Q99L27 (GMPR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GMP reductase 2
EC=1.7.1.7

Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase 2
Short name=Guanosine monophosphate reductase 2

Gene names

Name:

Gmpr2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides By similarity.
Catalytic activity	Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.
Sequence similarities	Belongs to the IMPDH/GMPR family.

Ontologies

Keywords
Ligand	Metal-binding NADP Potassium
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleotide metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	GMP reductase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 348	348	GMP reductase 2		PRO_0000093727
Regions
	Nucleotide binding	108 – 131	24	NADP By similarity
Sites
	Active site	186	1	Thioimidate intermediate By similarity
	Metal binding	181	1	Potassium; via carbonyl oxygen By similarity
	Metal binding	183	1	Potassium; via carbonyl oxygen By similarity
	Binding site	219	1	NADP By similarity
Amino acid modifications
	Modified residue	13	1	N6-acetyllysine By similarity
	Modified residue	291	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	105	1	S → T in AAH03886. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q99L27 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 83E6998193D22FC0	FASTA	348	38,019
	10 20 30 40 50 60 MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV IAANMDTVGT 70 80 90 100 110 120 FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA ASSGSGSADF EQLEQILEAI 130 140 150 160 170 180 PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI 190 200 210 220 230 240 GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM 250 260 270 280 290 300 LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD 310 320 330 340 VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Pancreas and Thymus.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK031004 mRNA. Translation: BAC27211.1. AK075772 mRNA. Translation: BAC35946.1. CH466535 Genomic DNA. Translation: EDL36258.1. BC003886 mRNA. Translation: AAH03886.1. BC024109 mRNA. Translation: AAH24109.1.
IPI	IPI00116248.
RefSeq	NP_818773.1. NM_177992.2.
UniGene	Mm.390685.
3D structure databases
ProteinModelPortal	Q99L27.
SMR	Q99L27. Positions 10-337.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99L27.
PTM databases
PhosphoSite	Q99L27.
Proteomic databases
PRIDE	Q99L27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002397; ENSMUSP00000002397; ENSMUSG00000002326.
GeneID	105446.
KEGG	mmu:105446.
Organism-specific databases
CTD	51292.
MGI	MGI:1917903. Gmpr2.
Phylogenomic databases
GeneTree	ENSGT00530000062923.
HOGENOM	HBG298985.
HOVERGEN	HBG051744.
InParanoid	Q99L27.
OrthoDB	EOG4FXR7V.
PhylomeDB	Q99L27.
Gene expression databases
ArrayExpress	Q99L27.
Bgee	Q99L27.
CleanEx	MM_GMPR2.
Genevestigator	Q99L27.
GermOnline	ENSMUSG00000002326. Mus musculus.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR005993. GMP_reduct1. IPR015875. IMP_DH/GMP_Rdtase_CS. IPR001093. IMP_DH_GMPRt. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KO	K00364.
Pfam	PF00478. IMPDH. 1 hit. [Graphical view]
PIRSF	PIRSF000235. GMP_reductase. 1 hit.
TIGRFAMs	TIGR01305. GMP_reduct_1. 1 hit.
PROSITE	PS00487. IMP_DH_GMP_RED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GMPR2_MOUSE

Accession

Primary (citable) accession number: Q99L27
Secondary accession number(s): Q542X2, Q8R1T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	July 27, 2011
Last modified:	November 16, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program