DB code: M00143

CATH domain 3.40.50.9600 : Rossmann fold
3.40.50.2300 : Rossmann fold
3.30.200.- : Phosphorylase Kinase; domain 1
1.10.510.- : Transferase(Phosphotransferase); domain 1
3.30.70.- : Alpha-Beta Plaits
E.C. 4.6.1.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.2300 : Rossmann fold D00144

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P18910 Atrial natriuretic peptide receptor 1
EC 4.6.1.2
Atrial natriuretic peptide receptor type A
ANP-A
ANPR-A
NPR-A
Guanylate cyclase A
GC-A
NP_036745.1 (Protein)
NM_012613.1 (DNA/RNA sequence)
PF01094 (ANF_receptor)
PF00211 (Guanylate_cyc)
PF07714 (Pkinase_Tyr)
[Graphical View]

KEGG enzyme name
guanylate cyclase
guanylyl cyclase
guanyl cyclase
GTP diphosphate-lyase (cyclizing)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P18910 ANPRA_RAT GTP = 3'',5''-cyclic GMP + diphosphate. Homodimer. Membrane, Single-pass type I membrane protein.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00044 C00081 C00286 C00013 C00942 C00943 C02507
E.C.
Compound GTP ITP dGTP Pyrophosphate 3',5'-Cyclic GMP 3',5'-Cyclic IMP 3',5'-Cyclic dGMP
Type amide group,amine group,nucleotide amide group,nucleotide amide group,amine group,nucleotide phosphate group/phosphate ion amide group,amine group,nucleotide amide group,nucleotide amide group,amine group,nucleotide
ChEBI 15996
16039
16497
29888
16356
27541
PubChem 6830
8583
65103
1023
21961011
24316
19069
439740
1dp4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dp4C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dp4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1dp4C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dp4A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dp4C01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dp4A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dp4C02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 7827054
Journal Biochemistry
Year 1995
Volume 34
Pages 955-64
Authors Mimeault M, De Lean A, Lafleur M, Bonenfant D, Fournier A
Title Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7721418
Journal Hypertension
Year 1995
Volume 25
Pages 694-8
Authors Miao ZH, Song DL, Douglas JG, Chang CH
Title Mutational inactivation of the catalytic domain of guanylate cyclase-A receptor.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8713120
Journal Biochem Biophys Res Commun
Year 1996
Volume 224
Pages 765-71
Authors Thorpe DS, Niu S, Morkin E
Title Refolding parameters for the allosteric homodimeric guanylyl cyclase catalytic core from the atrial natriuretic peptide receptor.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9914494
Journal Eur J Biochem
Year 1999
Volume 259
Pages 204-11
Authors Kashiwagi M, Miyamoto K, Takei Y, Hirose S
Title Cloning, properties and tissue distribution of natriuretic peptide receptor-A of euryhaline eel, Anguilla japonica.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11078709
Journal Am J Physiol Cell Physiol
Year 2000
Volume 279
Pages C1938-45
Authors Nara M, Dhulipala PD, Ji GJ, Kamasani UR, Wang YX, Matalon S, Kotlikoff MI
Title Guanylyl cyclase stimulatory coupling to K(Ca) channels.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10971587
Journal Eur J Biochem
Year 2000
Volume 267
Pages 5758-68
Authors Miyagi M, Zhang X, Misono KS
Title Glycosylation sites in the atrial natriuretic peptide receptor: oligosaccharide structures are not required for hormone binding.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10648635
Journal Mol Pharmacol
Year 2000
Volume 57
Pages 259-67
Authors Pandey KN, Kumar R, Li M, Nguyen H
Title Functional domains and expression of truncated atrial natriuretic peptide receptor-A: the carboxyl-terminal regions direct the receptor internalization and sequestration in COS-7 cells.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10894551
Journal Nature
Year 2000
Volume 406
Pages 101-4
Authors van den Akker F, Zhang X, Miyagi M, Huo X, Misono KS, Yee VC
Title Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor.
Related PDB 1dp4
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11558678
Journal Can J Physiol Pharmacol
Year 2001
Volume 79
Pages 692-704
Authors van den Akker F
Title Detailed analysis of the atrial natriuretic factor receptor hormone-binding domain crystal structure.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 11306239
Journal Cell Signal
Year 2001
Volume 13
Pages 221-31
Authors Silberbach M, Roberts CT Jr
Title Natriuretic peptide signalling: molecular and cellular pathways to growth regulation.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11556325
Journal J Mol Biol
Year 2001
Volume 311
Pages 923-37
Authors van den Akker F
Title Structural insights into the ligand binding domains of membrane bound guanylyl cyclases and natriuretic peptide receptors.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11269661
Journal Mol Cell Biochem
Year 2001
Volume 217
Pages 165-72
Authors Duda T, Yadav P, Jankowska A, Venkataraman V, Sharma RK
Title Three dimensional atomic model and experimental validation for the ATP-Regulated Module (ARM) of the atrial natriuretic factor receptor guanylate cyclase.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11573084
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 832
Authors Hollien J
Title Picture story. A hormone receptor springs into action.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11533490
Journal Science
Year 2001
Volume 293
Pages 1657-62
Authors He Xl, Chow Dc, Martick MM, Garcia KC
Title Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11952096
Journal Mol Cell Biochem
Year 2002
Volume 230
Pages 49-60
Authors Misono KS
Title Natriuretic peptide receptor: structure and signaling.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11952097
Journal Mol Cell Biochem
Year 2002
Volume 230
Pages 61-72
Authors Pandey KN
Title Intracellular trafficking and metabolic turnover of ligand-bound guanylyl cyclase/atrial natriuretic peptide receptor-A into subcellular compartments.
Related PDB
Related UniProtKB

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.

Created Updated
2004-07-15 2009-02-26