ID A0A2I3H0F5_NOMLE Unreviewed; 950 AA.
AC A0A2I3H0F5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE2A {ECO:0000313|Ensembl:ENSNLEP00000037074.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000037074.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000037074.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000037074.1}
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; ADFV01111729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01111738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3H0F5; -.
DR STRING; 61853.ENSNLEP00000037074; -.
DR Ensembl; ENSNLET00000047806.1; ENSNLEP00000037074.1; ENSNLEG00000017175.3.
DR GeneTree; ENSGT00940000159817; -.
DR InParanoid; A0A2I3H0F5; -.
DR OMA; HVKKGYR; -.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
DR GO; GO:0030553; F:cGMP binding; IEA:Ensembl.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0042301; F:phosphate ion binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030911; F:TPR domain binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:1904613; P:cellular response to 2,3,7,8-tetrachlorodibenzodioxine; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071321; P:cellular response to cGMP; IEA:Ensembl.
DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0046069; P:cGMP catabolic process; IEA:Ensembl.
DR GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0010752; P:regulation of cGMP-mediated signaling; IEA:Ensembl.
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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF102; 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; 3.
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:UP000001073}.
FT DOMAIN 587..911
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 665
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 665..669
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 706
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 706
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 706
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 817
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 868
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 950 AA; 106270 MW; E9DFC719B7707146 CRC64;
MGQACGHSIL CRSQQYPAAR PSFGQMGLPW PAWQSPSLPS PLFQDALLSL GSVIDISGLQ
RAVKEALSAV LPRVVGTVYT YLLDGESRLV CEDPLHELPQ EGKVREAIIS RKRLGCNGLG
FSDLPGKPLA RLVAPLAPDT QVLVMPLADK EAGAVAAVIL VHCGQLSDNE EWSLQAVEKH
TLVALRRVQA LQQRGPREAP RAVQNPPEGA AEDQKGGAAY TDRDRKILQL CGELYDLDAS
SLQLKVLQYL QQETRASRCC LLLVSEDNLQ LSCKVIGDKV LGEEVSFPLT GCLGQVVEDK
KSIQLKDLTS EDVQQLQSML GCALQAMLCV PVISRATDQV VALACAFNKL EGDLFTDQDE
HVIQHCFHYT STVLTSTLAF QKEQKLKCEC QALLQVAKNL FTHLGECTVL SAWVCVEARG
LGSLVSPCPR GPNPSLHSCS VFLLDQNELV AKVFDGGVVD DESYEIRIPA DQGIAGHVAT
TGQILNIPDA YAHPLFYRGV DDSTGFRTRN ILCFPIKNEN QEVIGVAELV NKINGPWFSK
FDEDLATAFS IYCGISIAHS LLYKKVNEAQ YRSHLANEMM MYHMKVSDDE YTKLLHDGIQ
PVAAIDCNFA SFTYTPRSLP EDDTSMAILS MLQDMNFINN YKIDCPTLAR FCLMVKKGYR
DPPYHNWMHA FSVSHFCYLL YKNLELTNYL EDIEIFALFI SCMCHDLDHR GTNNSFQVAS
KSVLAALYSS EGSVMERHHF AQAIAILNTH GCNIFDHFSR KDYQRMLDLM RDIILATDLA
HHLRIFKDLQ KMAEVGYDRN NKQHHRLLLC LLMTSCDLSD QTKGWKTTRK IAELIYKEFF
SQGDLEKAMG NRPMEMMDRE KAYIPELQIS FMEHIAMPIY KLLQDLFPKA AELYERVASN
REHWTKVSHK FTIRGLPSNN SLDFLDEEYE VPDLDGTGAP INGCCSLDAE
//
