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Database: UniProt
Entry: W5MLE4_LEPOC
LinkDB: W5MLE4_LEPOC
Original site: W5MLE4_LEPOC 
ID   W5MLE4_LEPOC            Unreviewed;       677 AA.
AC   W5MLE4;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000009203.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000009203.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   EMBL; AHAT01007670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5MLE4; -.
DR   STRING; 7918.ENSLOCP00000009203; -.
DR   Ensembl; ENSLOCT00000009214.1; ENSLOCP00000009203.1; ENSLOCG00000007575.1.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000159788; -.
DR   HOGENOM; CLU_005940_5_3_1; -.
DR   InParanoid; W5MLE4; -.
DR   OMA; SHCICSF; -.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000018468; Linkage group LG6.
DR   Bgee; ENSLOCG00000007575; Expressed in camera-type eye and 10 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
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:SF74; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4A; 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   SMART; SM00471; HDc; 1.
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};
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:UP000018468}.
FT   DOMAIN          232..561
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..677
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        308
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         308..312
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         349
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         466
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         466
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         517
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   677 AA;  76299 MW;  3E4382A1314A1FD6 CRC64;
     FDVENGPSPG RSPLDSQASP GLVLHPSFPQ SQRRESFLYR SDSDYDMSPK TMSRNSSITS
     EAHAEDLIVT PFAQVLASLR SVRSNFSILA NVTTPTNKRS PVGSQPTVPK ATLSEETYQQ
     LAKETLEELD WCLDQLETIQ TYRSVSEMAS NKFKRMLNRE LTHLSEMSRS GNQVSEYISS
     TFLDKQNEVE IPSPTQKERE KKKKQPMCQI SGVKKLMHSS SLTNSSIPRF GVKTEQEDSL
     ARELDDLNKW GLNIFRVAEF SNNRPLSCIM FAIFQERDLM KTFKIPVDTF ITYIMTLEDH
     YHADVAYHNS LHAADVTQST HVLLSTPALD AVFTDLEILA ALFAAAIHDV DHPGVSNQFL
     INTNSELALM YNDESVLENH HLAVGFKLLQ EENCDIFQNL SKRQRQSLRK MVIDMVLATD
     MSKHMSLLAD LKTMVETKKV TSSGVLLLDH YTDRIQVLRN MVHCADLSNP TKPLELYRQW
     TDRIMEEFFR QGDKERERGM EISPMCDKHT ASVEKSQVGF IDYIVHPLWE TWADLVHPDA
     QEILDTLEDN RDWYQSMIPQ SPSPPPDDPE KEPDACLDKF QFELTLEEEG EDPEGRNSRG
     AAAEEEGSPS QNHLGENCVA GSPEGEDEDP GQPGEPGVVV VVVGENGHSE GSPEEEEEEE
     DDEVGEEEEL PSSPAET
//
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