PHOS_CANLF
ID PHOS_CANLF Reviewed; 245 AA.
AC O77560; Q9TSE3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosducin;
DE Short=PHD;
DE AltName: Full=33 kDa phototransducing protein;
GN Name=PDC;
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 [MRNA], AND VARIANT PD GLY-82.
RX PubMed=9714819; DOI=10.1016/s0378-1119(98)00310-2;
RA Zhang Q., Acland G.M., Parshall C.J., Haskell J., Ray K., Aguirre G.D.;
RT "Characterization of canine photoreceptor phosducin cDNA and identification
RT of a sequence variant in dogs with photoreceptor dysplasia.";
RL Gene 215:231-239(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9820795; DOI=10.1006/exer.1998.0569;
RA Lin C.T., Petersen-Jones S.M., Sargan D.R.;
RT "Isolation and investigation of canine phosducin as a candidate for canine
RT generalized progressive retinal atrophies.";
RL Exp. Eye Res. 67:473-480(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12091798;
RA Dekomien G., Epplen J.T.;
RT "The canine Phosducin gene: characterization of the exon-intron structure
RT and exclusion as a candidate gene for generalized progressive retinal
RT atrophy in 11 dog breeds.";
RL Mol. Vis. 8:138-142(2002).
CC -!- FUNCTION: Inhibits the transcriptional activation activity of the cone-
CC rod homeobox CRX (By similarity). May participate in the regulation of
CC visual phototransduction or in the integration of photoreceptor
CC metabolism. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CRX (By similarity). Forms a complex with the
CC beta and gamma subunits of the GTP-binding protein, transducin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P20941}. Nucleus {ECO:0000250|UniProtKB:P20941}.
CC Cell projection, cilium, photoreceptor outer segment
CC {ECO:0000250|UniProtKB:P19632}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P19632}.
CC -!- PTM: Light-induced changes in cyclic nucleotide levels modulate the
CC phosphorylation of this protein by cAMP kinase. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in PDC are the cause of photoreceptor dysplasia
CC (PD); an autosomal recessive disease of miniature schnauzer dogs
CC causing retinal degeneration. {ECO:0000269|PubMed:9714819}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; AF046874; AAC27249.1; -; mRNA.
DR EMBL; Y17697; CAA76818.1; -; mRNA.
DR EMBL; AJ417559; CAD10383.2; -; Genomic_DNA.
DR EMBL; AJ417560; CAD10383.2; JOINED; Genomic_DNA.
DR EMBL; AJ417561; CAD10383.2; JOINED; Genomic_DNA.
DR RefSeq; NP_001003076.1; NM_001003076.1.
DR AlphaFoldDB; O77560; -.
DR SMR; O77560; -.
DR STRING; 9612.ENSCAFP00000035560; -.
DR PaxDb; O77560; -.
DR Ensembl; ENSCAFT00030000954; ENSCAFP00030000826; ENSCAFG00030000579.
DR Ensembl; ENSCAFT00040009818; ENSCAFP00040008503; ENSCAFG00040005240.
DR Ensembl; ENSCAFT00845009526; ENSCAFP00845007448; ENSCAFG00845005358.
DR GeneID; 403624; -.
DR KEGG; cfa:403624; -.
DR CTD; 5132; -.
DR VEuPathDB; HostDB:ENSCAFG00845005358; -.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000156236; -.
DR HOGENOM; CLU_085598_1_0_1; -.
DR InParanoid; O77560; -.
DR OMA; CRKMSMQ; -.
DR OrthoDB; 1324495at2759; -.
DR TreeFam; TF315179; -.
DR Proteomes; UP000002254; Chromosome 7.
DR Bgee; ENSCAFG00000013751; Expressed in testis.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd02987; Phd_like_Phd; 1.
DR Gene3D; 1.10.168.10; -; 2.
DR InterPro; IPR001200; Phosducin.
DR InterPro; IPR023196; Phosducin_N_dom_sf.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR PRINTS; PR00677; PHOSDUCIN.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cytoplasm; Disease variant; Nucleus;
KW Phosphoprotein; Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..245
FT /note="Phosducin"
FT /id="PRO_0000163749"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..245
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT COMPBIAS 26..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 73
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P19632"
FT VARIANT 82
FT /note="R -> G (in PD)"
FT /evidence="ECO:0000269|PubMed:9714819"
FT CONFLICT 198
FT /note="I -> L (in Ref. 1; AAC27249)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="V -> G (in Ref. 1; AAC27249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28306 MW; D201EF3A6E7DD232 CRC64;
MEEAKNQSLE EDFEGQATHT GPKGVINDWR KFKLESEDSD SVPPSKKEIL RQMSSPQNRD
DKDSKERFSR KMSIQEYELI HRDKEDENCL RKYRRQCMQD MHQKLSFGPR YGFVYELETG
EQFLETIEKE QKITTIVVHI YEDGVKGCDA LNSSFTCLAA EYPMVKFCKI KASNTGAGDR
FSSDVLPTLL IYKGGELISN FISVTEQFAE EFFAGDVESF LNEYGLLPER EIHALDQTNM
EEDTE
