ID A0A2I3SKH6_PANTR Unreviewed; 685 AA.
AC A0A2I3SKH6; A0A2J8PZR6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE2A {ECO:0000313|Ensembl:ENSPTRP00000077407.1,
GN ECO:0000313|VGNC:VGNC:3074};
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:ENSPTRP00000077407.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000077407.1, 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:ENSPTRP00000077407.1}
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; AACZ04016269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3SKH6; -.
DR SMR; A0A2I3SKH6; -.
DR Ensembl; ENSPTRT00000105175.1; ENSPTRP00000077407.1; ENSPTRG00000004036.6.
DR VGNC; VGNC:3074; PDE2A.
DR GeneTree; ENSGT00940000159817; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000004036; Expressed in dorsolateral prefrontal cortex 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; -; 1.
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; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 1.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..685
FT /note="Phosphodiesterase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015081605"
FT DOMAIN 322..646
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 400
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 400..404
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 441
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 552
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 603
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 685 AA; 78177 MW; A6087394B98221C3 CRC64;
MVLVLHHILI AVVQFLRRGQ QVFLKPDEPP PPPQPCADSL QDALLSLGSV IDISGLQRAV
KEALSAVLPR VETVYTYLLD GESQLVCEDP PHELPQEGKV RFTDEDEHVI QHCFHYTSTV
LTSTLAFQKE QKLKCECQAL LQVAKNLFTH LDDVSVLLQE IITEARNLSN AEICSVFLLD
QNELVAKVFD GGVVDDESYE IRIPADQGIA GHVATTGQIL NIPDAYAHPL FYRGVDDSTG
FRTRNILCFP IKNENQEVIG VAELVNKING PWFSKFDEDL ATAFSIYCGI SIAHSLLYKK
VNEAQYRSHL ANEMMMYHMK VSDDEYTKLL HDGIQPVAAI DSNFASFTYT PRSLPEDDTS
MAILSMLQDM NFINNYKIDC PTLARFCLMV KKGYRDPPYH NWMHAFSVSH FCYLLYKNLE
LTNYLEDIEI FALFISCMCH DLDHRGTNNS FQVASKSVLA ALYSSEGSVM ERHHFAQAIA
ILNTHGCNIF DHFSRKDYQR MLDLMRDIIL ATDLAHHLRI FKDLQKMAEV GYDRNNKQHH
RLLLCLLMTS CDLSDQTKGW KTTRKIAELI YKEFFSQGDL EKAMGNRPME MMDREKAYIP
ELQISFMEHI AMPIYKLLQD LFPKAAELYE RVASNREHWT KVSHKFTIRG LPSNNSLDFL
DEEYEVPDLD GTRAPINGCC SLDAE
//