PDE6C_MOUSE
ID PDE6C_MOUSE Reviewed; 861 AA.
AC Q91ZQ1; Q8R0D4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=cGMP phosphodiesterase 6C;
DE Flags: Precursor;
GN Name=Pde6c;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RA Chang B., Hawes N.L., Hurd R.E., Davisson M.T., Nusinowitz S.,
RA Heckenlively J.R.;
RT "A sequence alteration in Pde6c gene causes cone photoreceptor function
RT loss (cpfl1) in mice.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZQ1-2; Sequence=VSP_017422;
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; AF411063; AAK96254.1; -; mRNA.
DR EMBL; BC027050; AAH27050.1; -; mRNA.
DR CCDS; CCDS37971.1; -. [Q91ZQ1-1]
DR CCDS; CCDS50431.1; -. [Q91ZQ1-2]
DR RefSeq; NP_001164430.1; NM_001170959.1. [Q91ZQ1-2]
DR RefSeq; NP_291092.1; NM_033614.2. [Q91ZQ1-1]
DR AlphaFoldDB; Q91ZQ1; -.
DR SMR; Q91ZQ1; -.
DR BioGRID; 225961; 4.
DR STRING; 10090.ENSMUSP00000025956; -.
DR iPTMnet; Q91ZQ1; -.
DR PhosphoSitePlus; Q91ZQ1; -.
DR MaxQB; Q91ZQ1; -.
DR PaxDb; Q91ZQ1; -.
DR PRIDE; Q91ZQ1; -.
DR ProteomicsDB; 287989; -. [Q91ZQ1-1]
DR ProteomicsDB; 287990; -. [Q91ZQ1-2]
DR Antibodypedia; 30485; 121 antibodies from 21 providers.
DR DNASU; 110855; -.
DR Ensembl; ENSMUST00000025956; ENSMUSP00000025956; ENSMUSG00000024992. [Q91ZQ1-1]
DR Ensembl; ENSMUST00000112329; ENSMUSP00000107948; ENSMUSG00000024992. [Q91ZQ1-2]
DR GeneID; 110855; -.
DR KEGG; mmu:110855; -.
DR UCSC; uc008hjf.2; mouse. [Q91ZQ1-1]
DR UCSC; uc012blg.1; mouse. [Q91ZQ1-2]
DR CTD; 5146; -.
DR MGI; MGI:105956; Pde6c.
DR VEuPathDB; HostDB:ENSMUSG00000024992; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000157825; -.
DR HOGENOM; CLU_006980_2_0_1; -.
DR InParanoid; Q91ZQ1; -.
DR OMA; MYLNCER; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q91ZQ1; -.
DR TreeFam; TF316499; -.
DR BioGRID-ORCS; 110855; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pde6c; mouse.
DR PRO; PR:Q91ZQ1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91ZQ1; protein.
DR Bgee; ENSMUSG00000024992; Expressed in retinal neural layer and 25 other tissues.
DR Genevisible; Q91ZQ1; MM.
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:0007603; P:phototransduction, visible light; IMP:MGI.
DR GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; cGMP; cGMP-binding; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Methylation; Nucleotide-binding;
KW Prenylation; Reference proteome; Repeat; Sensory transduction; Vision.
FT CHAIN 1..858
FT /note="Cone cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit alpha'"
FT /id="PRO_0000226068"
FT PROPEP 859..861
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000370789"
FT DOMAIN 75..224
FT /note="GAF 1"
FT DOMAIN 256..433
FT /note="GAF 2"
FT DOMAIN 486..819
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 826..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 562
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 97
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 169..172
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 602
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 723
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 858
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000255"
FT LIPID 858
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 737..761
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017422"
SQ SEQUENCE 861 AA; 98785 MW; C582D78114652B5B CRC64;
MGEISQEAVE RYLEKNPCFA KEYFDKKLRV EALGVIFKNS HAGVQTGLSL PEMTQVEESA
VCLELLQCMQ DEAGSAEQMA HRALQRLAQL LQADCCSMFS CRARNGIPEV ASRLLNVTPT
SKFEDNLVAP DREVVFPLDI GIVGWVAHVK KALNVSDVKK NSHFSDFMDK QTGYVTRNLL
AVPIVAGKEV LAVVMAVNKI SAPEFSKQDE EVFSKYLSFV AVALRLQHTS YLYSVESRRS
QILMWSANKV FEELTDVERQ FHKALYTIRT YLNCDRYSIG LLDMTKEKEF YDEWPIKLGE
VEPYKGPKTP DGREIIFYKI IDYILHGKEE INVIPSPPAD HWTLVSGLPT YVAENGFICN
MLNAPADEYF TFQKGPVDET GWVIKNVLSL PIVNKKEDIV GVATFYNRKD GKPFDEHDEH
ITETLTQFLG WSLLNTDTYE RVNKLESRKD IAQEMVMNLT KATPDEISSI LKFKEKLNVE
VIEECEERQL LAILKEDLPD PRTADLYEFC FSDFPITEHE LVKCGLRLFL EINVVEKFKV
PVEVLTRWMY TVRKGYRPVT YHNWRHGFNV GQTMFTLLMT GRLKKYYTDL EAFAMLAAAF
CHDIDHRGTN NLYQMKSTSP LARLHGTSIL ERHHLEYSKT LLQDESLNIF QNLNKRQFET
VIHLFEVAII ATDLALYFKK RTMFQKIVDT CEQMQSEEET IKYVTSDPTK KEVIMAMMMT
ACDLSAITKP WEVQSQVALL VANEFWEQGD LERTVLQQQP IPMMDRSKKD ELPKLQVGFI
DFVCTFVYKE FSRFHGEITP MLNGLQNNRV EWKSLAEEYE AKVKVTEEEA GKQEEEASDG
KAATDLGGSA EDKKSKTCLM L
