ID M3YRQ4_MUSPF Unreviewed; 861 AA.
AC M3YRQ4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE6A {ECO:0000313|Ensembl:ENSMPUP00000014014.1};
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:ENSMPUP00000014014.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000014014.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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; AEYP01000963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3YRQ4; -.
DR STRING; 9669.ENSMPUP00000014014; -.
DR Ensembl; ENSMPUT00000014237.1; ENSMPUP00000014014.1; ENSMPUG00000014122.1.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000161330; -.
DR HOGENOM; CLU_006980_2_0_1; -.
DR InParanoid; M3YRQ4; -.
DR OMA; GPHFTKR; -.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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:SF115; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT ALPHA; 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}.
FT DOMAIN 483..816
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 823..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 559
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 559..563
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 600
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 720
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 720
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 773
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 861 AA; 99602 MW; 54ED20B802270FB0 CRC64;
MGEVTADQVE KFLDSNIRFA KQYYNLRYRA KVISDMLGAK EADVDFSDYH SLSSVEESEI
IFDLLRDFQE NLQAERCIFN VMKKLCFLLR ADRMSLFMYR VRNGIAELAT RLFNVHKDAV
LEECLVVPDS EIVFPLDMGV VGHVAHSKKI ANVLNTEEDE HFCDFVDTLT EYKTKNILAS
PIMNGKDTVA VIMAVNKVDG PHFTKTDEEI LLKYLNFANL IMKVYHLSYL HNCETRRGQI
LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
PYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV AQNGLICNIM
NAPAEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDEMDETLM
ESLAQFLGWS VLNPDTYESM NKLENRKDIF QDMVKYHVKC DNEEIQKILK TREVYGKEPW
ECEEEELAEI LQGELPDAEK YEINKFHFSD LPLTELELVK CGIQMYYELK VVDKFHIPQE
ALVRFMYSLS KGYRKITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD
IDHRGTNNLY QMKKQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH
MMDIAIIATD LALYFKKRTM FQKIVDQSKT YESQQEWTQY MMLEQTRKEI VMAMMMTACD
LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYDAKM KALEEEKQKQ EAAKQAAAGN
QPGGNPGPAG GAPASKSCCI Q
//
