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Database: UniProt
Entry: A0A2Y9Q0W5_DELLE
LinkDB: A0A2Y9Q0W5_DELLE
Original site: A0A2Y9Q0W5_DELLE 
ID   A0A2Y9Q0W5_DELLE        Unreviewed;       678 AA.
AC   A0A2Y9Q0W5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=PDE4D {ECO:0000313|RefSeq:XP_022452739.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022452739.1};
RN   [1] {ECO:0000313|RefSeq:XP_022452739.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022452739.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; EC=3.1.4.53;
CC         Evidence={ECO:0000256|ARBA:ARBA00033681};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000256|ARBA:ARBA00033681};
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   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE4 subfamily. {ECO:0000256|ARBA:ARBA00009517}.
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DR   RefSeq; XP_022452739.1; XM_022597031.2.
DR   AlphaFoldDB; A0A2Y9Q0W5; -.
DR   Ensembl; ENSDLET00000012396; ENSDLEP00000011233; ENSDLEG00000008101.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR040844; PDE4_UCR.
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:SF91; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4D; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF18100; PDE4_UCR; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
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   cAMP {ECO:0000256|ARBA:ARBA00023149}; 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:UP000248483}.
FT   DOMAIN          256..585
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          212..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..610
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..663
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        332
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         332..336
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         372
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         373
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         373
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         490
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         490
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         541
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   678 AA;  76633 MW;  501A3D4AC811C6D6 CRC64;
     MSIIMKPRSR STSSLRTSEG VCFDVDNGTS SGRSPLDPMT SPGSGLILQA NFVHSQRRES
     FLYRSDSDYD LSPKSMSRNS SIASDIHGDD LIVTPFAQVL ASLRTVRNNF AALTNLQDRA
     PSKRSPMCNQ PSINKATLTE EAYQKLASET LEELDWCLDQ LETLQTRHSV SEMASNKFKR
     MLNRELTHLS EMSRSGNQVS EYISNTFLDK QHEVEIPSPT QKEKEKKKRP MSQISGVKKL
     MHSSSLTNSS IPRFGVKTEQ EDILAKELED VNKWGLHVFR IAELSGNRPL TVIMHTIFQE
     RDLLKTFKIP VDTLITYLMT LEDHYHADVA YHNNIHAADV VQSTHVLLST PALEAVFTDL
     EILAAIFASA IHDVDHPGVS NQFLINTNSE LALMYNDSSV LENHHLAVGF KLLQEENCDI
     FQNLTKKQRQ SLRKMVIDIV LATDMSKHMN LLADLKTMVE TKKVTSSGVL LLDNYSDRIQ
     VLQNMVHCAD LSNPTKPLQL YRQWTDRIME EFFRQGDRER ERGMEISPMC DKHNASVEKS
     QVGFIDYIVH PLWETWADLV HPDAQDILDT LEDNREWYQS TIPQSPSPAP DDQEEGRQGQ
     TEKFQFELTL EEDGESDTEK DSGSQVEEDT SCSDSKTLCT QDSESTEIPL DEQAEEEAVG
     EEESQPEACA IGDHSPDT
//
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