EzCatDB: M00143
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DB codeM00143
CATH domainDomain 13.40.50.9600 : Rossmann fold
Domain 23.40.50.2300 : Rossmann fold
Domain 33.30.200.- : Phosphorylase Kinase; domain 1
Domain 41.10.510.- : Transferase(Phosphotransferase); domain 1
Domain 53.30.70.- : Alpha-Beta Plaits
E.C.4.6.1.2

CATH domainRelated DB codes (homologues)
3.40.50.2300 : Rossmann foldD00144

Enzyme Name
UniProtKBKEGG

P18910
Protein nameAtrial natriuretic peptide receptor 1guanylate cyclase
guanylyl cyclase
guanyl cyclase
GTP diphosphate-lyase (cyclizing)
SynonymsEC 4.6.1.2
Atrial natriuretic peptide receptor type A
ANP-A
ANPR-A
NPR-A
Guanylate cyclase A
GC-A
RefSeqNP_036745.1 (Protein)
NM_012613.1 (DNA/RNA sequence)
PfamPF01094 (ANF_receptor)
PF00211 (Guanylate_cyc)
PF07714 (Pkinase_Tyr)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism

UniProtKB:Accession NumberP18910
Entry nameANPRA_RAT
ActivityGTP = 3'',5''-cyclic GMP + diphosphate.
SubunitHomodimer.
Subcellular locationMembrane, Single-pass type I membrane protein.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00044C00081C00286C00013C00942C00943C02507
CompoundGTPITPdGTPPyrophosphate3',5'-Cyclic GMP3',5'-Cyclic IMP3',5'-Cyclic dGMP
Typeamide group,amine group,nucleotideamide group,nucleotideamide group,amine group,nucleotidephosphate group/phosphate ionamide group,amine group,nucleotideamide group,nucleotideamide group,amine group,nucleotide
ChEBI15996
16039
16497
29888
16356
27541

PubChem6830
8583
65103
21961011
1023
24316
19069
439740
               
1dp4A01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dp4C01UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dp4A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1dp4C02UnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
pdb
        
1dp4A01
1dp4C01
1dp4A02
1dp4C02


references
[1]
PubMed ID7827054
JournalBiochemistry
Year1995
Volume34
Pages955-64
AuthorsMimeault M, De Lean A, Lafleur M, Bonenfant D, Fournier A
TitleEvaluation of conformational and binding characteristics of various natriuretic peptides and related analogs.
[2]
PubMed ID7721418
JournalHypertension
Year1995
Volume25
Pages694-8
AuthorsMiao ZH, Song DL, Douglas JG, Chang CH
TitleMutational inactivation of the catalytic domain of guanylate cyclase-A receptor.
[3]
PubMed ID8713120
JournalBiochem Biophys Res Commun
Year1996
Volume224
Pages765-71
AuthorsThorpe DS, Niu S, Morkin E
TitleRefolding parameters for the allosteric homodimeric guanylyl cyclase catalytic core from the atrial natriuretic peptide receptor.
[4]
PubMed ID9914494
JournalEur J Biochem
Year1999
Volume259
Pages204-11
AuthorsKashiwagi M, Miyamoto K, Takei Y, Hirose S
TitleCloning, properties and tissue distribution of natriuretic peptide receptor-A of euryhaline eel, Anguilla japonica.
[5]
PubMed ID11078709
JournalAm J Physiol Cell Physiol
Year2000
Volume279
PagesC1938-45
AuthorsNara M, Dhulipala PD, Ji GJ, Kamasani UR, Wang YX, Matalon S, Kotlikoff MI
TitleGuanylyl cyclase stimulatory coupling to K(Ca) channels.
[6]
PubMed ID10971587
JournalEur J Biochem
Year2000
Volume267
Pages5758-68
AuthorsMiyagi M, Zhang X, Misono KS
TitleGlycosylation sites in the atrial natriuretic peptide receptor: oligosaccharide structures are not required for hormone binding.
[7]
PubMed ID10648635
JournalMol Pharmacol
Year2000
Volume57
Pages259-67
AuthorsPandey KN, Kumar R, Li M, Nguyen H
TitleFunctional domains and expression of truncated atrial natriuretic peptide receptor-A: the carboxyl-terminal regions direct the receptor internalization and sequestration in COS-7 cells.
[8]
CommentsX-ray crystallography
PubMed ID10894551
JournalNature
Year2000
Volume406
Pages101-4
Authorsvan den Akker F, Zhang X, Miyagi M, Huo X, Misono KS, Yee VC
TitleStructure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor.
Related PDB1dp4
[9]
PubMed ID11558678
JournalCan J Physiol Pharmacol
Year2001
Volume79
Pages692-704
Authorsvan den Akker F
TitleDetailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure.
[10]
PubMed ID11306239
JournalCell Signal
Year2001
Volume13
Pages221-31
AuthorsSilberbach M, Roberts CT Jr
TitleNatriuretic peptide signalling: molecular and cellular pathways to growth regulation.
[11]
PubMed ID11556325
JournalJ Mol Biol
Year2001
Volume311
Pages923-37
Authorsvan den Akker F
TitleStructural insights into the ligand binding domains of membrane bound guanylyl cyclases and natriuretic peptide receptors.
[12]
PubMed ID11269661
JournalMol Cell Biochem
Year2001
Volume217
Pages165-72
AuthorsDuda T, Yadav P, Jankowska A, Venkataraman V, Sharma RK
TitleThree dimensional atomic model and experimental validation for the ATP-Regulated Module (ARM) of the atrial natriuretic factor receptor guanylate cyclase.
[13]
PubMed ID11573084
JournalNat Struct Biol
Year2001
Volume8
Pages832
AuthorsHollien J
TitlePicture story. A hormone receptor springs into action.
[14]
PubMed ID11533490
JournalScience
Year2001
Volume293
Pages1657-62
AuthorsHe Xl, Chow Dc, Martick MM, Garcia KC
TitleAllosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
[15]
PubMed ID11952096
JournalMol Cell Biochem
Year2002
Volume230
Pages49-60
AuthorsMisono KS
TitleNatriuretic peptide receptor: structure and signaling.
[16]
PubMed ID11952097
JournalMol Cell Biochem
Year2002
Volume230
Pages61-72
AuthorsPandey KN
TitleIntracellular trafficking and metabolic turnover of ligand-bound guanylyl cyclase/atrial natriuretic peptide receptor-A into subcellular compartments.

comments
This enzyme is composed of N-terminal extracellular region and C-terminal intracellular region, which has a protein-kinase like domain and a guanylate-cyclase domain. The PDB structure, 1dp4, corresponds to the N-terminal extracellular region, which is hormone-binding domain (see [8] & [9]). Thus, the structure of the catalytic domain of this enzyme has not been determined yet.
This enzyme catalyzes an intramolecular transfer reaction, rather than an elimination reaction.

createdupdated
2004-07-152009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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