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Database: UniProt
Entry: A0A3Q1NKA2_BOVIN
LinkDB: A0A3Q1NKA2_BOVIN
Original site: A0A3Q1NKA2_BOVIN 
ID   A0A3Q1NKA2_BOVIN        Unreviewed;       762 AA.
AC   A0A3Q1NKA2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, 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=PDE8B {ECO:0000313|Ensembl:ENSBTAP00000072731.1};
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:ENSBTAP00000072731.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000072731.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072731.1,
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:ENSBTAP00000072731.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000072731.1};
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   -!- 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       PDE8 subfamily. {ECO:0000256|ARBA:ARBA00006437}.
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DR   AlphaFoldDB; A0A3Q1NKA2; -.
DR   Ensembl; ENSBTAT00000083290.1; ENSBTAP00000072731.1; ENSBTAG00000020205.6.
DR   VEuPathDB; HostDB:ENSBTAG00000020205; -.
DR   GeneTree; ENSGT00940000157817; -.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000020205; Expressed in cardiac ventricle and 103 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1NKA2; baseline.
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   CDD; cd00077; HDc; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF98; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8B; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50112; PAS; 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:UP000009136}.
FT   DOMAIN          151..215
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          416..752
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        492
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         492..496
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         496
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         532
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         533
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         533
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         533
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         658
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         658
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         710
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   762 AA;  86173 MW;  4F70B4A2E85D5073 CRC64;
     FSQPQSLRRN QVSSAEVRIG PMRLTQDPIQ VLLIFAKEDS QSDGFWWACD RAGYSCNIAR
     TPESALECFL DKHHEIIVID HRQTQNFDAE AVCRSIRATN PSEHAVILAV VSQRFMENSS
     IIACYNELIQ IEHGEVLSQF KLRACNSVFT ALDHCHEAIE ITSDDHVIQY VNPAFERMMG
     YHKGELLGKE LAELPKSDKN RADLLDTINT CIKKGKEWQG VYYARRKSGD SIQQHVKITP
     VIGQGGKIRH FVSLKKLCCS TDKNKQILKI HRDSGDNSQT ESHSFRYKNR RKESIDVKSI
     SSRGSDAPSL QNRRYPSMAR IHSMTIEAPI TKVINIINAA QENSPVTVAE ALDRVLEILR
     TTELYSPQLG TKDEDPHTSD LVGGLMTDGL RRLSGNEYVF TKNVHQSHSH LAMPGTITDV
     PPSVAQLLDN EESWEFNIFE LEAVTHKRPL VYLGLKVFSR FGVCEFLHCS ETTLRAWLQV
     IEANYHSSNA YHNSTHAADV LHATAFFLGK ERVKGSLDQL DEVAALIAAT VHDVDHPGRT
     NSFLCNAGSE LAVLYNDTAV LESHHTALAF QLTVKDSKCN IFKNIDRNHY RTLRQAIIDM
     VLATEMTKHF EHVNKFVNSI NKPMAAEIDG SDCECSPPGK NFPENQTLIK RMMIKCADVA
     NPCRPLDLCI EWAGRISEEY FAQTDEEKRQ GLPVVMPVFD RNTCSIPKSQ ISFIDYFITD
     MFDAWDAFAH LPTLMQHLAD NYKHWKTLDD LKCKSLRLPS DS
//
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