ID Q8CDV2_MOUSE Unreviewed; 603 AA.
AC Q8CDV2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Pde1c {ECO:0000313|Ensembl:ENSMUSP00000131892.2,
GN ECO:0000313|MGI:MGI:108413};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC26499.1};
RN [1] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA Hayashizaki Y.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [7] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [8] {ECO:0000313|EMBL:BAC26499.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC26499.1};
RC TISSUE=Testis {ECO:0000313|EMBL:BAC26499.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [9] {ECO:0000313|Ensembl:ENSMUSP00000131892.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131892.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [10] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11] {ECO:0000313|Ensembl:ENSMUSP00000131892.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000131892.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000256|ARBA:ARBA00033675};
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:0000256|ARBA:ARBA00033684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000256|ARBA:ARBA00033684};
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:0000256|ARBA:ARBA00033709};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC Evidence={ECO:0000256|ARBA:ARBA00033709};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
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:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE1 subfamily. {ECO:0000256|ARBA:ARBA00010664}.
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DR EMBL; AK029531; BAC26499.1; -; mRNA.
DR RefSeq; NP_001153429.1; NM_001159957.1.
DR RefSeq; NP_001153432.1; NM_001159960.1.
DR ProteomicsDB; 330385; -.
DR Antibodypedia; 12721; 195 antibodies from 28 providers.
DR DNASU; 18575; -.
DR Ensembl; ENSMUST00000166890.8; ENSMUSP00000131892.2; ENSMUSG00000004347.18.
DR GeneID; 18575; -.
DR UCSC; uc009cbg.2; mouse.
DR AGR; MGI:108413; -.
DR CTD; 5137; -.
DR MGI; MGI:108413; Pde1c.
DR VEuPathDB; HostDB:ENSMUSG00000004347; -.
DR GeneTree; ENSGT00940000155331; -.
DR OrthoDB; 240889at2759; -.
DR BioGRID-ORCS; 18575; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Pde1c; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000004347; Expressed in lumbar dorsal root ganglion and 136 other cell types or tissues.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 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 PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF32; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1C; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Proteomics identification {ECO:0007829|MaxQB:Q8CDV2,
KW ECO:0007829|PeptideAtlas:Q8CDV2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 123..500
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 425..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 200..204
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 241
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 348
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 399
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 603 AA; 68348 MW; 4561AC1AF2FBCF47 CRC64;
MAYSIQRKYK KTSQRLRSLV KQLERGEASV VDLKKNLEYA ATVLESVYID ETRRLLDTED
ELSDIQSDAV PSEVRDWLAS TFTRQMGMML RRSDEKPRFK SIVHAVQAGI FVERMYRRTS
NMVGLSYPPA VIDALKDVDT WSFDVFSLNE ASGDHALKFI FYELLTRYDL ISRFKIPISA
LVSFVEALEV GYSKHKNPYH NLMHAADVTQ TVHYLLYKTG VANWLTELEI FAIIFSAAIH
DYEHTGTTNN FHIQTRSDPA ILYNDRSVLE NHHLSAAYRL LQEDEEMNIL VNLSKDDWRE
FRTLVIEMVM ATDMSCHFQQ IKAMKTALQQ PEAIEKPKAL SLMLHTADIS HPAKAWDLHH
RWTMSLLEEF FRQGDREAEL GLPFSPLCDR KSTMVAQSQV GFIDFIVEPT FTVLTDMTEK
IVSPLIDESS QTGGTGQRRS SLNSINSSDA KRSGVKSSGS DGSAPINNSV IPVDYKSFKA
TWTEVVQINR ERWRAKVPKE EKAKKEAEEK ARLAAEEKQK EMEAKSQAEQ GTTSKGEKKT
SGEAKSQVNG TRKGDNPRGK NSKGEKAGEK QQNGDLKDGK NKADKKDHSN TGNESKKTDD
PEE
//
