ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9DCZ1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GMPR1_MOUSE
Primary accession number Q9DCZ1
Secondary accession numbers None
Integrated into Swiss-Prot on November 8, 2002
Sequence was last modified on June 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 52)
Name and origin of the protein
Protein name GMP reductase 1
Synonyms EC 1.7.1.7
Guanosine 5'-monophosphate oxidoreductase 1
Guanosine monophosphate reductase 1
Gene name
Name: Gmpr
Synonyms: Gmpr1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Heart, and Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK002326; BAB22014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK084508; BAC39203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010827; AAH10827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079784.1; -.
UniGene Mm.290802
3D structure databases
HSSP P49058; 1EEP. [HSSP ENTRY / PDB]
SMR Q9DCZ1; 1-343.
ModBase Q9DCZ1.
PTM databases
PhosphoSite Q9DCZ1; -.
Organism-specific databases
MGI MGI:1913605; Gmpr.
Gene expression databases
ArrayExpress Q9DCZ1; -.
CleanEx MM_GMPR; -.
GermOnline ENSMUSG00000000253; Mus musculus.
Family and domain databases
InterPro IPR013785; Aldolase_TIM.
IPR005993; GMP_reduct1.
IPR015875; IMP_DH/GMP_Rdtase_CS.
IPR001093; IMP_DHase_GMPRtase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF00478; IMPDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000235; GMP_reductase; 1.
TIGRFAMs TIGR01305; GMP_reduct_1; 1.
PROSITE PS00487; IMP_DH_GMP_RED; 1.
BLOCKS Q9DCZ1.
Genome annotation databases
Ensembl ENSMUSG00000000253; Mus musculus. [Contig view]
GeneID 66355; -.
KEGG mmu:66355; -.
Phylogenomic databases
HOGENOM Q9DCZ1; -.
HOVERGEN Q9DCZ1; -.
Other
SOURCE Gmpr; Mus musculus.
ProtoNet Q9DCZ1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Metal-binding; NADP; Oxidoreductase; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   345  345     GMP reductase 1. PRO_0000093724
NP_BIND   108   131  24     NADP (By similarity). 
ACT_SITE   186   186        Thioimidate intermediate (By similarity). 
METAL   181   181        Potassium (via carbonyl oxygen) (By similarity). 
METAL   183   183        Potassium (via carbonyl oxygen) (By similarity). 
BINDING   219   219        NADP (By similarity). 
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 37482 Da [This is the MW of the unprocessed precursor] CRC64: 9A801692C9284D72 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRIDADLKL DFKDVLLRPK RSSLKSRSEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT 

        70         80         90        100        110        120 
FEMAVVMSQH AMFTAVHKHY SLDDWKCFAE THPECLQHVA VSSGSGQNDL ERMSRILEAV 

       130        140        150        160        170        180 
PQVKFICLDV ANGYSEHFVE FVKLVRSKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV 

       190        200        210        220        230        240 
GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM 

       250        260        270        280        290        300 
LGGMFSGHTE CAGEVIERNG QKLKLFYGMS SDTAMKKHAG GVAEYRASEG KTVEVPYKGD 

       310        320        330        340 
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFG 

Q9DCZ1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!