ID   PDE6A_BOVIN             Reviewed;         859 AA.
AC   P11541;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha {ECO:0000250|UniProtKB:P16499};
DE            Short=GMP-PDE alpha;
DE            EC=3.1.4.35 {ECO:0000250|UniProtKB:P16499};
DE   AltName: Full=PDE V-B1;
DE   Flags: Precursor;
GN   Name=PDE6A {ECO:0000250|UniProtKB:P16499}; Synonyms=PDEA;
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=2155175; DOI=10.1016/0888-7543(90)90567-e;
RA   Pittler S.J., Baehr W., Wasmuth J.J., McConnell D.G., Champagne M.S.,
RA   VanTuinen P., Ledbetter D., Davis R.L.;
RT   "Molecular characterization of human and bovine rod photoreceptor cGMP
RT   phosphodiesterase alpha-subunit and chromosomal localization of the human
RT   gene.";
RL   Genomics 6:272-283(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2826095;
RA   Yu A., Ovchinnikov A., Gubanov V.V., Khramtsov N.V., Akhmedov N.B.,
RA   Ishchenko K.A., Zagranichnyi V.E., Vasilevskaya I.A., Rakitina T.V.,
RA   Atabekova N.V., Barinov A.A., Muradov K.G., Shuvaeva T.M., Bystrov N.S.,
RA   Severtsova I.V., Lipkin V.M.;
RT   "Cyclic GMP phosphodiesterase from the bovine retina. Amino acid sequence
RT   of the alpha-subunit and nucleotide sequence of corresponding cDNA.";
RL   Dokl. Akad. Nauk SSSR 296:487-491(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT
RP   GLY-2.
RC   TISSUE=Retina;
RX   PubMed=2822478; DOI=10.1016/0014-5793(87)80530-6;
RA   Ovchinnikov Y.A., Gubanov V.V., Khramtsov N.V., Ischenko K.A.,
RA   Zagranichny V.E., Muradov K.G., Shuvaeva T.M., Lipkin V.M.;
RT   "Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of
RT   the alpha-subunit and nucleotide sequence of the corresponding cDNA.";
RL   FEBS Lett. 223:169-173(1987).
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; X12756; CAA31243.1; -; mRNA.
DR   EMBL; M27541; AAA30441.1; -; mRNA.
DR   EMBL; M36683; AAA30442.1; -; mRNA.
DR   EMBL; M26043; AAA30443.1; -; mRNA.
DR   PIR; S06418; S06418.
DR   RefSeq; NP_001001526.2; NM_001001526.2.
DR   PDB; 6MZB; EM; 3.40 A; A=1-859.
DR   PDB; 7JSN; EM; 3.20 A; A=1-859.
DR   PDBsum; 6MZB; -.
DR   PDBsum; 7JSN; -.
DR   AlphaFoldDB; P11541; -.
DR   EMDB; EMD-22458; -.
DR   EMDB; EMD-9297; -.
DR   SMR; P11541; -.
DR   IntAct; P11541; 2.
DR   MINT; P11541; -.
DR   STRING; 9913.ENSBTAP00000036518; -.
DR   BindingDB; P11541; -.
DR   ChEMBL; CHEMBL3741; -.
DR   DrugCentral; P11541; -.
DR   iPTMnet; P11541; -.
DR   PaxDb; 9913-ENSBTAP00000036518; -.
DR   GeneID; 281973; -.
DR   KEGG; bta:281973; -.
DR   CTD; 5145; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   InParanoid; P11541; -.
DR   OrthoDB; 5479253at2759; -.
DR   PRO; PR:P11541; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
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:0060041; P:retina development in camera-type eye; IBA:GO_Central.
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; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF115; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT ALPHA; 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   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cell projection; cGMP;
KW   Direct protein sequencing; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Methylation; Prenylation; Reference proteome; Repeat; Sensory transduction;
KW   Vision.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2822478"
FT   CHAIN           2..856
FT                   /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT                   subunit alpha"
FT                   /id="PRO_0000198826"
FT   PROPEP          857..859
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396695"
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          821..859
FT                   /note="Disordered"
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:0000269|PubMed:2822478"
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   VARIANT         381
FT                   /note="M -> V"
FT   CONFLICT        194
FT                   /note="V -> A (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424
FT                   /note="T -> A (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675
FT                   /note="F -> C (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           22..27
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           29..36
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6MZB"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           76..89
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          92..102
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:6MZB"
FT   HELIX           139..147
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          151..154
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          177..195
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           205..214
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           216..248
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           255..262
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            265..269
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          272..279
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           288..295
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          330..334
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            340..344
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           347..353
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          356..360
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           362..364
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          385..391
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          397..406
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           414..429
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           432..457
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          462..465
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            466..468
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           471..474
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           479..481
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           487..492
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            498..504
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          511..513
FT                   /evidence="ECO:0007829|PDB:6MZB"
FT   HELIX           515..528
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           532..535
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           539..552
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          557..560
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           561..576
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           581..583
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           586..596
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            598..600
FT                   /evidence="ECO:0007829|PDB:6MZB"
FT   HELIX           608..613
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           618..621
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          623..625
FT                   /evidence="ECO:0007829|PDB:6MZB"
FT   HELIX           626..639
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           652..666
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           671..673
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   STRAND          675..678
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           679..687
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            688..690
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           698..702
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           706..720
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           722..725
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           728..751
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   TURN            759..761
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           763..768
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           769..779
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           783..791
FT                   /evidence="ECO:0007829|PDB:7JSN"
FT   HELIX           796..826
FT                   /evidence="ECO:0007829|PDB:7JSN"
SQ   SEQUENCE   859 AA;  99341 MW;  701CB148F73A1303 CRC64;
     MGEVTAEEVE KFLDSNVSFA KQYYNLRYRA KVISDLLGPR EAAVDFSNYH ALNSVEESEI
     IFDLLRDFQD NLQAEKCVFN VMKKLCFLLQ ADRMSLFMYR ARNGIAELAT RLFNVHKDAV
     LEECLVAPDS EIVFPLDMGV VGHVALSKKI VNVPNTEEDE HFCDFVDTLT EYQTKNILAS
     PIMNGKDVVA IIMVVNKVDG PHFTENDEEI LLKYLNFANL IMKVFHLSYL HNCETRRGQI
     LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
     PYAGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV AQNGLICNIM
     NAPSEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDEMDETLM
     ESLTQFLGWS VLNPDTYELM NKLENRKDIF QDMVKYHVKC DNEEIQTILK TREVYGKEPW
     ECEEEELAEI LQGELPDADK YEINKFHFSD LPLTELELVK CGIQMYYELK VVDKFHIPQE
     ALVRFMYSLS KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD
     IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH
     MMDIAIIATD LALYFKKRTM FQKIVDQSKT YETQQEWTQY MMLDQTRKEI VMAMMMTACD
     LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV
     CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYETKM KGLEEEKQKQ QAANQAAAGS
     QHGGKQPGGG PASKSCCVQ
//