ID PDE6C_BOVIN Reviewed; 855 AA. AC P16586; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 08-NOV-2023, entry version 148. DE RecName: Full=Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'; DE EC=3.1.4.35 {ECO:0000250|UniProtKB:P51160}; DE AltName: Full=PDE V-C1; DE AltName: Full=cGMP phosphodiesterase 6C; DE Flags: Precursor; GN Name=PDE6C; Synonyms=PDEA2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2153291; DOI=10.1073/pnas.87.1.293; RA Li T., Volpp K., Applebury M.L.; RT "Bovine cone photoreceptor cGMP phosphodiesterase structure deduced from a RT cDNA clone."; RL Proc. Natl. Acad. Sci. U.S.A. 87:293-297(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 308-502, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=2153290; DOI=10.1073/pnas.87.1.288; RA Charbonneau H., Prusti R.K., Letrong H., Sonnenburg W.K., Mullaney P.J., RA Walsh K., Beavo J.A.; RT "Identification of a noncatalytic cGMP-binding domain conserved in both the RT cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterases."; RL Proc. Natl. Acad. Sci. U.S.A. 87:288-292(1990). CC -!- FUNCTION: As cone-specific cGMP phosphodiesterase, it plays an CC essential role in light detection and cone phototransduction by rapidly CC decreasing intracellular levels of cGMP. CC {ECO:0000250|UniProtKB:P51160}. 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:P51160}; 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: Composed of two alpha' subunits that are associated with 3 CC smaller proteins of 11, 13, and 15 kDa. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. 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; M37838; AAA30687.1; -; mRNA. DR EMBL; M33140; AAA30688.1; -; mRNA. DR PIR; A34810; A34810. DR RefSeq; NP_776844.1; NM_174419.1. DR PDB; 3JAB; EM; 11.00 A; C/O=563-726. DR PDB; 3JBQ; EM; 11.00 A; B/F=556-811. DR PDBsum; 3JAB; -. DR PDBsum; 3JBQ; -. DR AlphaFoldDB; P16586; -. DR SMR; P16586; -. DR STRING; 9913.ENSBTAP00000000569; -. DR BindingDB; P16586; -. DR ChEMBL; CHEMBL3479; -. DR DrugCentral; P16586; -. DR PaxDb; 9913-ENSBTAP00000000569; -. DR GeneID; 281975; -. DR KEGG; bta:281975; -. DR CTD; 5146; -. DR eggNOG; KOG3689; Eukaryota. DR InParanoid; P16586; -. DR OrthoDB; 5479253at2759; -. DR PRO; PR:P16586; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0030553; F:cGMP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; IBA:GO_Central. 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:SF23; CONE CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 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 1: Evidence at protein level; KW 3D-structure; Cell membrane; cGMP; cGMP-binding; Direct protein sequencing; KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Methylation; KW Nucleotide-binding; Prenylation; Reference proteome; Repeat; KW Sensory transduction; Vision. FT CHAIN 1..852 FT /note="Cone cGMP-specific 3',5'-cyclic phosphodiesterase FT subunit alpha'" FT /id="PRO_0000198830" FT PROPEP 853..855 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000370787" FT DOMAIN 70..219 FT /note="GAF 1" FT DOMAIN 251..428 FT /note="GAF 2" FT DOMAIN 481..814 FT /note="PDEase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192" FT REGION 823..855 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 823..846 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 557 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 92 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000250" FT BINDING 164..167 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000250" FT BINDING 171 FT /ligand="3',5'-cyclic GMP" FT /ligand_id="ChEBI:CHEBI:57746" FT /evidence="ECO:0000250" FT BINDING 561 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 597 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 598 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 598 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 718 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT MOD_RES 852 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000255" FT LIPID 852 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" SQ SEQUENCE 855 AA; 98798 MW; 1FCFFFD045686D65 CRC64; MGEISQETVE KYLEANPQFA KEYFNRKLQV EVPSGGAQAP ASASFPGRTL AEEAALYLEL LEVLLEEAGS VELAAHRALQ RLAQLLQADR CSMFLCRARN GTPEVASKLL DVTPTSKFED NLVVPDREAV FPLDVGIVGW VAHTKKTFNV PDVKKNSHFS DFMDKQTGYV TRNLLATPIV MGKEVLAVFM AVNKVDASEF SKQDEEVFSK YLSFVSIILK LHHTNYLYNI ESRRSQILMW SANKVFEELT DVERQFHKAL YTVRTYLNCE RYSIGLLDMT KEKEFYDEWP VKLGEVEPYK GPKTPDGREV IFYKIIDYIL HGKEEIKVIP TPPMDHWTLI SGLPTYVAEN GFICNMLNAP ADEYFTFQKG PVDETGWVIK NVLSLPIVNK KEDIVGVATF YNRKDGKPFD EYDEHIAETL TQFLGWSLLN TDTYEKMNKL ENRKDIAQEM LMNHTKATPD EIKSILKFKE KLNIDVIEDC EEKQLVTILK EDLPDPRTAD LYEFRFRHLP ITEHELIKCG LRLFFEINVV EKFKVPVEVL TRWMYTVRKG YRAVTYHNWR HGFNVGQTMF TLLMTGRLKK YYTDLEAFAM LAAAFCHDID HRGTNNLYQM KSTSPLARLH GSSILERHHL EYSKTLLQDE SLNIFQNLNK RQYETVIHLF EVAIIATDLA LYFKKRTMFQ KIVDACEKME TEEEAIKYVT IDPTKKEIIM AMMMTACDLS AITKPWEVQS QVALLVANEF WEQGDLERTV LQQQPIPMMD RNKKDELPKL QVGFIDFVCT FVYKEFSRFH KEITPMLNGL QNNRVEWKSL ADEYDEKMKV IEEMKKQEEG NTTEKAVEDS GGGGDDKKSK TCLML //