DR EMBL; AK019169; BAB31583.2; -; mRNA.
DR EMBL; AK029690; BAC26565.1; -; mRNA.
DR EMBL; AK045007; BAC32182.1; -; mRNA.
DR EMBL; BC024942; AAH24942.1; -; mRNA.
DR CCDS; CCDS30532.1; -.
DR RefSeq; NP_001300687.1; NM_001313758.1.
DR RefSeq; NP_080938.1; NM_026662.5.
DR AlphaFoldDB; Q9CS42; -.
DR SMR; Q9CS42; -.
DR BioGRID; 225774; 23.
DR IntAct; Q9CS42; 2.
DR MINT; Q9CS42; -.
DR STRING; 10090.ENSMUSP00000026839; -.
DR iPTMnet; Q9CS42; -.
DR PhosphoSitePlus; Q9CS42; -.
DR SwissPalm; Q9CS42; -.
DR EPD; Q9CS42; -.
DR jPOST; Q9CS42; -.
DR MaxQB; Q9CS42; -.
DR PaxDb; Q9CS42; -.
DR PeptideAtlas; Q9CS42; -.
DR PRIDE; Q9CS42; -.
DR ProteomicsDB; 291565; -.
DR Antibodypedia; 8471; 248 antibodies from 29 providers.
DR DNASU; 110639; -.
DR Ensembl; ENSMUST00000026839; ENSMUSP00000026839; ENSMUSG00000025742.
DR GeneID; 110639; -.
DR KEGG; mmu:110639; -.
DR UCSC; uc009uxd.1; mouse.
DR CTD; 5634; -.
DR MGI; MGI:97776; Prps2.
DR VEuPathDB; HostDB:ENSMUSG00000025742; -.
DR eggNOG; KOG1448; Eukaryota.
DR GeneTree; ENSGT00950000182803; -.
DR HOGENOM; CLU_033546_4_0_1; -.
DR InParanoid; Q9CS42; -.
DR OMA; WSRAPIS; -.
DR OrthoDB; 1043963at2759; -.
DR PhylomeDB; Q9CS42; -.
DR TreeFam; TF106366; -.
DR Reactome; R-MMU-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR BioGRID-ORCS; 110639; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Prps2; mouse.
DR PRO; PR:Q9CS42; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CS42; protein.
DR Bgee; ENSMUSG00000025742; Expressed in gastrula and 240 other tissues.
DR Genevisible; Q9CS42; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IDA:MGI.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IDA:MGI.
DR GO; GO:0006167; P:AMP biosynthetic process; ISO:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0009165; P:nucleotide biosynthetic process; ISO:MGI.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; ISO:MGI.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="Ribose-phosphate pyrophosphokinase 2"
FT /id="PRO_0000141076"
FT REGION 212..227
FT /note="Binding of phosphoribosylpyrophosphate"
FT /evidence="ECO:0000255"
FT BINDING 96..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 318 AA; 34786 MW; 79675276E6667F3B CRC64;
MPNIVLFSGS SHQDLSQRVA DRLGLELGKV VTKKFSNQET SVEIGESVRG EDVYIIQSGC
GEINDNLMEL LIMINACKIA SSSRVTAVIP CFPYARQDKK DKSRAPISAK LVANMLSVAG
ADHIITMDLH ASQIQGFFDI PVDNLYAEPA VLQWIRENIT EWRNCIIVSP DAGGAKRVTS
IADRLNVEFA LIHKERKKAN EVDRMVLVGD VKDRVAILVD DMADTCGTIC HAADKLLSAG
ATKVYAILTH GIFSGPAISR INSAAFEAVV VTNTIPQEDK MKHCSKIQVI DISMILAEAI
RRTHNGESVS YLFSHVPL
