ID M3XVT2_MUSPF Unreviewed; 934 AA.
AC M3XVT2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE11A {ECO:0000313|Ensembl:ENSMPUP00000003182.1,
GN ECO:0000313|RefSeq:XP_004769050.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003182.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003182.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004769050.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004769050.1};
RG RefSeq;
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 EMBL; AEYP01071587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01071596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004769050.1; XM_004768993.3.
DR STRING; 9669.ENSMPUP00000003182; -.
DR Ensembl; ENSMPUT00000003247.1; ENSMPUP00000003182.1; ENSMPUG00000003215.1.
DR GeneID; 101692681; -.
DR KEGG; mpuf:101692681; -.
DR CTD; 50940; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000162151; -.
DR HOGENOM; CLU_006980_0_1_1; -.
DR OMA; IHCILAT; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0030553; F:cGMP binding; IEA:Ensembl.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
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:SF130; DUAL 3',5'-CYCLIC-AMP AND -GMP PHOSPHODIESTERASE 11A; 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; 2.
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:UP000000715}.
FT DOMAIN 588..912
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 40..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 664
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 664..668
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 704
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 705
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 705
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 816
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 869
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 934 AA; 104634 MW; 07F51B7AE55B0567 CRC64;
MTASHLDFGE VETFLDRHPE LFEDYLMRKG KQEMVEKWLQ RHRESQGAVG TRPTVAGTSS
VAHSGGAGSG RVGGGTGPNS SANSQLAPGG GDCGGVPLSP SWASGSRGDG SLQRRASQKE
LRKSFARSKA INVNRTYDEQ VTARAQEPLS SVRRRALLRK ASSLPPTTAH ILSALLESRV
NLPQYPPTAM DYKCHLKKHN ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL
FLVEGAAAGK KSLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP
DAYQDRRFND EIDKLTGYKT KSLLCMPIRS SDGEIIGVAQ AINKIPEGAP FTEDDEKVMQ
MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC
ERCSVLLLED IESPVVKFTK SFELMSPKCS ADAENSFKES VEKSSYSDWL VNNSVAELVA
STGLPVNISD AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKAFD
DADQRLFEAF VIFCGLGINN TIMYNQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANV
PLVSELAIND IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM
VLYHNWRHAF NVCQLMFAML TTAGFQEILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSG
SALAQLYGTS ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY
FERRTEFFEL VSKGDYDWNI KNHRDIFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE
QGDRERAELK LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNVK LKPMLDSVAA
NRRKWEELHQ KRLLASAASP SSSSLMLAAE EDRN
//
