ID   PDE6A_CANLF             Reviewed;         861 AA.
AC   Q28263; Q29470;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha {ECO:0000250|UniProtKB:P16499};
DE            Short=GMP-PDE alpha;
DE            EC=3.1.4.35 {ECO:0000250|UniProtKB:P16499};
DE   Flags: Precursor;
GN   Name=PDE6A {ECO:0000250|UniProtKB:P16499}; Synonyms=PDEA;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=8726673; DOI=10.1159/000267869;
RA   Kommonen B., Kylma T., Cohen R.J., Penn J.S., Paulin L., Hurwitz M.,
RA   Hurwitz R.L.;
RT   "Elevation of cGMP with normal expression and activity of rod cGMP-PDE in
RT   photoreceptor degenerate labrador retrievers.";
RL   Ophthalmic Res. 28:19-28(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9233984;
RA   Wang W., Acland G.M., Aguirre G.D., Ray K.;
RT   "Cloning and characterization of the cDNA encoding the alpha-subunit of
RT   cGMP-phosphodiesterase in canine retinal rod photoreceptor cells.";
RL   Mol. Vis. 2:3-3(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle X Briard; TISSUE=Retina;
RA   Veske A., Nilsson S.E.G., Gal A.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the
CC       hydrolysis of 3',5'-cyclic GMP. This protein participates in processes
CC       of transmission and amplification of the visual signal.
CC       {ECO:0000250|UniProtKB:P16499}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; EC=3.1.4.35;
CC         Evidence={ECO:0000250|UniProtKB:P16499};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000250|UniProtKB:P16499};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
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:0000250};
CC   -!- SUBUNIT: Oligomer composed of two catalytic chains (alpha and beta), an
CC       inhibitory chain (gamma) and the delta chain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16499};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P16499}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P16499}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:P16499}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000305}.
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DR   EMBL; Z68340; CAA92763.1; -; mRNA.
DR   EMBL; U52868; AAB70037.1; -; mRNA.
DR   EMBL; Y13282; CAA73731.1; -; mRNA.
DR   RefSeq; NP_001003073.1; NM_001003073.1.
DR   AlphaFoldDB; Q28263; -.
DR   SMR; Q28263; -.
DR   STRING; 9615.ENSCAFP00000026963; -.
DR   BindingDB; Q28263; -.
DR   ChEMBL; CHEMBL5151; -.
DR   PaxDb; 9612-ENSCAFP00000026963; -.
DR   Ensembl; ENSCAFT00000028993.4; ENSCAFP00000026963.3; ENSCAFG00000018251.5.
DR   Ensembl; ENSCAFT00040021065.1; ENSCAFP00040018290.1; ENSCAFG00040011047.1.
DR   Ensembl; ENSCAFT00805003223; ENSCAFP00805002496; ENSCAFG00805001725.
DR   Ensembl; ENSCAFT00845015823.1; ENSCAFP00845012309.1; ENSCAFG00845008935.1.
DR   GeneID; 403620; -.
DR   KEGG; cfa:403620; -.
DR   CTD; 5145; -.
DR   VEuPathDB; HostDB:ENSCAFG00845008935; -.
DR   VGNC; VGNC:44357; PDE6A.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000161330; -.
DR   InParanoid; Q28263; -.
DR   OrthoDB; 5479253at2759; -.
DR   Reactome; R-CFA-2485179; Activation of the phototransduction cascade.
DR   Reactome; R-CFA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   Reactome; R-CFA-4086398; Ca2+ pathway.
DR   PRO; PR:Q28263; -.
DR   Proteomes; UP000002254; Chromosome 4.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Chromosome 4.
DR   Proteomes; UP000805418; Chromosome 4.
DR   Bgee; ENSCAFG00000018251; Expressed in large intestine and 8 other cell types or tissues.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IBA:GO_Central.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cell projection; cGMP; Hydrolase; Lipoprotein;
KW   Membrane; Metal-binding; Methylation; Prenylation; Reference proteome;
KW   Repeat; Sensory transduction; Vision.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11541"
FT   CHAIN           2..858
FT                   /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT                   subunit alpha"
FT                   /id="PRO_0000198827"
FT   PROPEP          859..861
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396696"
FT   DOMAIN          73..222
FT                   /note="GAF 1"
FT   DOMAIN          254..431
FT                   /note="GAF 2"
FT   DOMAIN          483..816
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          821..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        559
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         563
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         599
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         600
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         600
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         720
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P11541"
FT   MOD_RES         858
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           858
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        388
FT                   /note="M -> L (in Ref. 2; AAB70037)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   861 AA;  99688 MW;  8F7DD6C2A891B4E7 CRC64;
     MGEVTAEQVE KFLDSNIIFA KQYYNLRYRA KVISDMLGAK EAAVDFSNYH SLSSVEESEI
     IFDLLRDFQE NLQAERCIFN VMKKLCFLLQ ADRMSLFMYR VRNGIAELAT RLFNVHKDAV
     LEECLVAPDS EIVFPLDMGV VGHVAHSKKI ANVVNTEEDE HFCDFVDTLT EYQTKNILAS
     PIMNGKDVVA VIMAVNKVDE PHFTKRDEEI LLKYLNFANL IMKVYHLSYL HNCETRRGQI
     LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
     PYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV AQNGLICNIM
     NAPAEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDEMDETLM
     ESLAQFLGWS VLNPDTYESM NRLENRKDIF QDMVKYHVKC DNEEIQKILK TREVYGKEPW
     ECEEEELAEI LQGELPDAEK YEINKFHFSD LPLTELELVK CGIQMYYELK VVDKFHIPQE
     ALVRFMYSLS KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD
     IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH
     MMDIAIIATD LALYFKKRTM FQKIVDQSKT YETQQEWTQY MMLEQTRKEI VMAMMMTACD
     LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV
     CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYDTKM KALEEEKQKQ QTAKQGAAGD
     QPGGNPSPAG GAPASKSCCI Q
//