PDE6B_HUMAN
ID PDE6B_HUMAN Reviewed; 854 AA.
AC P35913; B7Z9T9; E7ETT3; Q53XN5; Q9BWH5; Q9UD49;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 211.
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:0000269|PubMed:20940301};
DE Flags: Precursor;
GN Name=PDE6B {ECO:0000312|HGNC:HGNC:8786}; Synonyms=PDEB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1720239; DOI=10.1093/nar/19.22.6263;
RA Weber B., Riess O., Hutchinson G., Collins C., Lin B., Kowbel D.,
RA Andrew S., Schappert K.T., Hayden M.R.;
RT "Genomic organization and complete sequence of the human gene encoding the
RT beta-subunit of the cGMP phosphodiesterase and its localisation to
RT 4p16.3.";
RL Nucleic Acids Res. 19:6263-6268(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-320.
RC TISSUE=Retinal rod cell;
RX PubMed=1338685;
RA Khramtsov N.V., Feshchenko E.A., Suslova V.A., Terpugov B.E.,
RA Rakitina T.V., Atabekova N.V., Shmukler B.E., Lipkin V.M.;
RT "Structural studies of cDNA and the gene for the beta-subunit of cGMP
RT phosphodiesterase from human retina.";
RL Bioorg. Khim. 18:1551-1554(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-320.
RC TISSUE=Retina;
RX PubMed=1322354; DOI=10.1016/0888-7543(92)90144-h;
RA Collins C., Hutchinson G., Kowbel D., Riess O., Weber B., Hayden M.R.;
RT "The human beta-subunit of rod photoreceptor cGMP phosphodiesterase:
RT complete retinal cDNA sequence and evidence for expression in brain.";
RL Genomics 13:698-704(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=8394243; DOI=10.1016/0014-5793(93)81003-i;
RA Khramtsov N.V., Feshchenko E.A., Suslova V.A., Shmukler B.E.,
RA Terpugov B.E., Rakitina T.V., Atabekova N.V., Lipkin V.M.;
RT "The human rod photoreceptor cGMP phosphodiesterase beta-subunit.
RT Structural studies of its cDNA and gene.";
RL FEBS Lett. 327:275-278(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ILE-320
RP AND ASP-654.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ILE-320.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ILE-320
RP AND ASP-654.
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 197-297, AND VARIANT CSNBAD2 ASN-258.
RX PubMed=8075643; DOI=10.1038/ng0594-64;
RA Gal A., Orth U., Baehr W., Schwinger E., Rosenberg T.;
RT "Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-
RT subunit gene in autosomal dominant stationary night blindness.";
RL Nat. Genet. 7:64-68(1994).
RN [10]
RP ERRATUM OF PUBMED:8075643.
RX PubMed=7951329; DOI=10.1038/ng0894-551a;
RA Gal A., Orth U., Baehr W., Schwinger E., Rosenberg T.;
RL Nat. Genet. 7:551-551(1994).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 238-854, AND VARIANT ILE-320.
RC TISSUE=Retinal rod cell;
RX PubMed=8768262;
RA Suslova V.A., Suslov O.N., Kim E.E., Lipkin V.M.;
RT "Organization of the gene for the beta-subunit of human photoreceptor
RT cyclic GMP phosphodiesterase.";
RL Bioorg. Khim. 22:256-263(1996).
RN [12]
RP FUNCTION, AND VARIANT RP40 TYR-557.
RX PubMed=8394174; DOI=10.1038/ng0693-130;
RA McLaughlin M.E., Sandberg M.A., Berson E.L., Dryja T.P.;
RT "Recessive mutations in the gene encoding the beta-subunit of rod
RT phosphodiesterase in patients with retinitis pigmentosa.";
RL Nat. Genet. 4:130-134(1993).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20940301; DOI=10.1074/jbc.m110.170068;
RA Muradov H., Boyd K.K., Artemyev N.O.;
RT "Rod phosphodiesterase-6 PDE6A and PDE6B subunits are enzymatically
RT equivalent.";
RL J. Biol. Chem. 285:39828-39834(2010).
RN [14]
RP VARIANT RP40 ASP-576.
RX PubMed=8595886; DOI=10.1006/geno.1995.0001;
RA Danciger M., Blaney J., Gao Y.Q., Zhao D.Y., Heckenlively J.R.,
RA Jacobson S.G., Farber D.B.;
RT "Mutations in the PDE6B gene in autosomal recessive retinitis pigmentosa.";
RL Genomics 30:1-7(1995).
RN [15]
RP VARIANT RP40 HIS-228, AND VARIANTS LYS-166 AND HIS-212.
RX PubMed=8698075; DOI=10.1006/exer.1996.0019;
RA Gao Y.Q., Danciger M., Zhao D.Y., Blaney J., Piriev N.I., Shih J.,
RA Jacobson S.G., Heckenlively J.H., Farber D.B.;
RT "Screening of the PDE6B gene in patients with autosomal dominant retinitis
RT pigmentosa.";
RL Exp. Eye Res. 62:149-154(1996).
RN [16]
RP VARIANT RP40 ARG-699.
RX PubMed=8557257; DOI=10.1007/bf00218829;
RA Valverde D., Solans T., Grinberg D., Balcells S., Vilageliu L., Bayes M.,
RA Chivelet P., Besmond C., Goossens M., Gonzalez-Duarte R., Baiget M.;
RT "A novel mutation in exon 17 of the beta-subunit of rod phosphodiesterase
RT in two RP sisters of a consanguineous family.";
RL Hum. Genet. 97:35-38(1996).
RN [17]
RP VARIANT RP40 GLN-552.
RX PubMed=8956055; DOI=10.1002/humu.1380080403;
RA Valverde D., Baiget M., Seminago R., del Rio E., Garcia-Sandoval B.,
RA del Rio T., Bayes M., Balcells S., Martinez A., Grinberg D., Ayuso C.;
RT "Identification of a novel R552Q mutation in exon 13 of the beta-subunit of
RT rod phosphodiesterase gene in a Spanish family with autosomal recessive
RT retinitis pigmentosa.";
RL Hum. Mutat. 8:393-394(1996).
RN [18]
RP VARIANT RP40 ASN-535.
RX PubMed=9543643; DOI=10.1076/ceyr.17.3.332.5214;
RA Saga M., Mashima Y., Akeo K., Kudoh J., Oguchi Y., Shimizu N.;
RT "A novel homozygous Ile535Asn mutation in the rod cGMP phosphodiesterase
RT beta-subunit gene in two brothers of a Japanese family with autosomal
RT recessive retinitis pigmentosa.";
RL Curr. Eye Res. 17:332-335(1998).
RN [19]
RP VARIANTS RP40 HIS-100 AND ASN-776.
RX PubMed=22334370; DOI=10.1002/humu.22045;
RA Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L.,
RA Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J.,
RA Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E.,
RA den Hollander A.I., Hoischen A., Hoyng C., Klevering B.J.,
RA van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.;
RT "Next-generation genetic testing for retinitis pigmentosa.";
RL Hum. Mutat. 33:963-972(2012).
CC -!- FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the
CC hydrolysis of 3',5'-cyclic GMP (PubMed:20940301). 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 (PubMed:8394174).
CC {ECO:0000250|UniProtKB:P23440, ECO:0000269|PubMed:20940301,
CC ECO:0000269|PubMed:8394174}.
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:20940301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC Evidence={ECO:0000305|PubMed:20940301};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22 uM for 3',5'-cyclic GMP (with the chimera containing the N-
CC terminal regulatory GAF domains of PDE6C and the C-terminal catalytic
CC domain of PDE6B) {ECO:0000269|PubMed:20940301};
CC -!- SUBUNIT: Oligomer composed of two catalytic chains (alpha and beta), an
CC inhibitory chain (gamma) and the delta chain.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000269|PubMed:20940301}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P35913-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35913-2; Sequence=VSP_036884;
CC Name=3;
CC IsoId=P35913-3; Sequence=VSP_044919;
CC -!- DISEASE: Retinitis pigmentosa 40 (RP40) [MIM:613801]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:22334370,
CC ECO:0000269|PubMed:8394174, ECO:0000269|PubMed:8557257,
CC ECO:0000269|PubMed:8595886, ECO:0000269|PubMed:8698075,
CC ECO:0000269|PubMed:8956055, ECO:0000269|PubMed:9543643}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Night blindness, congenital stationary, autosomal dominant 2
CC (CSNBAD2) [MIM:163500]: A non-progressive retinal disorder
CC characterized by impaired night vision, often associated with nystagmus
CC and myopia. {ECO:0000269|PubMed:8075643}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the PDE6A/B/G genes; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/pdemut.htm";
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DR EMBL; X62692; CAA44569.1; -; Genomic_DNA.
DR EMBL; X62693; CAA44569.1; JOINED; Genomic_DNA.
DR EMBL; X62694; CAA44569.1; JOINED; Genomic_DNA.
DR EMBL; X62695; CAA44569.1; JOINED; Genomic_DNA.
DR EMBL; X66142; CAA46932.1; -; mRNA.
DR EMBL; S41458; AAB22690.1; -; mRNA.
DR EMBL; BT009794; AAP88796.1; -; mRNA.
DR EMBL; AK316054; BAH14425.1; -; mRNA.
DR EMBL; AC107464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000249; AAH00249.1; -; mRNA.
DR EMBL; X90587; CAA62215.1; -; Genomic_DNA.
DR EMBL; X90588; CAA62215.1; JOINED; Genomic_DNA.
DR EMBL; X90589; CAA62215.1; JOINED; Genomic_DNA.
DR EMBL; X90590; CAA62215.1; JOINED; Genomic_DNA.
DR CCDS; CCDS33932.1; -. [P35913-1]
DR CCDS; CCDS46993.1; -. [P35913-3]
DR CCDS; CCDS54703.1; -. [P35913-2]
DR PIR; A42828; A42828.
DR RefSeq; NP_000274.2; NM_000283.3. [P35913-1]
DR RefSeq; NP_001138763.1; NM_001145291.1. [P35913-2]
DR RefSeq; NP_001138764.1; NM_001145292.1. [P35913-3]
DR RefSeq; XP_016863774.1; XM_017008285.1.
DR RefSeq; XP_016863775.1; XM_017008286.1.
DR AlphaFoldDB; P35913; -.
DR SMR; P35913; -.
DR BioGRID; 111184; 23.
DR IntAct; P35913; 1.
DR STRING; 9606.ENSP00000420295; -.
DR BindingDB; P35913; -.
DR ChEMBL; CHEMBL3430880; -.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; P35913; -.
DR iPTMnet; P35913; -.
DR PhosphoSitePlus; P35913; -.
DR BioMuta; PDE6B; -.
DR DMDM; 226693550; -.
DR MassIVE; P35913; -.
DR PaxDb; P35913; -.
DR PeptideAtlas; P35913; -.
DR PRIDE; P35913; -.
DR ProteomicsDB; 18284; -.
DR ProteomicsDB; 55162; -. [P35913-1]
DR ProteomicsDB; 55163; -. [P35913-2]
DR Antibodypedia; 8018; 115 antibodies from 26 providers.
DR DNASU; 5158; -.
DR Ensembl; ENST00000255622.10; ENSP00000255622.6; ENSG00000133256.13. [P35913-2]
DR Ensembl; ENST00000429163.6; ENSP00000406334.2; ENSG00000133256.13. [P35913-3]
DR Ensembl; ENST00000496514.6; ENSP00000420295.1; ENSG00000133256.13. [P35913-1]
DR GeneID; 5158; -.
DR KEGG; hsa:5158; -.
DR MANE-Select; ENST00000496514.6; ENSP00000420295.1; NM_000283.4; NP_000274.3.
DR UCSC; uc003gao.5; human. [P35913-1]
DR CTD; 5158; -.
DR DisGeNET; 5158; -.
DR GeneCards; PDE6B; -.
DR GeneReviews; PDE6B; -.
DR HGNC; HGNC:8786; PDE6B.
DR HPA; ENSG00000133256; Tissue enriched (retina).
DR MalaCards; PDE6B; -.
DR MIM; 163500; phenotype.
DR MIM; 180072; gene.
DR MIM; 613801; phenotype.
DR neXtProt; NX_P35913; -.
DR OpenTargets; ENSG00000133256; -.
DR Orphanet; 215; Congenital stationary night blindness.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA33134; -.
DR VEuPathDB; HostDB:ENSG00000133256; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000156471; -.
DR HOGENOM; CLU_006980_2_0_1; -.
DR OMA; PGPTKFE; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; P35913; -.
DR TreeFam; TF316499; -.
DR PathwayCommons; P35913; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR SignaLink; P35913; -.
DR BioGRID-ORCS; 5158; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; PDE6B; human.
DR GeneWiki; PDE6B; -.
DR GenomeRNAi; 5158; -.
DR Pharos; P35913; Tclin.
DR PRO; PR:P35913; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P35913; protein.
DR Bgee; ENSG00000133256; Expressed in C1 segment of cervical spinal cord and 104 other tissues.
DR ExpressionAtlas; P35913; baseline and differential.
DR Genevisible; P35913; HS.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
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:0043153; P:entrainment of circadian clock by photoperiod; ISS:UniProtKB.
DR GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR GO; GO:1990009; P:retinal cell apoptotic process; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
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; Alternative splicing; Cell projection; cGMP;
KW Congenital stationary night blindness; Disease variant; Hydrolase;
KW Lipoprotein; Membrane; Metal-binding; Prenylation; Reference proteome;
KW Repeat; Retinitis pigmentosa; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23439"
FT CHAIN 2..851
FT /note="Rod cGMP-specific 3',5'-cyclic phosphodiesterase
FT subunit beta"
FT /id="PRO_0000023348"
FT PROPEP 852..854
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000023349"
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"
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 851
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..279
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044919"
FT VAR_SEQ 835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_036884"
FT VARIANT 74
FT /note="R -> C (in RP40; autosomal recessive;
FT dbSNP:rs144590560)"
FT /id="VAR_009283"
FT VARIANT 100
FT /note="R -> H (in RP40; dbSNP:rs555600300)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068361"
FT VARIANT 166
FT /note="E -> K (in dbSNP:rs115775983)"
FT /evidence="ECO:0000269|PubMed:8698075"
FT /id="VAR_009284"
FT VARIANT 212
FT /note="Y -> H (in dbSNP:rs551545798)"
FT /evidence="ECO:0000269|PubMed:8698075"
FT /id="VAR_009285"
FT VARIANT 219
FT /note="Y -> H (in RP40; autosomal recessive;
FT dbSNP:rs62295357)"
FT /id="VAR_009286"
FT VARIANT 228
FT /note="L -> H (in RP40; autosomal recessive and autosomal
FT dominant)"
FT /evidence="ECO:0000269|PubMed:8698075"
FT /id="VAR_009287"
FT VARIANT 228
FT /note="L -> I (in dbSNP:rs201584824)"
FT /id="VAR_009288"
FT VARIANT 258
FT /note="H -> N (in CSNBAD2; dbSNP:rs121918582)"
FT /evidence="ECO:0000269|PubMed:8075643"
FT /id="VAR_009289"
FT VARIANT 320
FT /note="V -> I (in dbSNP:rs10902758)"
FT /evidence="ECO:0000269|PubMed:1322354,
FT ECO:0000269|PubMed:1338685, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8768262,
FT ECO:0000269|Ref.5"
FT /id="VAR_054868"
FT VARIANT 527
FT /note="L -> P (in RP40; autosomal recessive;
FT dbSNP:rs760766981)"
FT /id="VAR_009290"
FT VARIANT 535
FT /note="I -> N (in RP40; autosomal recessive;
FT dbSNP:rs527236088)"
FT /evidence="ECO:0000269|PubMed:9543643"
FT /id="VAR_009291"
FT VARIANT 552
FT /note="R -> Q (in RP40; autosomal recessive;
FT dbSNP:rs751859807)"
FT /evidence="ECO:0000269|PubMed:8956055"
FT /id="VAR_009292"
FT VARIANT 557
FT /note="H -> Y (in RP40; autosomal dominant;
FT dbSNP:rs121918581)"
FT /evidence="ECO:0000269|PubMed:8394174"
FT /id="VAR_006050"
FT VARIANT 576
FT /note="G -> D (in RP40; autosomal recessive)"
FT /evidence="ECO:0000269|PubMed:8595886"
FT /id="VAR_006051"
FT VARIANT 654
FT /note="E -> D (in dbSNP:rs17849286)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_054869"
FT VARIANT 699
FT /note="L -> R (in RP40; autosomal recessive)"
FT /evidence="ECO:0000269|PubMed:8557257"
FT /id="VAR_006052"
FT VARIANT 776
FT /note="D -> N (in RP40; dbSNP:rs141563823)"
FT /evidence="ECO:0000269|PubMed:22334370"
FT /id="VAR_068362"
FT VARIANT 854
FT /note="L -> R (in RP40; autosomal recessive)"
FT /id="VAR_009293"
FT CONFLICT 33..35
FT /note="AAA -> GRG (in Ref. 1; CAA44569, 2; CAA46932 and 3;
FT AAB22690)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="K -> Q (in Ref. 1; CAA44569)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> L (in Ref. 1; CAA44569)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="A -> R (in Ref. 1; CAA44569)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="Y -> I (in Ref. 1; CAA44569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 98336 MW; BB11A519BE88C9DF CRC64;
MSLSEEQARS FLDQNPDFAR QYFGKKLSPE NVAAACEDGC PPDCDSLRDL CQVEESTALL
ELVQDMQESI NMERVVFKVL RRLCTLLQAD RCSLFMYRQR NGVAELATRL FSVQPDSVLE
DCLVPPDSEI VFPLDIGVVG HVAQTKKMVN VEDVAECPHF SSFADELTDY KTKNMLATPI
MNGKDVVAVI MAVNKLNGPF FTSEDEDVFL KYLNFATLYL KIYHLSYLHN CETRRGQVLL
WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW SVLMGESQPY
SGPRTPDGRE IVFYKVIDYV LHGKEEIKVI PTPSADHWAL ASGLPSYVAE SGFICNIMNA
SADEMFKFQE GALDDSGWLI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DEQDEVLMES
LTQFLGWSVM NTDTYDKMNK LENRKDIAQD MVLYHVKCDR DEIQLILPTR ARLGKEPADC
DEDELGEILK EELPGPTTFD IYEFHFSDLE CTELDLVKCG IQMYYELGVV RKFQIPQEVL
VRFLFSISKG YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLSEE TLNIYQNLNR RQHEHVIHLM
DIAIIATDLA LYFKKRAMFQ KIVDESKNYQ DKKSWVEYLS LETTRKEIVM AMMMTACDLS
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT
FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEKEEEERV AAKKVGTEIC
NGGPAPKSST CCIL
