PDE6A_MOUSE
ID PDE6A_MOUSE Reviewed; 859 AA.
AC P27664; E9Q673;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha {ECO:0000305};
DE Short=GMP-PDE alpha;
DE EC=3.1.4.35 {ECO:0000250|UniProtKB:P16499};
DE Flags: Precursor;
GN Name=Pde6a {ECO:0000312|MGI:MGI:97524}; Synonyms=Mpa, Pdea;
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].
RC TISSUE=Retina;
RX PubMed=1847109; DOI=10.1016/0014-5793(91)80095-k;
RA Baehr W., Champagne M.S., Lee A.K., Pittler S.J.;
RT "Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase
RT alpha- and beta-subunits, and identification of beta'-, a putative beta-
RT subunit isozyme produced by alternative splicing of the beta-subunit
RT gene.";
RL FEBS Lett. 278:107-114(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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; X60664; CAA43072.1; -; mRNA.
DR EMBL; AC121903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC148012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S13030; S13030.
DR AlphaFoldDB; P27664; -.
DR SMR; P27664; -.
DR IntAct; P27664; 1.
DR STRING; 10090.ENSMUSP00000025468; -.
DR iPTMnet; P27664; -.
DR PhosphoSitePlus; P27664; -.
DR MaxQB; P27664; -.
DR PaxDb; P27664; -.
DR PRIDE; P27664; -.
DR ProteomicsDB; 288015; -.
DR MGI; MGI:97524; Pde6a.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P27664; -.
DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR ChiTaRS; Pde6a; mouse.
DR PRO; PR:P27664; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P27664; protein.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
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..856
FT /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit alpha"
FT /id="PRO_0000198829"
FT PROPEP 857..859
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396698"
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 823..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..848
FT /note="Polar residues"
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 856
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 856
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 26
FT /note="F -> L (in Ref. 1; CAA43072)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="M -> V (in Ref. 1; CAA43072)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="T -> P (in Ref. 1; CAA43072)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="G -> R (in Ref. 1; CAA43072)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="V -> W (in Ref. 1; CAA43072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 99530 MW; E51B8563A1A93526 CRC64;
MGEVTAEEVE KFLDSNIGFA KQYYNFHYRG KVISDLLGAK EAAVDFSNYH DVNSVEESEI
IFDLLRDVQE NLQAEKCTFN VMKKLCFLLR ADRMSLFMYR TRNGIAELAT RLFNVHKDAV
LEDCLVMPDS EIVFPLDMGV VGHVAHSKKI ANVPNTEEDE HFCDFVDNLT EYQTKNILAS
PIMNGKDVVA IIMAVNKIDE PHFTKRDEEI LLKYLNFVNL IMKVFHLSYL HNCETRRGQI
LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
AYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPADHW ALVSGLPTYV AQNGLICNIM
NAPAEDFFEF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDDMDETLM
ESLTQFLGWS VLNPDTYESM NKLENRKDIF QDIVKYHVKC DNEEIQKILK TREVYGKEPW
ECEEEELAEI LQGELPDAES YEINKFHFSD LPLTELELVK CGIQMYYELR VVDKFHIPQE
ALVRFMYSLS KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD
IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH
MMDIAIIATD LALYFKKRTM FQKIVDQSKT YESTQEWTQY MMLEQTRKEI VMAMMMTACD
LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYEAKM KALEEEKQKQ QAAKQAASGN
QPGGNPLQGA PASKSCCIQ
