GMPR2_MOUSE
ID GMPR2_MOUSE Reviewed; 348 AA.
AC Q99L27; Q542X2; Q8R1T5;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=GMP reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=GMPR 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_03195};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=Guanosine monophosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
GN Name=Gmpr2 {ECO:0000255|HAMAP-Rule:MF_03195};
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=Pancreas, and Thymus;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, 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 irreversible NADPH-dependent deamination of GMP
CC to IMP. It functions in the conversion of nucleobase, nucleoside and
CC nucleotide derivatives of G to A nucleotides, and in maintaining the
CC intracellular balance of A and G nucleotides (Probable). Plays a role
CC in modulating cellular differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2T1, ECO:0000255|HAMAP-Rule:MF_03195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:58349; EC=1.7.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03195};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03195}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03195}.
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DR EMBL; AK031004; BAC27211.1; -; mRNA.
DR EMBL; AK075772; BAC35946.1; -; mRNA.
DR EMBL; CH466535; EDL36258.1; -; Genomic_DNA.
DR EMBL; BC003886; AAH03886.1; -; mRNA.
DR EMBL; BC024109; AAH24109.1; -; mRNA.
DR CCDS; CCDS27124.1; -.
DR RefSeq; NP_818773.1; NM_177992.2.
DR RefSeq; XP_006518429.1; XM_006518366.1.
DR AlphaFoldDB; Q99L27; -.
DR SMR; Q99L27; -.
DR BioGRID; 222860; 2.
DR STRING; 10090.ENSMUSP00000002397; -.
DR iPTMnet; Q99L27; -.
DR PhosphoSitePlus; Q99L27; -.
DR EPD; Q99L27; -.
DR jPOST; Q99L27; -.
DR MaxQB; Q99L27; -.
DR PaxDb; Q99L27; -.
DR PeptideAtlas; Q99L27; -.
DR PRIDE; Q99L27; -.
DR ProteomicsDB; 267637; -.
DR Antibodypedia; 61; 116 antibodies from 18 providers.
DR DNASU; 105446; -.
DR Ensembl; ENSMUST00000002397; ENSMUSP00000002397; ENSMUSG00000002326.
DR GeneID; 105446; -.
DR KEGG; mmu:105446; -.
DR UCSC; uc007uae.1; mouse.
DR CTD; 51292; -.
DR MGI; MGI:1917903; Gmpr2.
DR VEuPathDB; HostDB:ENSMUSG00000002326; -.
DR eggNOG; KOG2550; Eukaryota.
DR GeneTree; ENSGT00940000159574; -.
DR HOGENOM; CLU_022552_5_3_1; -.
DR InParanoid; Q99L27; -.
DR OMA; GSHCTTR; -.
DR OrthoDB; 618077at2759; -.
DR PhylomeDB; Q99L27; -.
DR TreeFam; TF300378; -.
DR Reactome; R-MMU-74217; Purine salvage.
DR BioGRID-ORCS; 105446; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gmpr2; mouse.
DR PRO; PR:Q99L27; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99L27; protein.
DR Bgee; ENSMUSG00000002326; Expressed in spermatocyte and 257 other tissues.
DR ExpressionAtlas; Q99L27; baseline and differential.
DR Genevisible; Q99L27; MM.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046038; P:GMP catabolic process; ISO:MGI.
DR GO; GO:0046037; P:GMP metabolic process; ISS:UniProtKB.
DR GO; GO:0032264; P:IMP salvage; TAS:MGI.
DR GO; GO:0030224; P:monocyte differentiation; ISO:MGI.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00596; GMP_reduct_type1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005993; GMPR.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; NADP; Oxidoreductase; Potassium;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..348
FT /note="GMP reductase 2"
FT /id="PRO_0000093727"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 26..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 129..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 180..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 189
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 219..221
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 242..243
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 268..270
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 285..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 286..290
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 314..317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2T1"
FT CONFLICT 105
FT /note="S -> T (in Ref. 3; AAH03886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 38019 MW; 83E6998193D22FC0 CRC64;
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV IAANMDTVGT
FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA ASSGSGSADF EQLEQILEAI
PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD
VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ
