GenomeNet

Database: UniProt
Entry: W5PTV2_SHEEP
LinkDB: W5PTV2_SHEEP
Original site: W5PTV2_SHEEP 
ID   W5PTV2_SHEEP            Unreviewed;       794 AA.
AC   W5PTV2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=PDE4C {ECO:0000313|Ensembl:ENSOARP00000013883.1};
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000013883.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000013883.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000013883.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000013883.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AMGL01090832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5PTV2; -.
DR   SMR; W5PTV2; -.
DR   STRING; 9940.ENSOARP00000013883; -.
DR   PaxDb; 9940-ENSOARP00000013883; -.
DR   Ensembl; ENSOART00000014089.1; ENSOARP00000013883.1; ENSOARG00000012952.1.
DR   eggNOG; KOG3689; Eukaryota.
DR   HOGENOM; CLU_005940_5_1_1; -.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000002356; Chromosome 5.
DR   Bgee; ENSOARG00000012952; Expressed in longissimus thoracis muscle and 48 other cell types or tissues.
DR   ExpressionAtlas; W5PTV2; 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   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:SF135; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4C; 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:UP000002356}.
FT   DOMAIN          374..703
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          724..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..740
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        450
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         450..454
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         454
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="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         491
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         491
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         491
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         608
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         608
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         659
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ   SEQUENCE   794 AA;  88196 MW;  624C8BA4CC703558 CRC64;
     QLLGINPTLS PATFSCLSTF SADSSSLSSP LPALAGTSAR TLFPPGDGSR ALLSACSPFW
     RMETPKVQEG LEASRELNSA RSRQGVARAP KHLWRQPRRP IRIQQRFHSD PDKSVGRRER
     DLSLRPALEK SRRSWPTSFH RRLDLENGLS CGRSILDPQA GSGFGRIVQA PAQHSQRRES
     FLYRSDSDYE LSSKTMSRNS SMASDLHGED LIVTPFAQVL ASLRTVRSNV AALAHLQDRG
     AAKQACVCNT PSGSQPPPPT EDTGQKLALE TLDELDWCLD QLETLQTQHS VGEMASNKFK
     RMLNRELTHL SETSRSGNQV SEYISQTFLE QQTEVELPRA TPAEPPRPVS QISSLRALPH
     SSSLSTATVP RFGVQTDQEG QLAKELEDTS KWGLDVFKVA ELSGNRPLTA IMFSIFQERD
     LLKTFQIPAD TLATYLLMLE SHYHNDVAYH NSLHAADVAQ STHVLLATPA LEAVFTDLEV
     LAAIFASAIH DVDHPGVSNQ FLINTNSELA LMYNDASVLE NHHLAVGFKL LQAENCDIFQ
     NLSTKQRLSL RRMVIDIVLA TDMSKHMNLL ADLKTMVETK KVTSLGVLLL DNYSDRIQVL
     QSLVHCADLS NPTKPLPLYR QWTDRIMAEF FQQGDSERES GLDISPMCDK HTASVEKSQV
     GFIDYIAHPL WETWADLVHP DAQDLLDTLE DNREWYQSKI PRSPEDPTSP KQGSPDRFQF
     QLTLEEAEEE EEEEEEALDG EASKSPDTEL RSSEASPDPG ASPDPGAPHL DYQRTVGKPC
     RDHEGNAMAE PLGT
//
DBGET integrated database retrieval system