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Database: UniProt
Entry: A0A3Q1N0G7_BOVIN
LinkDB: A0A3Q1N0G7_BOVIN
Original site: A0A3Q1N0G7_BOVIN 
ID   A0A3Q1N0G7_BOVIN        Unreviewed;       942 AA.
AC   A0A3Q1N0G7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=PDE2A {ECO:0000313|Ensembl:ENSBTAP00000062184.1,
GN   ECO:0000313|VGNC:VGNC:32674};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000062184.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000062184.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062184.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000062184.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062184.1};
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   RefSeq; NP_001137318.1; NM_001143846.1.
DR   AlphaFoldDB; A0A3Q1N0G7; -.
DR   Ensembl; ENSBTAT00000072822.1; ENSBTAP00000062184.1; ENSBTAG00000008419.6.
DR   GeneID; 281971; -.
DR   CTD; 5138; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008419; -.
DR   VGNC; VGNC:32674; PDE2A.
DR   GeneTree; ENSGT00940000159817; -.
DR   OMA; HVKKGYR; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000008419; Expressed in temporal cortex and 103 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1N0G7; baseline.
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; 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:UP000009136}.
FT   DOMAIN          579..903
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          16..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        657
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         657..661
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         661
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         697
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         698
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         698
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         809
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         809
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         860
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   942 AA;  105576 MW;  27E31145C4AF2865 CRC64;
     MGQACGHSIL CRSQQYPAAR PAEPRGQQVF LKPDEPPPPP QPCADSLQDA LLSLGSVIDV
     AGLQQAVKEA LSAVLPKVET VYTYLLDGES RLVCEEPPHE LPQEGKVREA VISRKRLGCN
     GLGPSDLPGK PLARLVAPLA PDTQVLVIPL VDKEAGAVAA VILVHCGQLS DNEEWSLQAV
     EKHTLVALKR VQALQQRESS VAPEATQNPP EEAAGDQKGG VAYTDQDRKI LQLCGELYDL
     DASSLQLKVL QYLQQETQAS RCCLLLVSED NLQLSCKVIG DKVLEEEISF PLTTGRLGQV
     VEDKKSIQLK DLTSEDMQQL QSMLGCEVQA MLCVPVISRA TDQVVALACA FNKLGGDLFT
     DQDEHVIQHC FHYTSTVLTS TLAFQKEQKL KCECQALLQV AKNLFTHLDD VSVLLQEIIT
     EARNLSNAEI CSVFLLDQNE LVAKVFDGGV VEDESYEIRI PADQGIAGHV ATTGQILNIP
     DAYAHPLFYR GVDDSTGFRT RNILCFPIKN ENQEVIGVAE LVNKINGPWF SKFDEDLATA
     FSIYCGISIA HSLLYKKVNE AQYRSHLANE MMMYHMKVSD DEYTKLLHDG IQPVAAIDSN
     FASFTYTPRS LPEDDTSMAI LSMLQDMNFI NNYKIDCPTL ARFCLMVKKG YRDPPYHNWM
     HAFSVSHFCY LLYKNLELTN YLEDMEIFAL FISCMCHDLD HRGTNNSFQV ASKSVLAALY
     SSEGSVMERH HFAQAIAILN THGCNIFDHF SRKDYQRMLD LMRDIILATD LAHHLRIFKD
     LQKMAEVGYD RTNKQHHSLL LCLLMTSCDL SDQTKGWKTT RKIAELIYKE FFSQGDLEKA
     MGNRPMEMMD REKAYIPELQ ISFMEHIAMP IYKLLQDLFP KAAELYERVA SNREHWTKVS
     HKFTIRGLPS NNSLDFLDEE YEVPDLDGAR APINGCCSLD AE
//
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