PDE6D_MOUSE
ID PDE6D_MOUSE Reviewed; 150 AA.
AC O55057;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta;
DE Short=GMP-PDE delta;
GN Name=Pde6d;
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 [GENOMIC DNA].
RX PubMed=9570951; DOI=10.1006/geno.1998.5210;
RA Li N., Florio S.K., Pettenati M.J., Rao P.N., Beavo J.A., Baehr W.;
RT "Characterization of human and mouse rod cGMP phosphodiesterase delta
RT subunit (PDE6D) and chromosomal localization of the human gene.";
RL Genomics 49:76-82(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9781033; DOI=10.1038/sj.ejhg.5200215;
RA Lorenz B., Migliaccio C., Lichtner P., Meyer C., Strom T.M., D'Urso M.,
RA Becker J., Ciccodicola A., Meitinger T.;
RT "Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit
RT gene (PDED) in man and mouse.";
RL Eur. J. Hum. Genet. 6:283-290(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP FUNCTION, AND INTERACTION WITH ARL3.
RX PubMed=10518933; DOI=10.1016/s0014-5793(99)01117-5;
RA Linari M., Hanzal-Bayer M., Becker J.;
RT "The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta,
RT interacts with the Arf-like protein Arl3 in a GTP specific manner.";
RL FEBS Lett. 458:55-59(1999).
RN [5]
RP INTERACTION WITH RPGR.
RX PubMed=9990021; DOI=10.1073/pnas.96.4.1315;
RA Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.;
RT "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta
RT subunit of rod cyclic GMP phosphodiesterase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH ARL2 AND ARL3.
RX PubMed=15979089; DOI=10.1016/j.jmb.2005.05.036;
RA Hanzal-Bayer M., Linari M., Wittinghofer A.;
RT "Properties of the interaction of Arf-like protein 2 with PDEdelta.";
RL J. Mol. Biol. 350:1074-1082(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22179043; DOI=10.1038/ncb2394;
RA Chandra A., Grecco H.E., Pisupati V., Perera D., Cassidy L., Skoulidis F.,
RA Ismail S.A., Hedberg C., Hanzal-Bayer M., Venkitaraman A.R.,
RA Wittinghofer A., Bastiaens P.I.;
RT "The GDI-like solubilizing factor PDEdelta sustains the spatial
RT organization and signalling of Ras family proteins.";
RL Nat. Cell Biol. 14:148-158(2012).
CC -!- FUNCTION: Promotes the release of prenylated target proteins from
CC cellular membranes (PubMed:22179043). Modulates the activity of
CC prenylated or palmitoylated Ras family members by regulating their
CC subcellular location (PubMed:22179043). Required for normal ciliary
CC targeting of farnesylated target proteins, such as INPP5E (By
CC similarity). Modulates the subcellular location of target proteins by
CC acting as a GTP specific dissociation inhibitor (GDI)
CC (PubMed:22179043). Increases the affinity of ARL3 for GTP by several
CC orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide
CC dissociation rate. {ECO:0000250|UniProtKB:O43924,
CC ECO:0000250|UniProtKB:Q95142, ECO:0000269|PubMed:10518933,
CC ECO:0000269|PubMed:15979089, ECO:0000269|PubMed:22179043}.
CC -!- SUBUNIT: Interacts with the prenylated catalytic subunits of PDE6, an
CC oligomer composed of two catalytic chains (PDE6A and PDE6B) and two
CC inhibitory chains (gamma); has no effect on enzyme activity but
CC promotes the release of the prenylated enzyme from cell membrane (By
CC similarity). Interacts with prenylated GRK1 and GRK7 (By similarity).
CC Interacts with prenylated INPP5E (By similarity). Interacts with
CC prenylated Ras family members, including HRAS, KRAS, NRAS, RAP2A, RAP2C
CC and RHEB (PubMed:22179043). Interacts with RAB13 (prenylated form);
CC dissociates RAB13 from membranes (By similarity). Interacts with RPGR
CC (PubMed:9990021). Interacts with ARL2 (PubMed:15979089). Interacts with
CC ARL3; the interaction occurs specifically with the GTP-bound form of
CC ARL3 (PubMed:15979089). Interaction with ARL2 and ARL3 promotes release
CC of farnesylated cargo proteins (By similarity).
CC {ECO:0000250|UniProtKB:O43924, ECO:0000250|UniProtKB:Q95142,
CC ECO:0000269|PubMed:10518933, ECO:0000269|PubMed:15979089,
CC ECO:0000269|PubMed:22179043, ECO:0000269|PubMed:9990021}.
CC -!- INTERACTION:
CC O55057; Q92834: RPGR; Xeno; NbExp=3; IntAct=EBI-6558402, EBI-6558417;
CC O55057; Q92834-2: RPGR; Xeno; NbExp=3; IntAct=EBI-6558402, EBI-6558503;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22179043}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O43924}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O43924}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:O43924}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; AF046000; AAC40094.1; -; Genomic_DNA.
DR EMBL; AF039216; AAC25686.1; -; mRNA.
DR EMBL; BC005636; AAH05636.1; -; mRNA.
DR CCDS; CCDS15121.1; -.
DR RefSeq; NP_032827.1; NM_008801.2.
DR PDB; 5T4X; X-ray; 1.81 A; A=1-150.
DR PDBsum; 5T4X; -.
DR AlphaFoldDB; O55057; -.
DR SMR; O55057; -.
DR BioGRID; 202080; 8.
DR CORUM; O55057; -.
DR IntAct; O55057; 1.
DR STRING; 10090.ENSMUSP00000027444; -.
DR PhosphoSitePlus; O55057; -.
DR PaxDb; O55057; -.
DR PeptideAtlas; O55057; -.
DR PRIDE; O55057; -.
DR ProteomicsDB; 294041; -.
DR Antibodypedia; 34421; 152 antibodies from 26 providers.
DR DNASU; 18582; -.
DR Ensembl; ENSMUST00000027444; ENSMUSP00000027444; ENSMUSG00000026239.
DR GeneID; 18582; -.
DR KEGG; mmu:18582; -.
DR UCSC; uc007bvq.1; mouse.
DR CTD; 5147; -.
DR MGI; MGI:1270843; Pde6d.
DR VEuPathDB; HostDB:ENSMUSG00000026239; -.
DR eggNOG; KOG4038; Eukaryota.
DR GeneTree; ENSGT00390000000263; -.
DR InParanoid; O55057; -.
DR OMA; FKGRCLE; -.
DR OrthoDB; 1192412at2759; -.
DR PhylomeDB; O55057; -.
DR TreeFam; TF314474; -.
DR Reactome; R-MMU-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 18582; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pde6d; mouse.
DR PRO; PR:O55057; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O55057; protein.
DR Bgee; ENSMUSG00000026239; Expressed in retinal neural layer and 279 other tissues.
DR ExpressionAtlas; O55057; baseline and differential.
DR Genevisible; O55057; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:MGI.
DR GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007602; P:phototransduction; TAS:MGI.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.70.50.40; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008015; PDED_dom.
DR InterPro; IPR037036; PDED_dom_sf.
DR InterPro; IPR017287; Rhodop-sen_GMP-Pdiesterase_dsu.
DR Pfam; PF05351; GMP_PDE_delta; 1.
DR PIRSF; PIRSF037825; GMP-Pdiesterase_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; cGMP; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Membrane; Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..150
FT /note="Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic
FT phosphodiesterase subunit delta"
FT /id="PRO_0000221209"
FT REGION 144..150
FT /note="Required for association with membranes"
FT /evidence="ECO:0000250"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:5T4X"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:5T4X"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:5T4X"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5T4X"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:5T4X"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:5T4X"
SQ SEQUENCE 150 AA; 17348 MW; 5E8D89C8020E38D5 CRC64;
MSAKDERARD ILRGFKLNWM NLRDAETGKI LWQGTEDLSV PGVEHEARVP KKILKCKAVS
RELNFSSAEQ MEKFRLEQKV YFKGQCLEEW FFEFGFVIPN STNTWQSLIE AAPESQMMPA
SVLTGNVIIE TKFFDDDLLV STSKVRLFYV
