PDE1C_HUMAN
ID PDE1C_HUMAN Reviewed; 709 AA.
AC Q14123; B3KPC6; E9PE92; Q14124; Q8NB10;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C {ECO:0000305|PubMed:8557689};
DE Short=Cam-PDE 1C;
DE EC=3.1.4.17 {ECO:0000269|PubMed:29860631, ECO:0000269|PubMed:8557689};
DE AltName: Full=Hcam3 {ECO:0000303|PubMed:8557689};
GN Name=PDE1C {ECO:0000312|HGNC:HGNC:8776};
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] (ISOFORMS PDE1C1 AND PDE1C2), FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=8557689; DOI=10.1074/jbc.271.2.796;
RA Loughney K., Martins T.J., Harris E.A.S., Sadhu K., Hicks J.B.,
RA Sonnenburg W.K., Beavo J.A., Ferguson K.;
RT "Isolation and characterization of cDNAs corresponding to two human
RT calcium, calmodulin-regulated, 3',5'-cyclic nucleotide
RT phosphodiesterases.";
RL J. Biol. Chem. 271:796-806(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PDE1C2 AND 3).
RC TISSUE=Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [5]
RP INVOLVEMENT IN DFNA74, VARIANT DFNA74 SER-260, CHARACTERIZATION OF VARIANT
RP DFNA74 SER-260, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=29860631; DOI=10.1007/s00439-018-1895-y;
RA Wang L., Feng Y., Yan D., Qin L., Grati M., Mittal R., Li T.,
RA Sundhari A.K., Liu Y., Chapagain P., Blanton S.H., Liao S., Liu X.;
RT "A dominant variant in the PDE1C gene is associated with nonsyndromic
RT hearing loss.";
RL Hum. Genet. 137:437-446(2018).
CC -!- FUNCTION: Calmodulin-dependent cyclic nucleotide phosphodiesterase with
CC a dual specificity for the second messengers cAMP and cGMP, which are
CC key regulators of many important physiological processes
CC (PubMed:8557689, PubMed:29860631). Has a high affinity for both cAMP
CC and cGMP (PubMed:8557689). Modulates the amplitude and duration of the
CC cAMP signal in sensory cilia in response to odorant stimulation, hence
CC contributing to the generation of action potentials. Regulates smooth
CC muscle cell proliferation. Regulates the stability of growth factor
CC receptors, including PDGFRB (Probable). {ECO:0000269|PubMed:29860631,
CC ECO:0000269|PubMed:8557689, ECO:0000305|PubMed:29860631}.
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:29860631, ECO:0000269|PubMed:8557689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC Evidence={ECO:0000305|PubMed:8557689};
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:29860631,
CC ECO:0000269|PubMed:8557689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:8557689};
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:29860631,
CC ECO:0000269|PubMed:8557689};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:8557689};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q01064};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q01064};
CC Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC preference for magnesium ions. {ECO:0000250|UniProtKB:Q01064};
CC -!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
CC calmodulin in the presence of Ca(2+). {ECO:0000250|UniProtKB:Q64338}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform PDE1C2]:
CC Kinetic parameters:
CC KM=0.3 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:8557689};
CC KM=0.6 uM for 3',5'-cyclic GMP {ECO:0000269|PubMed:8557689};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q64338}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=PDE1C2; Synonyms=Hcam3a {ECO:0000303|PubMed:8557689}, PDE1C3
CC {ECO:0000303|PubMed:8557689}, HSPDE1C3A {ECO:0000303|PubMed:8557689},
CC HSPDE1C3 {ECO:0000303|PubMed:8557689};
CC IsoId=Q14123-1; Sequence=Displayed;
CC Name=PDE1C1 {ECO:0000303|PubMed:8557689}; Synonyms=Hcam3b
CC {ECO:0000303|PubMed:8557689}, HSPDE1C1A {ECO:0000303|PubMed:8557689};
CC IsoId=Q14123-2; Sequence=VSP_004552, VSP_004553;
CC Name=3;
CC IsoId=Q14123-3; Sequence=VSP_044468;
CC -!- TISSUE SPECIFICITY: Isoform PDE1C2 is present in the heart and brain
CC and, at lower levels in the lung, liver, kidney and skeletal muscle
CC (PubMed:8557689). Isoform PDE1C1 is expressed in the heart and brain
CC and, at lower levels in lung (PubMed:8557689). Also expressed at low
CC levels in uterus and testis (PubMed:8557689).
CC {ECO:0000269|PubMed:8557689}.
CC -!- DISEASE: Deafness, autosomal dominant, 74 (DFNA74) [MIM:618140]: A form
CC of non-syndromic deafness characterized by progressive, postlingual
CC hearing loss with onset in the third decade of life.
CC {ECO:0000269|PubMed:29860631}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE1 subfamily. {ECO:0000305}.
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DR EMBL; U40371; AAC50437.1; -; mRNA.
DR EMBL; U40372; AAA96961.1; -; mRNA.
DR EMBL; AK056170; BAG51638.1; -; mRNA.
DR EMBL; AK091734; BAC03734.1; -; mRNA.
DR EMBL; AC004931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS5437.1; -. [Q14123-2]
DR CCDS; CCDS55099.1; -. [Q14123-1]
DR CCDS; CCDS55100.1; -. [Q14123-3]
DR RefSeq; NP_001177985.1; NM_001191056.3. [Q14123-2]
DR RefSeq; NP_001177986.1; NM_001191057.3. [Q14123-1]
DR RefSeq; NP_001177987.2; NM_001191058.3.
DR RefSeq; NP_001177988.1; NM_001191059.3. [Q14123-1]
DR RefSeq; NP_001308984.1; NM_001322055.1. [Q14123-1]
DR RefSeq; NP_001308985.1; NM_001322056.1. [Q14123-2]
DR RefSeq; NP_001308986.1; NM_001322057.1. [Q14123-2]
DR RefSeq; NP_001308987.1; NM_001322058.1.
DR RefSeq; NP_001308988.1; NM_001322059.1.
DR RefSeq; NP_005011.1; NM_005020.4. [Q14123-2]
DR RefSeq; XP_016867756.1; XM_017012267.1. [Q14123-1]
DR AlphaFoldDB; Q14123; -.
DR SMR; Q14123; -.
DR BioGRID; 111163; 49.
DR IntAct; Q14123; 3.
DR STRING; 9606.ENSP00000379496; -.
DR BindingDB; Q14123; -.
DR ChEMBL; CHEMBL4619; -.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; Q14123; -.
DR GuidetoPHARMACOLOGY; 1296; -.
DR iPTMnet; Q14123; -.
DR PhosphoSitePlus; Q14123; -.
DR BioMuta; PDE1C; -.
DR DMDM; 2499445; -.
DR jPOST; Q14123; -.
DR MassIVE; Q14123; -.
DR MaxQB; Q14123; -.
DR PaxDb; Q14123; -.
DR PeptideAtlas; Q14123; -.
DR PRIDE; Q14123; -.
DR ProteomicsDB; 19840; -.
DR ProteomicsDB; 59827; -. [Q14123-1]
DR ProteomicsDB; 59828; -. [Q14123-2]
DR Antibodypedia; 12721; 176 antibodies from 28 providers.
DR DNASU; 5137; -.
DR Ensembl; ENST00000321453.12; ENSP00000318105.7; ENSG00000154678.18. [Q14123-1]
DR Ensembl; ENST00000396182.6; ENSP00000379485.2; ENSG00000154678.18. [Q14123-2]
DR Ensembl; ENST00000396184.7; ENSP00000379487.3; ENSG00000154678.18. [Q14123-2]
DR Ensembl; ENST00000396191.6; ENSP00000379494.1; ENSG00000154678.18. [Q14123-1]
DR GeneID; 5137; -.
DR KEGG; hsa:5137; -.
DR MANE-Select; ENST00000396191.6; ENSP00000379494.1; NM_001191057.4; NP_001177986.1.
DR UCSC; uc003tcm.3; human. [Q14123-1]
DR CTD; 5137; -.
DR DisGeNET; 5137; -.
DR GeneCards; PDE1C; -.
DR HGNC; HGNC:8776; PDE1C.
DR HPA; ENSG00000154678; Group enriched (brain, heart muscle).
DR MalaCards; PDE1C; -.
DR MIM; 602987; gene.
DR MIM; 618140; phenotype.
DR neXtProt; NX_Q14123; -.
DR OpenTargets; ENSG00000154678; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA33124; -.
DR VEuPathDB; HostDB:ENSG00000154678; -.
DR eggNOG; KOG3688; Eukaryota.
DR GeneTree; ENSGT00940000155331; -.
DR OMA; HHRWTMQ; -.
DR OrthoDB; 1167208at2759; -.
DR PhylomeDB; Q14123; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.17; 2681.
DR PathwayCommons; Q14123; -.
DR Reactome; R-HSA-111957; Cam-PDE 1 activation.
DR SignaLink; Q14123; -.
DR SIGNOR; Q14123; -.
DR BioGRID-ORCS; 5137; 14 hits in 1066 CRISPR screens.
DR ChiTaRS; PDE1C; human.
DR GeneWiki; PDE1C; -.
DR GenomeRNAi; 5137; -.
DR Pharos; Q14123; Tclin.
DR PRO; PR:Q14123; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14123; protein.
DR Bgee; ENSG00000154678; Expressed in endothelial cell and 145 other tissues.
DR ExpressionAtlas; Q14123; baseline and differential.
DR Genevisible; Q14123; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; ISS: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:0007165; P:signal transduction; IBA:GO_Central.
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 Acetylation; Alternative splicing; Calmodulin-binding; cAMP; cGMP;
KW Deafness; Disease variant; Hydrolase; Lysosome; Magnesium; Metal-binding;
KW Non-syndromic deafness; Reference proteome; Zinc.
FT CHAIN 1..709
FT /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT cyclic nucleotide phosphodiesterase 1C"
FT /id="PRO_0000198792"
FT DOMAIN 151..528
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 123..146
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:P14100"
FT REGION 453..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q01064"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 1..38
FT /note="MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYK -> MTDAGNRKEG
FT FKKCRSATFSIDGYSFTIVANEAGDKNARPLARFSRSKSQNCLWNSLIDGLTGNVKEKP
FT RPTIVHDPRPPEEILADELPQLDSSEVLV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044468"
FT VAR_SEQ 631..634
FT /note="GTKQ -> DSQE (in isoform PDE1C1)"
FT /evidence="ECO:0000303|PubMed:8557689"
FT /id="VSP_004552"
FT VAR_SEQ 635..709
FT /note="Missing (in isoform PDE1C1)"
FT /evidence="ECO:0000303|PubMed:8557689"
FT /id="VSP_004553"
FT VARIANT 260
FT /note="A -> S (in DFNA74; increased 3',5'-cyclic-AMP
FT phosphodiesterase activity; increased 3',5'-cyclic-GMP
FT phosphodiesterase activity; approximately 10-fold increase
FT in 3',5'-cyclic-AMP and 3-fold for 3',5'-cyclic-GMP
FT compared to wild-type; dbSNP:rs775633137)"
FT /evidence="ECO:0000269|PubMed:29860631"
FT /id="VAR_081215"
FT CONFLICT 42
FT /note="Q -> F (in Ref. 2; BAC03734)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="R -> L (in Ref. 2; BAC03734)"
FT /evidence="ECO:0000305"
FT CONFLICT Q14123-3:4
FT /note="A -> V (in Ref. 2; BAC03734)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 80760 MW; 77133D4DDBE5F7C0 CRC64;
MESPTKEIEE FESNSLKYLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD
LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR
SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI EALKDVDKWS FDVFSLNEAS
GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV
HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH
HLSAAYRLLQ DDEEMNILIN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE
AIEKPKALSL MLHTADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS
TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDETSQT GGTGQRRSSL NSISSSDAKR
SGVKTSGSEG SAPINNSVIS VDYKSFKATW TEVVHINRER WRAKVPKEEK AKKEAEEKAR
LAAEEQQKEM EAKSQAEEGA SGKAEKKTSG ETKNQVNGTR ANKSDNPRGK NSKAEKSSGE
QQQNGDFKDG KNKTDKKDHS NIGNDSKKTD GTKQRSHGSP APSTSSTCRL TLPVIKPPLR
HFKRPAYASS SYAPSVSKKT DEHPARYKML DQRIKMKKIQ NISHNWNRK
