ID PDE6B_MOUSE Reviewed; 856 AA. AC P23440; Q80UF0; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 24-JAN-2024, entry version 185. DE RecName: Full=Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta {ECO:0000305}; DE Short=GMP-PDE beta; DE EC=3.1.4.35 {ECO:0000250|UniProtKB:P35913}; DE Flags: Precursor; GN Name=Pde6b {ECO:0000312|MGI:MGI:97525}; GN Synonyms=Mpb, Pdeb, rd {ECO:0000303|PubMed:1977087}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN RETINAL RP DEGENERATION. RC STRAIN=C57BL/6J; TISSUE=Retina; RX PubMed=1977087; DOI=10.1038/347677a0; RA Bowes C., Li T., Danciger M., Baxter L.C., Applebury M.L., Farber D.B.; RT "Retinal degeneration in the rd mouse is caused by a defect in the beta RT subunit of rod cGMP-phosphodiesterase."; RL Nature 347:677-680(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), RP AND FUNCTION. RC TISSUE=Retina; RX PubMed=1847109; DOI=10.1016/0014-5793(91)80095-k; RA Baehr W., Champagne M.S., Lee A.K., Pittler S.J.; RT "Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase RT alpha- and beta-subunits, and identification of beta'-, a putative beta- RT subunit isozyme produced by alternative splicing of the beta-subunit RT gene."; RL FEBS Lett. 278:107-114(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Retina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP INVOLVEMENT IN RETINAL DEGENERATION, AND VARIANT RETINAL DEGENERATION RP 347-TYR--LEU-856 DEL. RX PubMed=1656438; DOI=10.1073/pnas.88.19.8322; RA Pittler S.J., Baehr W.; RT "Identification of a nonsense mutation in the rod photoreceptor cGMP RT phosphodiesterase beta-subunit gene of the rd mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8322-8326(1991). RN [6] RP INVOLVEMENT IN RETINAL DEGENERATION. RX PubMed=25613321; DOI=10.1038/ncomms7006; RA Nishiguchi K.M., Carvalho L.S., Rizzi M., Powell K., Holthaus S.M., RA Azam S.A., Duran Y., Ribeiro J., Luhmann U.F., Bainbridge J.W., Smith A.J., RA Ali R.R.; RT "Gene therapy restores vision in rd1 mice after removal of a confounding RT mutation in Gpr179."; RL Nat. Commun. 6:6006-6006(2015). RN [7] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=30240620; DOI=10.1016/j.isci.2018.08.010; RA Ota W., Nakane Y., Hattar S., Yoshimura T.; RT "Impaired Circadian Photoentrainment in Opn5-Null Mice."; RL IScience 6:299-305(2018). CC -!- FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the CC hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the CC formation of a functional phosphodiesterase holoenzyme CC (PubMed:1847109). Involved in retinal circadian rhythm photoentrainment CC via modulation of UVA and orange light-induced phase-shift of the CC retina clock (PubMed:30240620). May participate in processes of CC transmission and amplification of the visual signal (By similarity). CC {ECO:0000250|UniProtKB:P35913, ECO:0000269|PubMed:1847109, CC ECO:0000269|PubMed:30240620}. 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:P35913}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; CC Evidence={ECO:0000250|UniProtKB:P35913}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:Q07343}; 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|UniProtKB:Q07343}; 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P23440-1; Sequence=Displayed; CC Name=2; Synonyms=Beta'; CC IsoId=P23440-2; Sequence=VSP_004592; CC -!- DISEASE: Note=Defects in Pde6b are the cause of the retinal CC degeneration (rd) allele, which is characterized by retinal CC degeneration (PubMed:1977087, PubMed:1656438). The retinal degeneration CC 1 (rd1) allele also contains a cofounding mutation in the Gpr179 gene CC (PubMed:25613321). {ECO:0000269|PubMed:1656438, CC ECO:0000269|PubMed:1977087, ECO:0000269|PubMed:25613321}. CC -!- DISRUPTION PHENOTYPE: Abolishes the retinal photoreceptor layer, outer CC nuclear layer, and outer plexiform layer in the retinal ultrastructure CC (PubMed:30240620). Loss of Opn1sw, Opn1mw and Rho expression in the CC retina (PubMed:30240620). Reduced rate of circadian photoentrainment, CC UVA and orange light-induced phase-shift response and Fos expression in CC the suprachiasmatic nuclei (SCN) in the brain (PubMed:30240620). Pde6b CC and Opn5 double knockout mice also show loss of retinal ultrastructures CC and a more severe reduction in the rate of circadian photoentrainment, CC light-induced phase-shift response and Fos expression in the SCN CC (PubMed:30240620). {ECO:0000269|PubMed:30240620}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X55968; CAA39439.1; -; mRNA. DR EMBL; X60133; CAA42719.1; -; mRNA. DR EMBL; AK044364; BAC31885.1; -; mRNA. DR EMBL; CH466529; EDL20122.1; -; Genomic_DNA. DR CCDS; CCDS19510.1; -. [P23440-1] DR PIR; S30762; S30762. DR RefSeq; NP_032832.2; NM_008806.2. [P23440-1] DR AlphaFoldDB; P23440; -. DR SMR; P23440; -. DR BioGRID; 202084; 21. DR STRING; 10090.ENSMUSP00000031456; -. DR iPTMnet; P23440; -. DR PhosphoSitePlus; P23440; -. DR MaxQB; P23440; -. DR PaxDb; 10090-ENSMUSP00000031456; -. DR ProteomicsDB; 288016; -. [P23440-1] DR ProteomicsDB; 288017; -. [P23440-2] DR Antibodypedia; 8018; 130 antibodies from 26 providers. DR DNASU; 18587; -. DR Ensembl; ENSMUST00000031456.8; ENSMUSP00000031456.8; ENSMUSG00000029491.8. [P23440-1] DR GeneID; 18587; -. DR KEGG; mmu:18587; -. DR UCSC; uc008ynz.1; mouse. [P23440-1] DR AGR; MGI:97525; -. DR CTD; 5158; -. DR MGI; MGI:97525; Pde6b. DR VEuPathDB; HostDB:ENSMUSG00000029491; -. DR eggNOG; KOG3689; Eukaryota. DR GeneTree; ENSGT00940000156471; -. DR HOGENOM; CLU_006980_2_0_1; -. DR InParanoid; P23440; -. DR OMA; REVYDCE; -. DR OrthoDB; 5479253at2759; -. DR PhylomeDB; P23440; -. DR TreeFam; TF316499; -. DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade. DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR Reactome; R-MMU-4086398; Ca2+ pathway. DR BioGRID-ORCS; 18587; 3 hits in 76 CRISPR screens. DR ChiTaRS; Pde6b; mouse. DR PRO; PR:P23440; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P23440; Protein. DR Bgee; ENSMUSG00000029491; Expressed in retinal neural layer and 23 other cell types or tissues. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. 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; IMP:MGI. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB. DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI. DR GO; GO:1990009; P:retinal cell apoptotic process; ISO:MGI. 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:SF73; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT BETA; 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. DR Genevisible; P23440; MM. PE 2: Evidence at transcript level; KW Acetylation; Alternative splicing; Cell projection; cGMP; Hydrolase; KW Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding; Prenylation; KW Reference proteome; Repeat; Sensory transduction; Vision; Zinc. 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_0000023350" FT PROPEP 854..856 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000023351" 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 ACT_SITE 557 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q07343" FT BINDING 561 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q07343" FT BINDING 597 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q07343" FT BINDING 598 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q07343" FT BINDING 598 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q07343" FT BINDING 718 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q07343" 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" FT VAR_SEQ 801..856 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_004592" FT VARIANT 347..856 FT /note="Missing (in Rd mouse, causes retinal degeneration)" FT /evidence="ECO:0000269|PubMed:1656438" FT CONFLICT 5 FT /note="E -> G (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 19 FT /note="A -> S (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 49..50 FT /note="EL -> DV (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 158 FT /note="P -> T (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 176 FT /note="L -> C (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="E -> R (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="G -> S (in Ref. 1; CAA39439)" FT /evidence="ECO:0000305" SQ SEQUENCE 856 AA; 98535 MW; 209F3A936DD16D46 CRC64; MSLSEEQVRS FLDGNPTFAH QYFGKKLSPE NVAGACEDGW LADCGSLREL CQVEESAALF ELVQDMQESV NMERVVFKIL RRLCTILHAD RCSLFMYRQR NGIAELATRL FSVQPDSLLE DCLVPPDSEI VFPLDIGIVG HVAQTKKMIN VQDVAECPHF SSFADELTDY VTKNILSTPI MNGKDVVAVI MAVNKLDGPC FTSEDEDVFT KYLNFATLNL KIYHLSYLHN CETRRGQVLL WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW PVLMGEAQPY SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PTPPADHWAL ASGLPTYVAE SGFICNIMNA SADEMFNFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DDQDEVLMES LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQEILPTR DRLGKEPADC EEDELGKILK EELPGPTKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL VRFLFSVSKA YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLAEE SLNIYQNLNR RQHEHVIHLM DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DKKSWVEYLS LETTRKEIVM AMMMTACDLS AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEEKKKEED RVAAKKVGTE VCNGGPAPKS STCCIL //