ID PDE8B_HUMAN Reviewed; 885 AA. AC O95263; Q5J7V7; Q86XK8; Q8IUJ7; Q8IUJ8; Q8IUJ9; Q8IUK0; Q8N3T2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B; DE Short=HsPDE8B; DE EC=3.1.4.53 {ECO:0000269|PubMed:12681444}; DE AltName: Full=Cell proliferation-inducing gene 22 protein; GN Name=PDE8B; ORFNames=PIG22; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 6), AND TISSUE RP SPECIFICITY. RX PubMed=12372422; DOI=10.1016/s0006-291x(02)02371-9; RA Hayashi M., Shimada Y., Nishimura Y., Hama T., Tanaka T.; RT "Genomic organization, chromosomal localization, and alternative splicing RT of the human phosphodiesterase 8B gene."; RL Biochem. Biophys. Res. Commun. 297:1253-1258(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), CATALYTIC ACTIVITY, RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RC TISSUE=Thyroid; RX PubMed=12681444; DOI=10.1016/s0898-6568(02)00146-8; RA Gamanuma M., Yuasa K., Sasaki T., Sakurai N., Kotera J., Omori K.; RT "Comparison of enzymatic characterization and gene organization of cyclic RT nucleotide phosphodiesterase 8 family in humans."; RL Cell. Signal. 15:565-574(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RA Kim J.W.; RT "Identification of a human proliferation-inducing gene."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 227-885 (ISOFORM 1). RX PubMed=9784418; DOI=10.1006/bbrc.1998.9379; RA Hayashi M., Matsushima K., Ohashi H., Tsunoda H., Murase S., Kawarada Y., RA Tanaka T.; RT "Molecular cloning and characterization of human PDE8B, a novel thyroid- RT specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase."; RL Biochem. Biophys. Res. Commun. 250:751-756(1998). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-885 (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP INVOLVEMENT IN ADSD1. RX PubMed=20085714; DOI=10.1016/j.ajhg.2009.12.003; RA Appenzeller S., Schirmacher A., Halfter H., Baumer S., Pendziwiat M., RA Timmerman V., De Jonghe P., Fekete K., Stogbauer F., Ludemann P., Hund M., RA Quabius E.S., Ringelstein E.B., Kuhlenbaumer G.; RT "Autosomal-dominant striatal degeneration is caused by a mutation in the RT phosphodiesterase 8B gene."; RL Am. J. Hum. Genet. 86:83-87(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP VARIANT PPNAD3 PRO-305, AND CHARACTERIZATION OF VARIANT PPNAD3 PRO-305. RX PubMed=18431404; DOI=10.1038/ejhg.2008.85; RA Horvath A., Giatzakis C., Tsang K., Greene E., Osorio P., Boikos S., RA Libe R., Patronas Y., Robinson-White A., Remmers E., Bertherat J., RA Nesterova M., Stratakis C.A.; RT "A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal RT hyperplasia is expressed widely in human and mouse tissues: a novel PDE8B RT isoform in human adrenal cortex."; RL Eur. J. Hum. Genet. 16:1245-1253(2008). CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key CC regulator of many important physiological processes. May be involved in CC specific signaling in the thyroid gland. CC -!- CATALYTIC ACTIVITY: CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, CC ChEBI:CHEBI:456215; EC=3.1.4.53; CC Evidence={ECO:0000269|PubMed:12681444}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Site 1 may CC preferentially bind zinc ions, while site 2 has a preference for CC magnesium and/or manganese ions. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by dipyridimole. Insensitive to CC selective PDE inhibitors including rolipram and milrinone as well as to CC the non-selective inhibitor, IBMX. Unaffected by cGMP. CC {ECO:0000269|PubMed:12681444}. CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from CC 3',5'-cyclic AMP: step 1/1. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=PDE8B1; CC IsoId=O95263-1; Sequence=Displayed; CC Name=2; Synonyms=PDE8B2, PDE8B3; CC IsoId=O95263-2; Sequence=VSP_008084; CC Name=3; Synonyms=PDE8B3; CC IsoId=O95263-3; Sequence=VSP_008085; CC Name=4; Synonyms=PDE8B4; CC IsoId=O95263-4; Sequence=VSP_008082; CC Name=5; CC IsoId=O95263-5; Sequence=VSP_008081; CC Name=6; Synonyms=PDE8B2; CC IsoId=O95263-6; Sequence=VSP_008083; CC -!- TISSUE SPECIFICITY: Abundantly expressed in the thyroid. Also very CC weakly expressed in brain, spinal cord and placenta. In the thyroid CC isoform 1 predominates, and isoforms 2 and 6 are also highly expressed. CC In the placenta isoforms 1 and 2 are expressed equally. In the brain CC isoform 2 predominates. {ECO:0000269|PubMed:12372422, CC ECO:0000269|PubMed:12681444}. CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two CC putative divalent metal sites and an N-terminal regulatory domain. CC -!- DISEASE: Striatal degeneration, autosomal dominant 1 (ADSD1) CC [MIM:609161]: A movement disorder affecting the striatal part of the CC basal ganglia and characterized by bradykinesia, dysarthria and muscle CC rigidity. These symptoms resemble idiopathic Parkinson disease, but CC tremor is not present. {ECO:0000269|PubMed:20085714}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Primary pigmented nodular adrenocortical disease 3 (PPNAD3) CC [MIM:614190]: A rare bilateral adrenal defect causing ACTH-independent CC Cushing syndrome. Macroscopic appearance of the adrenals is CC characteristic with small pigmented micronodules observed in the CC cortex. Adrenal glands show overall normal size and weight, and CC multiple small yellow-to-dark brown nodules surrounded by a cortex with CC a uniform appearance. Microscopically, there are moderate diffuse CC cortical hyperplasia with mostly nonpigmented nodules, multiple CC capsular deficits and massive circumscribed and infiltrating extra- CC adrenal cortical excrescences with micronodules. Clinical CC manifestations of Cushing syndrome include facial and truncal obesity, CC abdominal striae, muscular weakness, osteoporosis, arterial CC hypertension, diabetes. {ECO:0000269|PubMed:18431404}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC PDE8 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY129948; AAN71723.1; -; mRNA. DR EMBL; AY129949; AAN71724.1; -; mRNA. DR EMBL; AY129950; AAN71725.1; -; Genomic_DNA. DR EMBL; AY129950; AAN71726.1; -; Genomic_DNA. DR EMBL; AY129950; AAN71727.1; -; Genomic_DNA. DR EMBL; AB085824; BAC53762.1; -; mRNA. DR EMBL; AB085825; BAC53763.1; -; mRNA. DR EMBL; AB085826; BAC53764.1; -; mRNA. DR EMBL; AB085827; BAC53765.1; -; mRNA. DR EMBL; AY423729; AAS00492.1; -; mRNA. DR EMBL; CH471084; EAW95803.1; -; Genomic_DNA. DR EMBL; BC043209; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF079529; AAC69564.2; -; mRNA. DR EMBL; AL831924; CAD38584.1; -; mRNA. DR CCDS; CCDS34190.1; -. [O95263-3] DR CCDS; CCDS34191.1; -. [O95263-6] DR CCDS; CCDS34192.1; -. [O95263-2] DR CCDS; CCDS34193.1; -. [O95263-4] DR CCDS; CCDS4037.1; -. [O95263-1] DR PIR; JE0293; JE0293. DR RefSeq; NP_001025022.1; NM_001029851.2. [O95263-2] DR RefSeq; NP_001025023.1; NM_001029852.2. [O95263-3] DR RefSeq; NP_001025024.1; NM_001029853.2. [O95263-4] DR RefSeq; NP_001025025.1; NM_001029854.2. [O95263-6] DR RefSeq; NP_003710.1; NM_003719.3. [O95263-1] DR AlphaFoldDB; O95263; -. DR SMR; O95263; -. DR BioGRID; 114177; 11. DR IntAct; O95263; 3. DR MINT; O95263; -. DR STRING; 9606.ENSP00000264917; -. DR BindingDB; O95263; -. DR ChEMBL; CHEMBL4408; -. DR DrugBank; DB00201; Caffeine. DR DrugBank; DB09283; Trapidil. DR DrugCentral; O95263; -. DR GuidetoPHARMACOLOGY; 1308; -. DR iPTMnet; O95263; -. DR PhosphoSitePlus; O95263; -. DR BioMuta; PDE8B; -. DR EPD; O95263; -. DR jPOST; O95263; -. DR MassIVE; O95263; -. DR MaxQB; O95263; -. DR PaxDb; 9606-ENSP00000264917; -. DR PeptideAtlas; O95263; -. DR ProteomicsDB; 50759; -. [O95263-1] DR ProteomicsDB; 50760; -. [O95263-2] DR ProteomicsDB; 50761; -. [O95263-3] DR ProteomicsDB; 50762; -. [O95263-4] DR ProteomicsDB; 50763; -. [O95263-5] DR ProteomicsDB; 50764; -. [O95263-6] DR Pumba; O95263; -. DR Antibodypedia; 12495; 164 antibodies from 26 providers. DR DNASU; 8622; -. DR Ensembl; ENST00000264917.10; ENSP00000264917.6; ENSG00000113231.14. [O95263-1] DR Ensembl; ENST00000333194.8; ENSP00000331336.4; ENSG00000113231.14. [O95263-3] DR Ensembl; ENST00000340978.7; ENSP00000345446.3; ENSG00000113231.14. [O95263-6] DR Ensembl; ENST00000342343.8; ENSP00000345646.4; ENSG00000113231.14. [O95263-4] DR Ensembl; ENST00000346042.7; ENSP00000330428.3; ENSG00000113231.14. [O95263-2] DR Ensembl; ENST00000505283.1; ENSP00000423461.1; ENSG00000113231.14. [O95263-5] DR GeneID; 8622; -. DR KEGG; hsa:8622; -. DR MANE-Select; ENST00000264917.10; ENSP00000264917.6; NM_003719.5; NP_003710.1. DR UCSC; uc003kfa.4; human. [O95263-1] DR AGR; HGNC:8794; -. DR CTD; 8622; -. DR DisGeNET; 8622; -. DR GeneCards; PDE8B; -. DR HGNC; HGNC:8794; PDE8B. DR HPA; ENSG00000113231; Tissue enriched (thyroid). DR MalaCards; PDE8B; -. DR MIM; 603390; gene. DR MIM; 609161; phenotype. DR MIM; 614190; phenotype. DR neXtProt; NX_O95263; -. DR OpenTargets; ENSG00000113231; -. DR Orphanet; 228169; Autosomal dominant striatal neurodegeneration. DR PharmGKB; PA33142; -. DR VEuPathDB; HostDB:ENSG00000113231; -. DR eggNOG; KOG1229; Eukaryota. DR GeneTree; ENSGT00940000157817; -. DR HOGENOM; CLU_005940_4_2_1; -. DR InParanoid; O95263; -. DR OMA; RWCCGGS; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; O95263; -. DR TreeFam; TF314638; -. DR BRENDA; 3.1.4.53; 2681. DR PathwayCommons; O95263; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR SignaLink; O95263; -. DR UniPathway; UPA00762; UER00747. DR BioGRID-ORCS; 8622; 19 hits in 1161 CRISPR screens. DR ChiTaRS; PDE8B; human. DR GeneWiki; PDE8B; -. DR GenomeRNAi; 8622; -. DR Pharos; O95263; Tclin. DR PRO; PR:O95263; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O95263; Protein. DR Bgee; ENSG00000113231; Expressed in left lobe of thyroid gland and 104 other cell types or tissues. DR ExpressionAtlas; O95263; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001662; P:behavioral fear response; IEA:Ensembl. DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0090032; P:negative regulation of steroid hormone biosynthetic process; IEA:Ensembl. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0035106; P:operant conditioning; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0008542; P:visual learning; IEA:Ensembl. DR CDD; cd00077; HDc; 1. DR CDD; cd00130; PAS; 1. DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR000014; PAS. DR InterPro; IPR035965; PAS-like_dom_sf. DR InterPro; IPR023088; PDEase. DR InterPro; IPR002073; PDEase_catalytic_dom. DR InterPro; IPR036971; PDEase_catalytic_dom_sf. DR InterPro; IPR023174; PDEase_CS. DR InterPro; IPR013938; PDEase_PDE8. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1. DR PANTHER; PTHR11347:SF98; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8B; 1. DR Pfam; PF13426; PAS_9; 1. DR Pfam; PF08629; PDE8; 1. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00471; HDc; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1. DR PROSITE; PS50112; PAS; 1. DR PROSITE; PS00126; PDEASE_I_1; 1. DR PROSITE; PS51845; PDEASE_I_2; 1. DR UCD-2DPAGE; O95263; -. DR Genevisible; O95263; HS. PE 1: Evidence at protein level; KW Alternative splicing; cAMP; Cushing syndrome; Disease variant; Hydrolase; KW Metal-binding; Phosphoprotein; Reference proteome. FT CHAIN 1..885 FT /note="High affinity cAMP-specific and IBMX-insensitive FT 3',5'-cyclic phosphodiesterase 8B" FT /id="PRO_0000198840" FT DOMAIN 267..338 FT /note="PAS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140" FT DOMAIN 539..875 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 18..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 72..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 393..436 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..422 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 615 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O76083" FT BINDING 619 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O60658" FT BINDING 655 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O60658" FT BINDING 656 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O60658" FT BINDING 656 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:O60658" FT BINDING 781 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:O60658" FT MOD_RES 517 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 754 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q4S1" FT VAR_SEQ 1..535 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_008081" FT VAR_SEQ 114..133 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12681444" FT /id="VSP_008082" FT VAR_SEQ 293..389 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12372422, FT ECO:0000303|PubMed:12681444" FT /id="VSP_008084" FT VAR_SEQ 293..339 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12372422" FT /id="VSP_008083" FT VAR_SEQ 456..510 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12681444" FT /id="VSP_008085" FT VARIANT 305 FT /note="H -> P (in PPNAD3; shows significantly higher cyclic FT AMP levels after transfection with the mutant protein than FT after transfection with the wild-type, indicating an FT impaired ability of the mutant protein to degrade cAMP; FT dbSNP:rs121918360)" FT /evidence="ECO:0000269|PubMed:18431404" FT /id="VAR_066503" FT CONFLICT 147 FT /note="G -> R (in Ref. 7; CAD38584)" FT /evidence="ECO:0000305" SQ SEQUENCE 885 AA; 98979 MW; DB4F763E51F745A3 CRC64; MGCAPSIHVS QSGVIYCRDS DESSSPRQTT SVSQGPAAPL PGLFVQTDAA DAIPPSRASG PPSVARVRRA RTELGSGSSA GSAAPAATTS RGRRRHCCSS AEAETQTCYT SVKQVSSAEV RIGPMRLTQD PIQVLLIFAK EDSQSDGFWW ACDRAGYRCN IARTPESALE CFLDKHHEII VIDHRQTQNF DAEAVCRSIR ATNPSEHTVI LAVVSRVSDD HEEASVLPLL HAGFNRRFME NSSIIACYNE LIQIEHGEVR SQFKLRACNS VFTALDHCHE AIEITSDDHV IQYVNPAFER MMGYHKGELL GKELADLPKS DKNRADLLDT INTCIKKGKE WQGVYYARRK SGDSIQQHVK ITPVIGQGGK IRHFVSLKKL CCTTDNNKQI HKIHRDSGDN SQTEPHSFRY KNRRKESIDV KSISSRGSDA PSLQNRRYPS MARIHSMTIE APITKVINII NAAQENSPVT VAEALDRVLE ILRTTELYSP QLGTKDEDPH TSDLVGGLMT DGLRRLSGNE YVFTKNVHQS HSHLAMPITI NDVPPCISQL LDNEESWDFN IFELEAITHK RPLVYLGLKV FSRFGVCEFL NCSETTLRAW FQVIEANYHS SNAYHNSTHA ADVLHATAFF LGKERVKGSL DQLDEVAALI AATVHDVDHP GRTNSFLCNA GSELAVLYND TAVLESHHTA LAFQLTVKDT KCNIFKNIDR NHYRTLRQAI IDMVLATEMT KHFEHVNKFV NSINKPMAAE IEGSDCECNP AGKNFPENQI LIKRMMIKCA DVANPCRPLD LCIEWAGRIS EEYFAQTDEE KRQGLPVVMP VFDRNTCSIP KSQISFIDYF ITDMFDAWDA FAHLPALMQH LADNYKHWKT LDDLKCKSLR LPSDS //