PDE6D_CANLF
ID PDE6D_CANLF Reviewed; 150 AA.
AC Q9XT54;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta;
DE Short=GMP-PDE delta;
GN Name=PDE6D;
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 [GENOMIC DNA / MRNA].
RX PubMed=10452952; DOI=10.1016/s0378-1119(99)00246-2;
RA Wang W., Zhang Q., Acland G.M., Mellersh C., Ostrander E.A., Ray K.,
RA Aguirre G.D.;
RT "Molecular characterization and mapping of canine cGMP-phosphodiesterase
RT delta subunit (PDE6D).";
RL Gene 236:325-332(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RA Petersen-Jones S.M., Zhu F.-X., Entz D.D.;
RT "Exclusion of the rod phosphodiesterase delta subunit (PDE6D) gene as the
RT locus responsible for progressive retinal atrophy in 9 breeds of dog.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dekomien G., Epplen J.T.;
RT "Identification of intron 1 and mutation analysis for gPRA of the PDED
RT gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes the release of prenylated target proteins from
CC cellular membranes (By similarity). Modulates the activity of
CC prenylated or palmitoylated Ras family members by regulating their
CC subcellular location (By similarity). 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) (By similarity).
CC Increases the affinity of ARL3 for GTP by several orders of magnitude.
CC Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By
CC similarity). {ECO:0000250|UniProtKB:O43924,
CC ECO:0000250|UniProtKB:O55057, ECO:0000250|UniProtKB:Q95142}.
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 (By similarity). Interacts with RAB13 (prenylated form);
CC dissociates RAB13 from membranes (By similarity). Interacts with RPGR
CC (By similarity). Interacts with ARL2 (By similarity). Interacts with
CC ARL3; the interaction occurs specifically with the GTP-bound form of
CC ARL3 (By similarity). Interaction with ARL2 and ARL3 promotes release
CC of farnesylated cargo proteins (By similarity).
CC {ECO:0000250|UniProtKB:O43924, ECO:0000250|UniProtKB:O55057,
CC ECO:0000250|UniProtKB:Q95142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O55057}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:O43924}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43924}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:O43924}.
CC -!- TISSUE SPECIFICITY: Retina. {ECO:0000303|Ref.2}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; AF113996; AAD39365.1; -; Genomic_DNA.
DR EMBL; AF109151; AAD54058.1; -; mRNA.
DR EMBL; AY029186; AAK31798.1; -; mRNA.
DR EMBL; AJ427395; CAD20650.2; -; Genomic_DNA.
DR EMBL; AJ427396; CAD20650.2; JOINED; Genomic_DNA.
DR RefSeq; NP_001003156.1; NM_001003156.1.
DR AlphaFoldDB; Q9XT54; -.
DR SMR; Q9XT54; -.
DR STRING; 9612.ENSCAFP00000016354; -.
DR ChEMBL; CHEMBL3286064; -.
DR PaxDb; Q9XT54; -.
DR Ensembl; ENSCAFT00000109058; ENSCAFP00000071585; ENSCAFG00000011104.
DR Ensembl; ENSCAFT00030033084; ENSCAFP00030028860; ENSCAFG00030017873.
DR Ensembl; ENSCAFT00040045318; ENSCAFP00040039574; ENSCAFG00040024325.
DR Ensembl; ENSCAFT00845042834; ENSCAFP00845033577; ENSCAFG00845024260.
DR GeneID; 403781; -.
DR KEGG; cfa:403781; -.
DR CTD; 5147; -.
DR VEuPathDB; HostDB:ENSCAFG00845024260; -.
DR VGNC; VGNC:44360; PDE6D.
DR eggNOG; KOG4038; Eukaryota.
DR GeneTree; ENSGT00390000000263; -.
DR HOGENOM; CLU_119682_0_0_1; -.
DR InParanoid; Q9XT54; -.
DR OMA; FKGRCLE; -.
DR OrthoDB; 1192412at2759; -.
DR TreeFam; TF314474; -.
DR Reactome; R-CFA-5624958; ARL13B-mediated ciliary trafficking of INPP5E.
DR Reactome; R-CFA-9648002; RAS processing.
DR Proteomes; UP000002254; Chromosome 25.
DR Bgee; ENSCAFG00000011104; Expressed in placenta and 49 other tissues.
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:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell projection; cGMP; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW 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_0000221207"
FT REGION 144..150
FT /note="Required for association with membranes"
FT /evidence="ECO:0000250"
SQ SEQUENCE 150 AA; 17362 MW; 797002FC4F905EBF CRC64;
MSAKDERARE ILKGFKLNWM NLRDAETGKI LWQGTEDLSV PGVEHEARVP KKILKCKAVS
RELNFSSAEQ MEKFRLEQKV YFKGQCLEEW FFEFGFVIPN STNTWQSLIE AAPESQMMPA
SVLTGNVIIE TKFFDDDLLV STSRVRLFYV
