ID F8WHK3_MOUSE Unreviewed; 716 AA.
AC F8WHK3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Pde10a {ECO:0000313|Ensembl:ENSMUSP00000024647.7,
GN ECO:0000313|MGI:MGI:1345143};
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|Ensembl:ENSMUSP00000024647.7, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000024647.7, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000024647.7,
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 [2] {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 [3] {ECO:0000313|Ensembl:ENSMUSP00000024647.7}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000024647.7};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU363067}.
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DR ProteomicsDB; 338958; -.
DR Antibodypedia; 33512; 285 antibodies from 27 providers.
DR Ensembl; ENSMUST00000024647.13; ENSMUSP00000024647.7; ENSMUSG00000023868.18.
DR Ensembl; ENSMUST00000115715.8; ENSMUSP00000111380.2; ENSMUSG00000023868.18.
DR AGR; MGI:1345143; -.
DR MGI; MGI:1345143; Pde10a.
DR VEuPathDB; HostDB:ENSMUSG00000023868; -.
DR GeneTree; ENSGT00940000156543; -.
DR HOGENOM; CLU_006980_1_0_1; -.
DR ChiTaRS; Pde10a; mouse.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000023868; Expressed in caudate-putamen and 235 other cell types or tissues.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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 PANTHER; PTHR11347:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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 cGMP {ECO:0000256|ARBA:ARBA00022535};
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:F8WHK3,
KW ECO:0007829|PeptideAtlas:F8WHK3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 372..689
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 694..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 445
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 445..449
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 483
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 484
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 594
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 646
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 716 AA; 81220 MW; F10D3CB6928899A3 CRC64;
MQGVVYELNS YIEQRLDTGG DNHLLLYELS SIIRIATKAD GFALYFLGEC NNSLCVFIPP
GMKEGQPRLI PAGPITQGTT ISAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC
LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC RGLAKQTELN
DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY SDLFDIGEEK
EGKPIFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP RFNREVDLYT GYTTRNILCM
PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL ALHCANMYHR IRHSECIYRV
TMEKLSYHSI CTSEEWQGLM RFNLPARICR DIELFHFDIG PFENMWPGIF VYMIHRSCGT
SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNNGLFTD LERKGLLIAC
LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI FSTLSSSEYE
QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLHNQS HRDRVIGLMM TACDLCSVTK
LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKRD EVPQGQLGFY NAVAIPCYTT
LTQILPPTEP LLKACRDNLN QWEKVIRGEE TAMWISGPGP APSKSTPEKL NVKVED
//
