ID H2R4C3_PANTR Unreviewed; 772 AA.
AC H2R4C3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE10A {ECO:0000313|Ensembl:ENSPTRP00000046931.5,
GN ECO:0000313|VGNC:VGNC:7902};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000046931.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000046931.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000046931.5}
RP IDENTIFICATION.
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 EMBL; AACZ04028740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04028741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04028742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2R4C3; -.
DR Ensembl; ENSPTRT00000050003.5; ENSPTRP00000046931.5; ENSPTRG00000018787.6.
DR VGNC; VGNC:7902; PDE10A.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156543; -.
DR HOGENOM; CLU_006980_1_0_1; -.
DR OMA; HNWAHGW; -.
DR TreeFam; TF316499; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018787; Expressed in colon and 18 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:UP000002277}.
FT DOMAIN 435..752
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 508
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 508..512
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
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 547
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 657
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 709
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 772 AA; 87383 MW; 449A76CB2B30D5BA CRC64;
MATLYGLTDE KVKAYLSLHP QVLDEFVSES VSAETVEKWL KRKNNKSEDE SAPKEVSRYQ
DTNMQGVVYE LNSYIEQRLD TGGDNQLLLY ELSSIIKIAT KADGFALYFL GECNNSLCIF
TPPGIKEGKP RLIPAGPITQ GTTVSAYVAK SRKTLLVEDI LGDERFPGGT GLESGTRIQS
VLCLPIVTAI GDLIGILELY RHWGKEAFCL SHQEVATANL AWASVAIHQV QVCRGLAKQT
ELNDFLLDVS KTYFDNIVAI DSLLEHIMIY AKNLVNADRC ALFQVDHKNK ELYSDLFDIG
EEKEGKPVFK KTKEIRFSIE KGIAGQVART GEVLNIPDAY ADPRFNREVD LYTGYTTRNI
LCMPIVSRGS VIGVVQMVNK ISGSAFSKTD ENNFKMFAVF CALALHCANM YHRIRHSECI
YRVTMEKLSY HSICTSEEWQ GLMQFTLPVR LCKEIELFHF DIGPFENMWP GIFVYMVHRS
CGTSCFELEK LCRFIMSVKK NYRRVPYHNW KHAVTVAHCM YAILQNNHTL FTDLERKGLL
IACLCHDLDH RGFSNSYLQK FDHPLAALYS TSTMEQHHFS QTVSILQLEG HNIFSTLSSS
EYEQVLEIIR KAIIATDLAL YFGNRKQLEE MYQTGSLNLN NQSHRDRVIG LMMTACDLCS
VTKLWPVTKL TANDIYAEFW AEGDEMKKLG IQPIPMMDRD KKDEVPQGQL GFYNAVAIPC
YTTLTQILPP TEPLLKACRD NLSQWEKVIR GEETATWISS PSVAQKAAAS ED
//
