PDE6C_BOVIN
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 03-AUG-2022, entry version 143.
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}.
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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; P16586; -.
DR PRIDE; P16586; -.
DR GeneID; 281975; -.
DR KEGG; bta:281975; -.
DR CTD; 5146; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P16586; -.
DR OrthoDB; 904682at2759; -.
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; 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; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
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 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
