ID A0A2K5N3U4_CERAT Unreviewed; 779 AA.
AC A0A2K5N3U4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE10A {ECO:0000313|Ensembl:ENSCATP00000032134.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000032134.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032134.1}
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_011933414.1; XM_012078024.1.
DR RefSeq; XP_011933415.1; XM_012078025.1.
DR AlphaFoldDB; A0A2K5N3U4; -.
DR Ensembl; ENSCATT00000056401.1; ENSCATP00000032134.1; ENSCATG00000039033.1.
DR GeneID; 105594220; -.
DR CTD; 10846; -.
DR GeneTree; ENSGT00940000156543; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000039033; Expressed in cerebellum and 11 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:UP000233060}.
FT DOMAIN 442..759
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 515
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 515..519
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 554
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 664
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 716
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 779 AA; 88408 MW; BC8D1E86643AF700 CRC64;
MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK NNKSEDESAP
KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS SIIKIATKAD GFALYFLGEC
NNSLCIFTPP GIKEGKPRLI PAGPITQGTT VSAYVAKSRK TLLVEDILGD ERFPRGTGLE
SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC
RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY
SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP RFNREVDLYT
GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL ALHCANMYHR
IRHSECIYRV TMEKLSYHSI CTAEEWQGLM QFTLPVRLCK EIELFHFDIG PFENMWPGIF
VYMVHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHALFTD
LERKGLLIAC LCHDLDHRGF SNTYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI
FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS HRDRVIGLMM
TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKKD EVPQGQLGFY
NAVAIPCYTT LTQILPPTEP LLKACRDNLN QWEKVIRGEE TATWISSPSV AQKAAASED
//
