PDE6A_CANLF
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 03-AUG-2022, entry version 133.
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}.
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; 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; 9612.ENSCAFP00000026963; -.
DR BindingDB; Q28263; -.
DR ChEMBL; CHEMBL5151; -.
DR PaxDb; Q28263; -.
DR Ensembl; ENSCAFT00040021065; ENSCAFP00040018290; ENSCAFG00040011047.
DR Ensembl; ENSCAFT00845015823; ENSCAFP00845012309; ENSCAFG00845008935.
DR GeneID; 403620; -.
DR KEGG; cfa:403620; -.
DR CTD; 5145; -.
DR VEuPathDB; HostDB:ENSCAFG00845008935; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000161330; -.
DR InParanoid; Q28263; -.
DR OrthoDB; 904682at2759; -.
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 Bgee; ENSCAFG00000018251; Expressed in large intestine and 8 other 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; 1.10.1300.10; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR032958; PDE6A.
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:SF115; PTHR11347:SF115; 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 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
