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UniProtKB/Swiss-Prot entry P36959


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

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Entry information
Entry name GMPR1_HUMAN
Primary accession number P36959
Secondary accession number Q96HQ6
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on June 1, 1994 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 87)
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
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1016/0092-8674(89)90440-6; PubMed=2758468 [NCBI, ExPASy, EBI, Israel, Japan]
Kanno H., Huang I.Y., Kan Y.W., Yoshida A.;
"Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase.";
Cell 58:595-606(1989).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=1661705 [NCBI, ExPASy, EBI, Israel, Japan]
Kondoh T., Kanno H., Chang L., Yoshida A.;
"Genomic structure and expression of human guanosine monophosphate reductase.";
Hum. Genet. 88:219-224(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-256.
TISSUE=Placenta;
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).
[5]
SIMILARITY TO GMP REDUCTASE.
DOI=10.1016/0092-8674(89)90498-4; PubMed=2570640 [NCBI, ExPASy, EBI, Israel, Japan]
Henikoff S., Smith J.M.;
"The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase.";
Cell 58:1021-1022(1989).
[6]
LACK OF ROLE IN G6PD.
DOI=10.1016/0092-8674(90)90233-5; PubMed=1694726 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshida A., Kan Y.W.;
"Origin of 'fused' glucose-6-phosphate dehydrogenase.";
Cell 62:11-12(1990).
[7]
VARIANTS THR-234 AND ILE-256.
PubMed=1757097 [NCBI, ExPASy, EBI, Israel, Japan]
Kondoh T., Kanno H., Chang L., Yoshida A.;
"Identification of common variant alleles of the human guanosine monophosphate reductase gene.";
Hum. Genet. 88:225-227(1991).
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.
  • CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.
  • SUBUNIT: Homotetramer.
  • POLYMORPHISM: At least two different alleles are known.
  • SIMILARITY: Belongs to the IMPDH/GMPR family.
  • CAUTION: The N-terminus was initially (Ref.1) thought to be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in vivo. However, Ref.5 showed that it encodes a GMP reductase, and Ref.6 showed that the chimeric protein is an artifact.
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
L35304; AAA52503.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27941; AAA53106.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24470; AAA52498.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009031; CAI21422.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138883; CAI21422.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL138883; CAI19917.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL009031; CAI19917.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008281; AAH08281.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B32902; B32902.
RefSeq NP_006868.3; -.
UniGene Hs.484741
3D structure databases
PDB
2BLE; X-ray; 1.90 A; A=1-345.[ExPASy / RCSB / EBI]
2BWG; X-ray; 2.40 A; A/B/C/D=1-345.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2BLE; -.
2BWG; -.
ModBase P36959.
PTM databases
PhosphoSite P36959; -.
Organism-specific databases
H-InvDB HIX0005598; -.
HGNC HGNC:4376; GMPR.
GenAtlas GMPR.
MIM 139265; gene. [NCBI / EBI]
PharmGKB PA28761; -.
GeneCards P36959.
Gene expression databases
ArrayExpress P36959; -.
CleanEx HS_GMPR; -.
GermOnline ENSG00000137198; Homo sapiens.
Ontologies
GO
GO:0003920; Molecular function: GMP reductase activity (traceable author statement from ProtInc).
GO:0009409; Biological process: response to cold (traceable author statement from ProtInc).
QuickGo view.
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 P36959.
Proteomic databases
PeptideAtlas P36959; -.
Genome annotation databases
Ensembl ENSG00000137198; Homo sapiens. [Contig view]
GeneID 2766; -.
KEGG hsa:2766; -.
Phylogenomic databases
HOGENOM P36959; -.
HOVERGEN P36959; -.
Other
SOURCE GMPR; Homo sapiens.
ProtoNet P36959.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Metal-binding; NADP; Oxidoreductase; Polymorphism; Potassium.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   345  345     GMP reductase 1. PRO_0000093723
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). 
VARIANT   234   234  1     A -> T. VAR_003969 [3D]
VARIANT   256   256  1     F -> I (in dbSNP:rs1042391 [NCBI]). VAR_003970 [3D]
STRAND   3     9  7      
HELIX   12    14  3      
STRAND   15    17  3      
HELIX   27    29  3      
STRAND   34    37  4      
TURN   39    41  3      
STRAND   44    47  4      
STRAND   50    52  3      
TURN   56    58  3      
HELIX   61    67  7      
HELIX   68    70  3      
STRAND   73    75  3      
HELIX   82    91  10      
HELIX   93    98  6      
STRAND   99   103  5      
HELIX   107   119  13      
STRAND   125   129  5      
HELIX   136   148  13      
STRAND   152   159  8      
HELIX   162   170  9      
STRAND   174   178  5      
HELIX   188   191  4      
HELIX   198   210  13      
TURN   211   213  3      
STRAND   215   220  6      
HELIX   225   234  10      
STRAND   237   242  6      
HELIX   243   245  3      
STRAND   251   253  3      
STRAND   263   267  5      
HELIX   272   277  6      
STRAND   285   288  4      
STRAND   292   296  5      
HELIX   301   319  19      
HELIX   324   326  3      
HELIX   327   330  4      
STRAND   332   337  6      
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 37419 Da [This is the MW of the unprocessed precursor] CRC64: 217E1A5A599CA510 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI IVANMDTVGT 

        70         80         90        100        110        120 
FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA VSSGSGQNDL EKMTSILEAV 

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

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

       250        260        270        280        290        300 
LGGMFSGHTE CAGEVFERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD 

       310        320        330        340 
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS 

P36959 in FASTA format

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View entry in raw text format (no links)
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