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Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (GMP-PDE alpha) (EC 3.1.4.35)

 PDE6A_CANLF             Reviewed;         861 AA.
Q28263; Q29470;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-DEC-2017, entry version 116.
RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha;
Short=GMP-PDE alpha;
EC=3.1.4.35;
Flags: Precursor;
Name=PDE6A; Synonyms=PDEA;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
PubMed=8726673; DOI=10.1159/000267869;
Kommonen B., Kylma T., Cohen R.J., Penn J.S., Paulin L., Hurwitz M.,
Hurwitz R.L.;
"Elevation of cGMP with normal expression and activity of rod cGMP-PDE
in photoreceptor degenerate labrador retrievers.";
Ophthalmic Res. 28:19-28(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9233984;
Wang W., Acland G.M., Aguirre G.D., Ray K.;
"Cloning and characterization of the cDNA encoding the alpha-subunit
of cGMP-phosphodiesterase in canine retinal rod photoreceptor cells.";
Mol. Vis. 2:3-3(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle X Briard; TISSUE=Retina;
Veske A., Nilsson S.E.G., Gal A.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: This protein participates in processes of transmission
and amplification of the visual signal.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=Binds 2 divalent metal cations per subunit. Site 1 may
preferentially bind zinc ions, while site 2 has a preference for
magnesium and/or manganese ions. {ECO:0000250};
-!- SUBUNIT: Oligomer composed of two catalytic chains (alpha and
beta), an inhibitory chain (gamma) and the delta chain.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
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EMBL; Z68340; CAA92763.1; -; mRNA.
EMBL; U52868; AAB70037.1; -; mRNA.
EMBL; Y13282; CAA73731.1; -; mRNA.
RefSeq; NP_001003073.1; NM_001003073.1.
UniGene; Cfa.1198; -.
ProteinModelPortal; Q28263; -.
SMR; Q28263; -.
STRING; 9615.ENSCAFP00000026963; -.
BindingDB; Q28263; -.
ChEMBL; CHEMBL5151; -.
PaxDb; Q28263; -.
GeneID; 403620; -.
KEGG; cfa:403620; -.
CTD; 5145; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
HOGENOM; HOG000007069; -.
HOVERGEN; HBG053539; -.
InParanoid; Q28263; -.
KO; K08718; -.
PRO; PR:Q28263; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR032958; PDE6A.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
PANTHER; PTHR11347:SF115; PTHR11347:SF115; 1.
Pfam; PF01590; GAF; 2.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 3.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
2: Evidence at transcript level;
Acetylation; Cell membrane; cGMP; Complete proteome; Hydrolase;
Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
Reference proteome; Repeat; Sensory transduction; Vision.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P11541}.
CHAIN 2 858 Rod cGMP-specific 3',5'-cyclic
phosphodiesterase subunit alpha.
/FTId=PRO_0000198827.
PROPEP 859 861 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000396696.
DOMAIN 73 222 GAF 1.
DOMAIN 254 431 GAF 2.
DOMAIN 483 816 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
ACT_SITE 559 559 Proton donor. {ECO:0000250}.
METAL 563 563 Divalent metal cation 1. {ECO:0000250}.
METAL 599 599 Divalent metal cation 1. {ECO:0000250}.
METAL 600 600 Divalent metal cation 1. {ECO:0000250}.
METAL 600 600 Divalent metal cation 2. {ECO:0000250}.
METAL 720 720 Divalent metal cation 1. {ECO:0000250}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:P11541}.
MOD_RES 858 858 Cysteine methyl ester. {ECO:0000250}.
LIPID 858 858 S-farnesyl cysteine. {ECO:0000250}.
CONFLICT 388 388 M -> L (in Ref. 2; AAB70037).
{ECO:0000305}.
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


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