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Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A (EC 3.1.4.35) (EC 3.1.4.53) (cAMP and cGMP phosphodiesterase 11A)

 PDE11_HUMAN             Reviewed;         933 AA.
Q9HCR9; Q14CD1; Q53T16; Q96S76; Q9GZY7; Q9HB46; Q9NY45;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
12-SEP-2018, entry version 131.
RecName: Full=Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A;
EC=3.1.4.35;
EC=3.1.4.53;
AltName: Full=cAMP and cGMP phosphodiesterase 11A;
Name=PDE11A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Prostate;
PubMed=10906126; DOI=10.1074/jbc.M003041200;
Yuasa K., Kotera J., Fujishige K., Michibata H., Sasaki T., Omori K.;
"Isolation and characterization of two novel phosphodiesterase PDE11A
variants showing unique structure and tissue-specific expression.";
J. Biol. Chem. 275:31469-31479(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=10725373; DOI=10.1073/pnas.97.7.3702;
Fawcett L., Baxendale R., Stacey P., McGrouther C., Harrow I.,
Soderling S., Hetman J., Beavo J.A., Phillips S.C.;
"Molecular cloning and characterization of a distinct human
phosphodiesterase gene family: PDE11A.";
Proc. Natl. Acad. Sci. U.S.A. 97:3702-3707(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
PubMed=11050148; DOI=10.1073/pnas.200355397;
Hetman J.M., Robas N.M., Baxendale R., Fidock M., Phillips S.C.,
Soderling S.H., Beavo J.A.;
"Cloning and characterisation of two splice variants of human
phosphodiesterase 11A.";
Proc. Natl. Acad. Sci. U.S.A. 97:12891-12895(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2
AND 4), AND TISSUE SPECIFICITY.
PubMed=11121118; DOI=10.1046/j.1432-1327.2001.01866.x;
Yuasa K., Kanoh Y., Okumura K., Omori K.;
"Genomic organization of the human phosphodiesterase PDE11A gene:
evolutionary relatedness with other PDEs containing GAF domains.";
Eur. J. Biochem. 268:168-178(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
TISSUE SPECIFICITY.
PubMed=15800651; DOI=10.1038/sj.ijir.3901317;
Loughney K., Taylor J., Florio V.A.;
"3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human
tissues.";
Int. J. Impot. Res. 17:320-325(2005).
[8]
ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
PubMed=16079899; DOI=10.1038/sj.ijir.3901377;
Francis S.H.;
"Phosphodiesterase 11 (PDE11): is it a player in human testicular
function?";
Int. J. Impot. Res. 17:467-468(2005).
[9]
DOMAIN, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-355.
PubMed=16330539; DOI=10.1074/jbc.M511468200;
Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E.;
"cAMP is a ligand for the tandem GAF domain of human phosphodiesterase
10 and cGMP for the tandem GAF domain of phosphodiesterase 11.";
J. Biol. Chem. 281:2841-2846(2006).
[10]
INVOLVEMENT IN PPNAD2, TISSUE SPECIFICITY, AND VARIANTS HIS-804 AND
GLY-867.
PubMed=16767104; DOI=10.1038/ng1809;
Horvath A., Boikos S., Giatzakis C., Robinson-White A., Groussin L.,
Griffin K.J., Stein E., Levine E., Delimpasi G., Hsiao H.P., Keil M.,
Heyerdahl S., Matyakhina L., Libe R., Fratticci A., Kirschner L.S.,
Cramer K., Gaillard R.C., Bertagna X., Carney J.A., Bertherat J.,
Bossis I., Stratakis C.A.;
"A genome-wide scan identifies mutations in the gene encoding
phosphodiesterase 11A4 (PDE11A) in individuals with adrenocortical
hyperplasia.";
Nat. Genet. 38:794-800(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
-!- FUNCTION: Plays a role in signal transduction by regulating the
intracellular concentration of cyclic nucleotides cAMP and cGMP.
Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-
GMP, respectively. {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148}.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- ACTIVITY REGULATION: Inhibited by 3-isobutyl-1-methylxanthine
(IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric
activator. Weakly inhibited by Sildenafil (Viagra) and Tadalafil
(Cialis); however, the fact that the protein is probably absent
from testis, suggests that it is not biologically relevant and is
not related with erectile dysfunction.
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:11050148,
ECO:0000269|PubMed:16079899, ECO:0000269|PubMed:16330539}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.0 uM for cAMP (isoform 1) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=1.4 uM for cGMP (isoform 1) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=3.0 uM for cAMP (isoform 2) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=1.5 uM for cGMP (isoform 2) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=3.3 uM for cAMP (isoform 3) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=3.7 uM for cGMP (isoform 3) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=1.04 uM for cAMP (isoform 4) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
KM=0.52 uM for cGMP (isoform 4) {ECO:0000269|PubMed:10725373,
ECO:0000269|PubMed:10906126, ECO:0000269|PubMed:11050148};
Vmax=3.6 pmol/min/ug enzyme with cAMP as substrate (isoform 4)
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:10906126,
ECO:0000269|PubMed:11050148};
Vmax=3.9 pmol/min/ug enzyme with cGMP as substrate (isoform 4)
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:10906126,
ECO:0000269|PubMed:11050148};
Vmax=270 pmol/min/ug enzyme with cAMP as substrate (isoform 1)
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:10906126,
ECO:0000269|PubMed:11050148};
Vmax=120 pmol/min/ug enzyme with cGMP as substrate (isoform 1)
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:10906126,
ECO:0000269|PubMed:11050148};
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10906126}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=PDE11A4;
IsoId=Q9HCR9-1; Sequence=Displayed;
Name=2; Synonyms=PDE11A3;
IsoId=Q9HCR9-2; Sequence=VSP_019900, VSP_019901;
Name=3; Synonyms=PDE11A2;
IsoId=Q9HCR9-3; Sequence=VSP_019899;
Name=4; Synonyms=PDE11A1;
IsoId=Q9HCR9-4; Sequence=VSP_019898;
-!- TISSUE SPECIFICITY: Isoform 1 is present in prostate, pituitary,
heart and liver. It is however not present in testis nor in penis,
suggesting that weak inhibition by Tadalafil (Cialis) is not
relevant (at protein level). Isoform 2 may be expressed in testis.
Isoform 4 is expressed in adrenal cortex.
{ECO:0000269|PubMed:10725373, ECO:0000269|PubMed:11121118,
ECO:0000269|PubMed:15800651, ECO:0000269|PubMed:16079899,
ECO:0000269|PubMed:16767104}.
-!- DOMAIN: The tandem GAF domains bind cGMP, and regulate enzyme
activity. The binding of cGMP stimulates enzyme activity.
{ECO:0000269|PubMed:16330539}.
-!- DISEASE: Primary pigmented nodular adrenocortical disease 2
(PPNAD2) [MIM:610475]: A rare bilateral adrenal defect causing
ACTH-independent Cushing syndrome. Macroscopic appearance of the
adrenals is characteristic with small pigmented micronodules
observed in the cortex. Adrenal glands show overall normal size
and weight, and multiple small yellow-to-dark brown nodules
surrounded by a cortex with a uniform appearance. Microscopically,
there are moderate diffuse cortical hyperplasia with mostly
nonpigmented nodules, multiple capsular deficits and massive
circumscribed and infiltrating extra-adrenal cortical excrescences
with micronodules. Clinical manifestations of Cushing syndrome
include facial and truncal obesity, abdominal striae, muscular
weakness, osteoporosis, arterial hypertension, diabetes.
{ECO:0000269|PubMed:16767104}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PDE11AID44448ch2q31.html";
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EMBL; AB036704; BAB16371.1; -; mRNA.
EMBL; AB038041; BAB16372.1; -; mRNA.
EMBL; AJ251509; CAB82573.1; -; mRNA.
EMBL; AF281865; AAG32023.1; -; mRNA.
EMBL; AJ278682; CAC15567.1; -; mRNA.
EMBL; AB048423; BAB62712.1; -; Genomic_DNA.
EMBL; AB048423; BAB62713.2; -; Genomic_DNA.
EMBL; AB048423; BAB62714.1; -; Genomic_DNA.
EMBL; AC073834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC083824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC012499; AAY14803.1; -; Genomic_DNA.
EMBL; BC112393; AAI12394.1; -; mRNA.
EMBL; BC114431; AAI14432.1; -; mRNA.
CCDS; CCDS33334.1; -. [Q9HCR9-1]
CCDS; CCDS42785.1; -. [Q9HCR9-2]
CCDS; CCDS42786.1; -. [Q9HCR9-4]
CCDS; CCDS46459.1; -. [Q9HCR9-3]
RefSeq; NP_001070664.1; NM_001077196.1. [Q9HCR9-4]
RefSeq; NP_001070665.1; NM_001077197.1. [Q9HCR9-2]
RefSeq; NP_001070826.1; NM_001077358.1. [Q9HCR9-3]
RefSeq; NP_058649.3; NM_016953.3. [Q9HCR9-1]
UniGene; Hs.570273; -.
ProteinModelPortal; Q9HCR9; -.
SMR; Q9HCR9; -.
STRING; 9606.ENSP00000286063; -.
BindingDB; Q9HCR9; -.
ChEMBL; CHEMBL2717; -.
DrugBank; DB00201; Caffeine.
DrugBank; DB00820; Tadalafil.
GuidetoPHARMACOLOGY; 1311; -.
iPTMnet; Q9HCR9; -.
PhosphoSitePlus; Q9HCR9; -.
BioMuta; PDE11A; -.
DMDM; 296439264; -.
EPD; Q9HCR9; -.
PaxDb; Q9HCR9; -.
PeptideAtlas; Q9HCR9; -.
PRIDE; Q9HCR9; -.
ProteomicsDB; 81789; -.
ProteomicsDB; 81790; -. [Q9HCR9-2]
ProteomicsDB; 81791; -. [Q9HCR9-3]
ProteomicsDB; 81792; -. [Q9HCR9-4]
Ensembl; ENST00000286063; ENSP00000286063; ENSG00000128655. [Q9HCR9-1]
Ensembl; ENST00000389683; ENSP00000374333; ENSG00000128655. [Q9HCR9-4]
Ensembl; ENST00000409504; ENSP00000386539; ENSG00000128655. [Q9HCR9-3]
GeneID; 50940; -.
KEGG; hsa:50940; -.
UCSC; uc002ulp.4; human. [Q9HCR9-1]
CTD; 50940; -.
DisGeNET; 50940; -.
EuPathDB; HostDB:ENSG00000128655.16; -.
GeneCards; ENSG00000284741; -.
GeneCards; PDE11A; -.
HGNC; HGNC:8773; PDE11A.
HPA; HPA034560; -.
MalaCards; PDE11A; -.
MIM; 604961; gene.
MIM; 610475; phenotype.
neXtProt; NX_Q9HCR9; -.
OpenTargets; ENSG00000128655; -.
Orphanet; 189439; Primary pigmented nodular adrenocortical disease.
PharmGKB; PA33121; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOVERGEN; HBG101207; -.
KO; K13298; -.
OMA; ATNRSKW; -.
OrthoDB; EOG091G04JU; -.
PhylomeDB; Q9HCR9; -.
TreeFam; TF316499; -.
BRENDA; 3.1.4.17; 2681.
Reactome; R-HSA-418457; cGMP effects.
Reactome; R-HSA-418555; G alpha (s) signalling events.
ChiTaRS; PDE11A; human.
GeneWiki; PDE11A; -.
GenomeRNAi; 50940; -.
PRO; PR:Q9HCR9; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000128655; Expressed in 118 organ(s), highest expression level in vastus lateralis.
CleanEx; HS_PDE11A; -.
ExpressionAtlas; Q9HCR9; baseline and differential.
Genevisible; Q9HCR9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA:UniProtKB.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 2.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
Allosteric enzyme; Alternative splicing; cAMP; cGMP;
Complete proteome; Cushing syndrome; Cytoplasm; Hydrolase;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat.
CHAIN 1 933 Dual 3',5'-cyclic-AMP and -GMP
phosphodiesterase 11A.
/FTId=PRO_0000247040.
DOMAIN 217 370 GAF 1.
DOMAIN 402 558 GAF 2.
DOMAIN 588 912 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
ACT_SITE 664 664 Proton donor. {ECO:0000250}.
METAL 668 668 Divalent metal cation 1.
{ECO:0000255|PROSITE-ProRule:PRU01192}.
METAL 704 704 Divalent metal cation 1.
{ECO:0000255|PROSITE-ProRule:PRU01192}.
METAL 705 705 Divalent metal cation 1.
{ECO:0000255|PROSITE-ProRule:PRU01192}.
METAL 705 705 Divalent metal cation 2.
{ECO:0000255|PROSITE-ProRule:PRU01192}.
METAL 816 816 Divalent metal cation 1.
{ECO:0000255|PROSITE-ProRule:PRU01192}.
BINDING 869 869 cAMP or cGMP. {ECO:0000250}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P0C1Q2}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000250|UniProtKB:P0C1Q2}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 444 Missing (in isoform 4).
{ECO:0000303|PubMed:10725373}.
/FTId=VSP_019898.
VAR_SEQ 1 358 Missing (in isoform 3).
{ECO:0000303|PubMed:11050148}.
/FTId=VSP_019899.
VAR_SEQ 1 250 Missing (in isoform 2).
{ECO:0000303|PubMed:10906126,
ECO:0000303|PubMed:11050148}.
/FTId=VSP_019900.
VAR_SEQ 251 304 KTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVG
EHGETVNIPDAYQ -> MLKQARRPLFRNVLSATQWKKVKI
TRLVQISGASLAEKQEKHQDFLIQRQTKTK (in
isoform 2). {ECO:0000303|PubMed:10906126,
ECO:0000303|PubMed:11050148}.
/FTId=VSP_019901.
VARIANT 804 804 R -> H (in dbSNP:rs75127279).
{ECO:0000269|PubMed:16767104}.
/FTId=VAR_027056.
VARIANT 867 867 R -> G (in dbSNP:rs61306957).
{ECO:0000269|PubMed:16767104}.
/FTId=VAR_027057.
MUTAGEN 355 355 D->A: Induces a decrease in enzyme
activity due to the inability of cGMP to
bind and stimulate enzyme activity.
{ECO:0000269|PubMed:16330539}.
CONFLICT 184 184 R -> Q (in Ref. 1; BAB16371, 4; BAB62712
and 6; AAI12394/AAI14432). {ECO:0000305}.
CONFLICT 921 921 S -> SS (in Ref. 1; BAB16371/BAB16372, 2;
CAB82573, 3; AAG32023/CAC15567, 4;
BAB62712/BAB62713/BAB62714 and 6;
AAI12394/AAI14432). {ECO:0000305}.
SEQUENCE 933 AA; 104752 MW; B725AE6963D6E799 CRC64;
MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQEMVEKWLQ RHSQGQGALG PRPSLAGTSS
LAHSTCRGGS SVGGGTGPNG SAHSQPLPGG GDCGGVPLSP SWAGGSRGDG NLQRRASQKE
LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS SVRRRALLRK ASSLPPTTAH ILSALLESRV
NLPRYPPTAI DYKCHLKKHN ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL
FLVEGAAAGK KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP
DAYQDRRFND EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP FTEDDEKVMQ
MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC
ERCSVLLLED IESPVVKFTK SFELMSPKCS ADAENSFKES MEKSSYSDWL INNSIAELVA
STGLPVNISD AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD
DADQRLFEAF VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI
PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM
VLYHNWRHAF NVCQLMFAML TTAGFQDILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSG
SALAQLYGTS ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY
FERRTEFFEL VSKGEYDWNI KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE
QGDRERLELK LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAT
NRSKWEELHQ KRLLASTASS SPASVMVAKE DRN


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