PDE8B_HUMAN
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 03-AUG-2022, entry version 198.
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}.
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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; 9.
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 UCD-2DPAGE; O95263; -.
DR EPD; O95263; -.
DR jPOST; O95263; -.
DR MassIVE; O95263; -.
DR MaxQB; O95263; -.
DR PaxDb; O95263; -.
DR PeptideAtlas; O95263; -.
DR PRIDE; 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 Antibodypedia; 12495; 159 antibodies from 25 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 CTD; 8622; -.
DR DisGeNET; 8622; -.
DR GeneCards; PDE8B; -.
DR HGNC; HGNC:8794; PDE8B.
DR HPA; ENSG00000113231; Tissue enhanced (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 Orphanet; 189439; Primary pigmented nodular adrenocortical disease.
DR PharmGKB; PA33142; -.
DR VEuPathDB; HostDB:ENSG00000113231; -.
DR eggNOG; KOG1229; Eukaryota.
DR GeneTree; ENSGT00940000157817; -.
DR HOGENOM; CLU_005940_4_2_1; -.
DR OMA; NIVQFLN; -.
DR OrthoDB; 904682at2759; -.
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 1075 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 102 other tissues.
DR ExpressionAtlas; O95263; baseline and differential.
DR Genevisible; O95263; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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: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; -; 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 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; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
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
