ID   PDE6A_CANFA             Reviewed;         861 AA.
AC   Q28263; Q29470;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha;
DE            Short=GMP-PDE alpha;
DE            EC=3.1.4.35;
GN   Name=PDE6A; Synonyms=PDEA;
OS   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   MEDLINE=96331105; PubMed=8726673;
RA   Kommonen B., Kylma T., Cohen R.J., Penn J.S., Paulin L., Hurwitz M.,
RA   Hurwitz R.L.;
RT   "Elevation of cGMP with normal expression and activity of rod cGMP-PDE
RT   in photoreceptor degenerate labrador retrievers.";
RL   Ophthalmic Res. 28:19-28(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98099662; PubMed=9233984;
RA   Wang W., Acland G.M., Aguirre G.D., Ray K.;
RT   "Cloning and characterization of the cDNA encoding the alpha-subunit
RT   of cGMP-phosphodiesterase in canine retinal rod photoreceptor cells.";
RL   Mol. Vis. 2:3-3(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle X Briard; TISSUE=Retina;
RA   Veske A., Nilsson S.E.G., Gal A.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein participates in processes of transmission
CC       and amplification of the visual signal.
CC   -!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
CC       guanosine 5'-phosphate.
CC   -!- SUBUNIT: Oligomer composed of two catalytic chains (alpha and
CC       beta), an inhibitory chain (gamma) and the delta chain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family.
CC   -!- SIMILARITY: Contains 2 GAF domains.
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DR   EMBL; Z68340; CAA92763.1; -; mRNA.
DR   EMBL; U52868; AAB70037.1; -; mRNA.
DR   EMBL; Y13282; CAA73731.1; -; mRNA.
DR   RefSeq; NP_001003073.1; -.
DR   UniGene; Cfa.1198; -.
DR   HSSP; Q08499; 1OYN.
DR   Ensembl; ENSCAFG00000018251; Canis familiaris.
DR   GeneID; 403620; -.
DR   KEGG; cfa:403620; -.
DR   HOVERGEN; Q28263; -.
DR   BRENDA; 3.1.4.35; 463.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EC.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR003607; Met-dep_phosphohydro_HD.
DR   InterPro; IPR002073; PDEase.
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.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; cGMP; Hydrolase; Lipoprotein; Membrane;
KW   Prenylation; Repeat; Sensory transduction; Vision.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    861       Rod cGMP-specific 3',5'-cyclic
FT                                phosphodiesterase subunit alpha.
FT                                /FTId=PRO_0000198827.
FT   DOMAIN       73    222       GAF 1.
FT   DOMAIN      254    431       GAF 2.
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   LIPID       858    858       S-farnesyl cysteine (By similarity).
FT   CONFLICT    388    388       M -> L (in Ref. 2; AAB70037).
SQ   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
//