ID Q62037_MOUSE Unreviewed; 800 AA.
AC Q62037;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 22-FEB-2023, entry version 114.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Pde6b {ECO:0000313|MGI:MGI:97525};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:CAA61202.1};
RN [1] {ECO:0000313|EMBL:CAA61202.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Retina {ECO:0000313|EMBL:CAA61202.1};
RX PubMed=1847109; DOI=10.1016/0014-5793(91)80095-K;
RA Baehr W., Champagne M.S., Lee A.K., Pittler S.J.;
RT "Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase
RT alpha- and beta-subunits, and identification of beta'-, a putative beta-
RT subunit isozyme produced by alternative splicing of the beta-subunit
RT gene.";
RL FEBS Lett. 278:107-114(1991).
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; X87952; CAA61202.1; -; mRNA.
DR PIR; S13032; S13032.
DR AlphaFoldDB; Q62037; -.
DR AGR; MGI:97525; -.
DR MGI; MGI:97525; Pde6b.
DR ChiTaRS; Pde6b; mouse.
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:SF73; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT BETA; 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 2: Evidence at transcript level;
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 481..800
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 557
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 557..561
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 598
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 718
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 718
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 771
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 800 AA; 92077 MW; 06BB88BCB8E6B90F CRC64;
MSLSEEQVRS FLDGNPTFAH QYFGKKLSPE NVAGACEDGW LADCGSLREL CQVEESAALF
ELVQDMQESV NMERVVFKIL RRLCTILHAD RCSLFMYRQR NGIAELATRL FSVQPDSLLE
DCLVPPDSEI VFPLDIGIVG HVAQTKKMIN VQDVAECPHF SSFADELTDY VTKNILSTPI
MNGKDVVAVI MAVNKLDGPC FTSEDEDVFT KYLNFATLNL KIYHLSYLHN CETRRGQVLL
WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW PVLMGEAQPY
SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PTPPADHWAL ASGLPTYVAE SGFICNIMNA
SADEMFNFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DDQDEVLMES
LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQEILPTR DRLGKEPADC
EEDELGKILK EELPGPTKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL
VRFLFSVSKA YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLAEE SLNIYQNLNR RQHEHVIHLM
DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DKKSWVEYLS LETTRKEIVM AMMMTACDLS
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT
FVYKFPLGIF SISRRDPAHV
//
