PDE6A_BOVIN
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 03-AUG-2022, entry version 154.
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 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; P11541; -.
DR PRIDE; P11541; -.
DR GeneID; 281973; -.
DR KEGG; bta:281973; -.
DR CTD; 5145; -.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; P11541; -.
DR OrthoDB; 904682at2759; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 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
