PDE1B_HUMAN
ID PDE1B_HUMAN Reviewed; 536 AA.
AC Q01064; Q92825; Q96KP3;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B {ECO:0000305|PubMed:9419816};
DE Short=Cam-PDE 1B;
DE EC=3.1.4.17 {ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:8855339, ECO:0000269|PubMed:9419816};
DE AltName: Full=63 kDa Cam-PDE {ECO:0000303|PubMed:1326532};
GN Name=PDE1B {ECO:0000312|HGNC:HGNC:8775}; Synonyms=PDES1B;
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 [MRNA] (ISOFORM PDE1B1), FUNCTION, CATALYTIC ACTIVITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=8855339; DOI=10.1073/pnas.93.20.11236;
RA Jiang X., Li J., Paskind M., Epstein P.M.;
RT "Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in
RT human leukemic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11236-11241(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1B1), FUNCTION, CATALYTIC ACTIVITY,
RP AND ACTIVITY REGULATION.
RC TISSUE=Brain;
RX PubMed=9419816; DOI=10.1016/s0898-6568(97)00046-6;
RA Yu J., Frazier A.L.B., Wolda S.L., Florio V.A., Martins T.J., Snyder P.B.,
RA Harris E.A.S., McCaw K.N., Farrell C.A., Steiner B., Bentley J.K.,
RA Beavo J.A., Ferguson K., Gelinas R.;
RT "Identification and characterisation of a human calmodulin-stimulated
RT phosphodiesterase PDE1B1.";
RL Cell. Signal. 9:519-529(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1B2).
RC TISSUE=Testis;
RX PubMed=11747989; DOI=10.1016/s0898-6568(01)00207-8;
RA Fidock M.D., Miller M., Lanfear J.;
RT "Isolation and differential tissue distribution of two human cDNAs encoding
RT PDE1 splice variants.";
RL Cell. Signal. 14:53-60(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE1B2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE1B1).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-337.
RX PubMed=1326532; DOI=10.1016/s0021-9258(19)37015-2;
RA Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
RT "A polymerase chain reaction strategy to identify and clone cyclic
RT nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding
RT the 63-kDa calmodulin-dependent phosphodiesterase.";
RL J. Biol. Chem. 267:18683-18688(1992).
RN [8] {ECO:0007744|PDB:1TAZ}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 146-506 IN COMPLEX WITH METAL
RP IONS, COFACTOR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15260978; DOI=10.1016/j.molcel.2004.07.005;
RA Zhang K.Y.J., Card G.L., Suzuki Y., Artis D.R., Fong D., Gillette S.,
RA Hsieh D., Neiman J., West B.L., Zhang C., Milburn M.V., Kim S.-H.,
RA Schlessinger J., Bollag G.;
RT "A glutamine switch mechanism for nucleotide selectivity by
RT phosphodiesterases.";
RL Mol. Cell 15:279-286(2004).
CC -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual specificity
CC for the second messengers cAMP and cGMP, which are key regulators of
CC many important physiological processes (PubMed:8855339, PubMed:9419816,
CC PubMed:15260978). Has a preference for cGMP as a substrate
CC (PubMed:9419816). {ECO:0000269|PubMed:15260978,
CC ECO:0000269|PubMed:8855339, ECO:0000269|PubMed:9419816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC Evidence={ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:8855339,
CC ECO:0000269|PubMed:9419816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC Evidence={ECO:0000305|PubMed:15260978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:15260978,
CC ECO:0000269|PubMed:9419816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:15260978};
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; Evidence={ECO:0000269|PubMed:15260978,
CC ECO:0000269|PubMed:8855339, ECO:0000269|PubMed:9419816};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:15260978};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15260978};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000269|PubMed:15260978};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15260978};
CC Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC preference for magnesium ions. {ECO:0000269|PubMed:15260978};
CC -!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
CC calmodulin in the presence of Ca(2+). {ECO:0000269|PubMed:9419816}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC -!- INTERACTION:
CC Q01064; Q9NUX5: POT1; NbExp=2; IntAct=EBI-7413304, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8855339}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=PDE1B1 {ECO:0000303|PubMed:8855339};
CC IsoId=Q01064-1; Sequence=Displayed;
CC Name=PDE1B2 {ECO:0000303|PubMed:11747989};
CC IsoId=Q01064-2; Sequence=VSP_038643, VSP_038644;
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE1 subfamily. {ECO:0000305}.
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DR EMBL; U56976; AAC50769.1; -; mRNA.
DR EMBL; U86078; AAC51872.1; -; mRNA.
DR EMBL; AJ401609; CAC82207.1; -; mRNA.
DR EMBL; AK302931; BAG64092.1; -; mRNA.
DR EMBL; CH471054; EAW96790.1; -; Genomic_DNA.
DR EMBL; BC032226; AAH32226.1; -; mRNA.
DR EMBL; M94539; AAA58405.1; -; mRNA.
DR CCDS; CCDS53800.1; -. [Q01064-2]
DR CCDS; CCDS8882.1; -. [Q01064-1]
DR PIR; JC6129; JC6129.
DR RefSeq; NP_000915.1; NM_000924.3. [Q01064-1]
DR RefSeq; NP_001159447.1; NM_001165975.2. [Q01064-2]
DR RefSeq; NP_001275697.1; NM_001288768.1.
DR RefSeq; NP_001275698.1; NM_001288769.1.
DR RefSeq; NP_001302463.1; NM_001315534.1.
DR RefSeq; NP_001302464.1; NM_001315535.1.
DR PDB; 1TAZ; X-ray; 1.77 A; A=146-506.
DR PDB; 4NPV; X-ray; 2.40 A; A=142-507.
DR PDB; 4NPW; X-ray; 1.90 A; A=142-507.
DR PDB; 5B25; X-ray; 1.90 A; A/B/C/D=146-506.
DR PDB; 5UOY; X-ray; 1.82 A; A=146-506.
DR PDB; 5UP0; X-ray; 2.04 A; A=146-506.
DR PDB; 5W6E; X-ray; 1.90 A; A=142-507.
DR PDBsum; 1TAZ; -.
DR PDBsum; 4NPV; -.
DR PDBsum; 4NPW; -.
DR PDBsum; 5B25; -.
DR PDBsum; 5UOY; -.
DR PDBsum; 5UP0; -.
DR PDBsum; 5W6E; -.
DR AlphaFoldDB; Q01064; -.
DR SMR; Q01064; -.
DR BioGRID; 111179; 4.
DR IntAct; Q01064; 3.
DR MINT; Q01064; -.
DR STRING; 9606.ENSP00000243052; -.
DR BindingDB; Q01064; -.
DR ChEMBL; CHEMBL4425; -.
DR DrugBank; DB01244; Bepridil.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB01023; Felodipine.
DR DrugBank; DB00622; Nicardipine.
DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; Q01064; -.
DR GuidetoPHARMACOLOGY; 1295; -.
DR iPTMnet; Q01064; -.
DR PhosphoSitePlus; Q01064; -.
DR BioMuta; PDE1B; -.
DR DMDM; 3183514; -.
DR jPOST; Q01064; -.
DR MassIVE; Q01064; -.
DR MaxQB; Q01064; -.
DR PaxDb; Q01064; -.
DR PeptideAtlas; Q01064; -.
DR PRIDE; Q01064; -.
DR ProteomicsDB; 57904; -. [Q01064-1]
DR ProteomicsDB; 57905; -. [Q01064-2]
DR Antibodypedia; 15408; 394 antibodies from 31 providers.
DR DNASU; 5153; -.
DR Ensembl; ENST00000243052.8; ENSP00000243052.3; ENSG00000123360.12. [Q01064-1]
DR Ensembl; ENST00000550620.1; ENSP00000448519.1; ENSG00000123360.12. [Q01064-2]
DR GeneID; 5153; -.
DR KEGG; hsa:5153; -.
DR MANE-Select; ENST00000243052.8; ENSP00000243052.3; NM_000924.4; NP_000915.1.
DR UCSC; uc001sgd.3; human. [Q01064-1]
DR CTD; 5153; -.
DR DisGeNET; 5153; -.
DR GeneCards; PDE1B; -.
DR HGNC; HGNC:8775; PDE1B.
DR HPA; ENSG00000123360; Tissue enriched (brain).
DR MIM; 171891; gene.
DR neXtProt; NX_Q01064; -.
DR OpenTargets; ENSG00000123360; -.
DR PharmGKB; PA33123; -.
DR VEuPathDB; HostDB:ENSG00000123360; -.
DR eggNOG; KOG3688; Eukaryota.
DR GeneTree; ENSGT00940000160712; -.
DR HOGENOM; CLU_005940_1_0_1; -.
DR OMA; HCADIAH; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q01064; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.17; 2681.
DR PathwayCommons; Q01064; -.
DR Reactome; R-HSA-111957; Cam-PDE 1 activation.
DR Reactome; R-HSA-418457; cGMP effects.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SignaLink; Q01064; -.
DR SIGNOR; Q01064; -.
DR BioGRID-ORCS; 5153; 15 hits in 1074 CRISPR screens.
DR EvolutionaryTrace; Q01064; -.
DR GeneWiki; PDE1B; -.
DR GenomeRNAi; 5153; -.
DR Pharos; Q01064; Tclin.
DR PRO; PR:Q01064; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q01064; protein.
DR Bgee; ENSG00000123360; Expressed in caudate nucleus and 104 other tissues.
DR ExpressionAtlas; Q01064; baseline and differential.
DR Genevisible; Q01064; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IDA:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0042428; P:serotonin metabolic process; 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 Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR InterPro; IPR013706; PDEase_N.
DR Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calmodulin-binding; cAMP; cGMP;
KW Cytoplasm; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..536
FT /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT cyclic nucleotide phosphodiesterase 1B"
FT /id="PRO_0000198789"
FT DOMAIN 146..503
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..47
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P14100"
FT REGION 118..141
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P14100"
FT REGION 447..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15260978,
FT ECO:0007744|PDB:1TAZ, ECO:0007744|PDB:4NPV,
FT ECO:0007744|PDB:4NPW"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15260978,
FT ECO:0007744|PDB:1TAZ, ECO:0007744|PDB:4NPV,
FT ECO:0007744|PDB:4NPW"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15260978,
FT ECO:0007744|PDB:1TAZ"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15260978,
FT ECO:0007744|PDB:1TAZ, ECO:0007744|PDB:4NPV,
FT ECO:0007744|PDB:4NPW"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15260978,
FT ECO:0007744|PDB:1TAZ, ECO:0007744|PDB:4NPV,
FT ECO:0007744|PDB:4NPW"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01065"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01065"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01065"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01065"
FT VAR_SEQ 1..18
FT /note="MELSPRSPPEMLEESDCP -> MANPVPVQRSHLQGPILR (in isoform
FT PDE1B2)"
FT /evidence="ECO:0000303|PubMed:11747989,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_038643"
FT VAR_SEQ 19..38
FT /note="Missing (in isoform PDE1B2)"
FT /evidence="ECO:0000303|PubMed:11747989,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_038644"
FT CONFLICT 225..226
FT /note="QI -> SM (in Ref. 2; AAA58405)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="S -> A (in Ref. 2; AAA58405)"
FT /evidence="ECO:0000305"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:1TAZ"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:1TAZ"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1TAZ"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 225..242
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:1TAZ"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1TAZ"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 378..402
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:1TAZ"
FT HELIX 429..444
FT /evidence="ECO:0007829|PDB:1TAZ"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:5B25"
FT HELIX 476..501
FT /evidence="ECO:0007829|PDB:1TAZ"
SQ SEQUENCE 536 AA; 61380 MW; D15211AC32C756A4 CRC64;
MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE INIEELKKNL
EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW LASTFTQQAR AKGRRAEEKP
KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY STAVLNCLKN LDLWCFDVFS LNQAADDHAL
RTIVFELLTR HNLISRFKIP TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL
RTGMVHCLSE IELLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAIVYNDRS VLENHHISSV
FRLMQDDEMN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL QQLERIDKPK
ALSLLLHAAD ISHPTKQWLV HSRWTKALME EFFRQGDKEA ELGLPFSPLC DRTSTLVAQS
QIGFIDFIVE PTFSVLTDVA EKSVQPLADE DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS
FRSTWVKRIQ ENKQKWKERA ASGITNQMSI DELSPCEEEA PPSPAEDEHN QNGNLD
