PDE6B_CANLF
ID PDE6B_CANLF Reviewed; 856 AA.
AC P33726;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta {ECO:0000250|UniProtKB:P35913};
DE Short=GMP-PDE beta;
DE EC=3.1.4.35 {ECO:0000269|PubMed:8387203};
DE Flags: Precursor;
GN Name=PDE6B {ECO:0000250|UniProtKB:P35913}; Synonyms=PDBS, PDEB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=Red setter; TISSUE=Retina;
RX PubMed=8387203; DOI=10.1073/pnas.90.9.3968;
RA Suber M.L., Pittler S.J., Qin N., Wright G.C., Holcombe V., Lee R.H.,
RA Craft C.M., Lolley R.N., Baehr W.B., Hurwitz R.L.;
RT "Irish setter dogs affected with rod/cone dysplasia contain a nonsense
RT mutation in the rod cGMP phosphodiesterase beta-subunit gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3968-3972(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Boxer X Doberman; TISSUE=Retina;
RA Clements P.J.;
RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the
CC hydrolysis of 3',5'-cyclic GMP (PubMed:8387203). Necessary for the
CC formation of a functional phosphodiesterase holoenzyme (By similarity).
CC Involved in retinal circadian rhythm photoentrainment via modulation of
CC UVA and orange light-induced phase-shift of the retina clock (By
CC similarity). May participate in processes of transmission and
CC amplification of the visual signal (By similarity).
CC {ECO:0000250|UniProtKB:P23440, ECO:0000250|UniProtKB:P35913,
CC ECO:0000269|PubMed:8387203}.
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:0000269|PubMed:8387203};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:8387203};
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: Membrane {ECO:0000250|UniProtKB:P35913}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P35913}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P35913}.
CC -!- DISEASE: Note=Irish setter dogs affected with rod/cone dysplasia (RCD1)
CC contain a nonsense mutation in the gene that gives rise to a protein of
CC 807 AA lacking 49 AA in the C-terminal. {ECO:0000269|PubMed:8387203}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; Z23014; CAA80557.1; -; mRNA.
DR EMBL; L13262; AAA30882.1; ALT_SEQ; mRNA.
DR PIR; A47451; A47451.
DR RefSeq; NP_001002934.1; NM_001002934.1.
DR AlphaFoldDB; P33726; -.
DR SMR; P33726; -.
DR STRING; 9615.ENSCAFP00000024683; -.
DR PaxDb; P33726; -.
DR Ensembl; ENSCAFT00030038883; ENSCAFP00030033913; ENSCAFG00030021135.
DR Ensembl; ENSCAFT00040007999; ENSCAFP00040006969; ENSCAFG00040004174.
DR GeneID; 399653; -.
DR KEGG; cfa:399653; -.
DR CTD; 5158; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_006980_2_0_1; -.
DR InParanoid; P33726; -.
DR OMA; PGPTKFE; -.
DR OrthoDB; 904682at2759; -.
DR TreeFam; TF316499; -.
DR Reactome; R-CFA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-CFA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-CFA-4086398; Ca2+ pathway.
DR Proteomes; UP000002254; Unplaced.
DR Bgee; ENSCAFG00000016782; Expressed in testis and 11 other tissues.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IBA:GO_Central.
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:0009583; P:detection of light stimulus; IEA:Ensembl.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
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; 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; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
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 Acetylation; Cell projection; cGMP; Disease variant; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Prenylation; Reference proteome;
KW Repeat; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23439"
FT CHAIN 2..853
FT /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit beta"
FT /id="PRO_0000023346"
FT PROPEP 854..856
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023347"
FT DOMAIN 71..220
FT /note="GAF 1"
FT DOMAIN 252..429
FT /note="GAF 2"
FT DOMAIN 481..814
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 823..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 557
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 718
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-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P23439"
FT LIPID 853
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 856 AA; 98462 MW; AC9D03F64D1BA132 CRC64;
MSLSEEQVQH FLDQNPDFTD QYFGKTLSPE HVAGACGDGQ PTDCASFREL CQVEESAALF
ELVQDMQESV NMERVVFKIL RRLCTILRAD RCSLFMYRQR NGVAELATRL FSVQPGSALE
DCLVPPDSEI VFPLDIGVVG HVAQTKKMVN VQDVTECPHF SPFADELTGY ETRNILATPI
MNGKDVVAVI MALNKLDGPC FTSEDEDVFL KYLNFGTLNL KIYHLSYLHN CETRRGQVLL
WSANKVFEEL TDIERQFHKA FYTVRAYLNC DRYSVGLLDM TKEKEFFDVW PVLMGEAQPY
SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PSPPADHWAL ASGLPTYVAE SGFICNIMNT
AADEMFTFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DEQDEVLMES
LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQLILPTR ERLGKEPADC
EEDELGILLK EVLPGPSKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL
VRFLFSVSKG YRRITYHNWR HGFNVAQTMF TLLTTGKLKS YYTDLEAFAM VTAGLCHDID
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLSEE TLNIYQNLNR RQHEHVIHLM
DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DRKSWVEYLS LETTRKEIVM AMMMTACDLS
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT
FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKLKA LEEEKQQQED RTTAKKAGTE
ICNGGPAPKS STCCIL
