PDE6D_BOVIN
ID PDE6D_BOVIN Reviewed; 150 AA.
AC Q95142;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta;
DE Short=GMP-PDE delta;
GN Name=PDE6D;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=8798640; DOI=10.1074/jbc.271.39.24036;
RA Florio S.K., Prusti R.K., Beavo J.A.;
RT "Solubilization of membrane-bound rod phosphodiesterase by the rod
RT phosphodiesterase recombinant delta subunit.";
RL J. Biol. Chem. 271:24036-24047(1996).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=14561760; DOI=10.1074/jbc.m306559200;
RA Zhang H., Liu X.H., Zhang K., Chen C.K., Frederick J.M., Prestwich G.D.,
RA Baehr W.;
RT "Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as
RT a prenyl-binding protein.";
RL J. Biol. Chem. 279:407-413(2004).
CC -!- FUNCTION: Promotes the release of prenylated target proteins from
CC cellular membranes (PubMed:8798640). 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:0000269|PubMed:14561760}.
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
CC (PubMed:8798640). Interacts with prenylated GRK1 and GRK7
CC (PubMed:14561760). Interacts with prenylated INPP5E (By similarity).
CC Interacts with prenylated Ras family members, including HRAS, KRAS,
CC NRAS, RAP2A, RAP2C and RHEB (By similarity). Interacts with RAB13
CC (prenylated form); dissociates RAB13 from membranes (By similarity).
CC Interacts with RPGR (By similarity). Interacts with ARL2
CC (PubMed:14561760). Interacts with ARL3; the interaction occurs
CC specifically with the GTP-bound form of ARL3 (By similarity).
CC Interaction with ARL2 and ARL3 promotes release of farnesylated cargo
CC proteins (By similarity). {ECO:0000250|UniProtKB:O43924,
CC ECO:0000250|UniProtKB:O55057, ECO:0000269|PubMed:14561760,
CC ECO:0000269|PubMed:8798640}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14561760,
CC ECO:0000305|PubMed:8798640}. 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: Detected in retina photoreceptor cells, especially
CC in rods (at protein level)(PubMed:8798640, PubMed:14561760). Detected
CC in retina, brain and adrenal gland (PubMed:8798640).
CC {ECO:0000269|PubMed:14561760, ECO:0000269|PubMed:8798640}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; U65073; AAC48634.1; -; mRNA.
DR RefSeq; NP_776845.1; NM_174420.2.
DR AlphaFoldDB; Q95142; -.
DR SMR; Q95142; -.
DR BioGRID; 159267; 1.
DR STRING; 9913.ENSBTAP00000025947; -.
DR BindingDB; Q95142; -.
DR ChEMBL; CHEMBL2096979; -.
DR DrugCentral; Q95142; -.
DR PaxDb; Q95142; -.
DR PRIDE; Q95142; -.
DR Ensembl; ENSBTAT00000025947; ENSBTAP00000025947; ENSBTAG00000019480.
DR GeneID; 281976; -.
DR KEGG; bta:281976; -.
DR CTD; 5147; -.
DR VEuPathDB; HostDB:ENSBTAG00000019480; -.
DR VGNC; VGNC:32682; PDE6D.
DR eggNOG; KOG4038; Eukaryota.
DR GeneTree; ENSGT00390000000263; -.
DR HOGENOM; CLU_119682_0_0_1; -.
DR InParanoid; Q95142; -.
DR OMA; FKGRCLE; -.
DR OrthoDB; 1192412at2759; -.
DR TreeFam; TF314474; -.
DR PRO; PR:Q95142; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000019480; Expressed in oocyte and 103 other tissues.
DR ExpressionAtlas; Q95142; baseline and differential.
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:0042622; C:photoreceptor outer segment membrane; IDA:CAFA.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Cell projection; cGMP; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Membrane; Reference proteome;
KW Sensory transduction; Vision.
FT CHAIN 1..150
FT /note="Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic
FT phosphodiesterase subunit delta"
FT /id="PRO_0000221206"
FT REGION 144..150
FT /note="Required for association with membranes"
FT /evidence="ECO:0000250"
SQ SEQUENCE 150 AA; 17390 MW; 5E8D881372905EA0 CRC64;
MSAKDERARE ILRGFKLNWM NLRDAETGKI LWQGTEDLSV PGVEHEARVP KKILKCKAVS
RELNFSSAEQ MEKFRLEQKV YFKGQCLEEW FFEFGFVIPN STNTWQSLIE AAPESQMMPA
SVLTGNVIIE TKFFDDDLLV STSRVRLFYV
