ID A0A2K6B761_MACNE Unreviewed; 806 AA.
AC A0A2K6B761;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE10A {ECO:0000313|Ensembl:ENSMNEP00000007259.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000007259.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000007259.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_011749302.1; XM_011751000.1.
DR AlphaFoldDB; A0A2K6B761; -.
DR STRING; 9545.ENSMNEP00000007259; -.
DR Ensembl; ENSMNET00000031409.1; ENSMNEP00000007259.1; ENSMNEG00000027445.1.
DR GeneID; 105487544; -.
DR CTD; 10846; -.
DR GeneTree; ENSGT00940000156543; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000027445; Expressed in cerebellum and 9 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 469..786
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 542
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 542..546
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 581
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 691
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 691
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 743
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 806 AA; 90838 MW; D11C8F3ECE250412 CRC64;
MLKGGSKGPA LLALRSGTDP RAQMSDDTAE GTLDPCSAPG LTDEKVKAYL SLHPQVLDEF
VSESVSAETV EKWLKRKNNK SEDESAPKEV SRYQDTNMQG VVYELNSYIE QRLDTGGDNQ
LLLYELSSII KIATKADGFA LYFLGECNNS LCIFTPPGIK EGKPRLIPAG PITQGTTISA
YVAKSRKTLL VEDILGDERF PRGTGLESGT RIQSVLCLPI VTAIGDLIGI LELYRHWGKE
AFCLSHQEVA TANLAWASVA IHQVQVCRGL AKQTELNDFL LDVSKTYFDN IVAIDSLLEH
IMIYAKNLVN ADRCALFQVD HKNKELYSDL FDIGEEKEGK PVFKKTKEIR FSIEKGIAGQ
VARTGEVLNI PDAYADPRFN REVDLYTGYT TRNILCMPIV SRGSVIGVVQ MVNKISGSAF
SKTDENNFKM FAVFCALALH CANMYHRIRH SECIYRVTME KLSYHSICTA EEWQGLMRFT
LPVRLCKEIE LFHFDIGPFE NMWPGIFVYM VHRSCGTSCF ELEKLCRFIM SVKKNYRRVP
YHNWKHAVTV AHCMYAILQN NHALFTDLER KGLLIACLCH DLDHRGFSNT YLQKFDHPLA
ALYSTSTMEQ HHFSQTVSIL QLEGHNIFST LSSSEYEQVL EIIRKAIIAT DLALYFGNRK
QLEEMYQTGS LNLNNQSHRD RVIGLMMTAC DLCSVTKLWP VTKLTANDIY AEFWAEGDEM
KKLGIQPIPM MDRDKKDEVP QGQLGFYNAV AIPCYTTLTQ ILPPTEPLLK ACRDNLNQWE
KVIRGEETAT WISSPSVAQK AAASED
//
