PHOS_RAT
ID PHOS_RAT Reviewed; 246 AA.
AC P20942; Q63420;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phosducin;
DE Short=PHD;
DE AltName: Full=33 kDa phototransducing protein;
DE AltName: Full=Protein MEKA;
DE AltName: Full=Rod photoreceptor 1;
DE Short=RPR-1;
GN Name=Pdc; Synonyms=Rpr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pineal gland, and Retina;
RX PubMed=2210381; DOI=10.1016/0378-1119(90)90090-e;
RA Abe T., Nakabayashi H., Tamada H., Takagi T., Sakuragi S., Yamaki K.,
RA Shinohara T.;
RT "Analysis of the human, bovine and rat 33-kDa proteins and cDNA in retina
RT and pineal gland.";
RL Gene 91:209-215(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pineal gland;
RX PubMed=2071146; DOI=10.1016/0888-7543(91)90325-9;
RA Craft C.M., Lolley R.N., Seldin M.F., Lee R.H.;
RT "Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and
RT chromosomal assignment in the mouse.";
RL Genomics 10:400-409(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH G-BETA AND G-GAMMA.
RX PubMed=10360181; DOI=10.1016/s1097-2765(00)80358-5;
RA Gaudet R., Savage J.R., McLaughlin J.N., Willardson B.M., Sigler P.B.;
RT "A molecular mechanism for the phosphorylation-dependent regulation of
RT heterotrimeric G-proteins by phosducin. Structural analysis of phosducin
RT and its phosphorylation-regulated interaction with transducin beta-gamma.";
RL Mol. Cell 3:649-660(1999).
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.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; M33528; AAA40604.1; -; mRNA.
DR EMBL; M33530; AAA40603.1; -; mRNA.
DR EMBL; M60738; AAA41841.1; -; mRNA.
DR PIR; A39903; A39903.
DR PIR; JH0216; JH0216.
DR RefSeq; NP_037004.1; NM_012872.1.
DR PDB; 1B9X; X-ray; 3.00 A; C=1-246.
DR PDB; 1B9Y; X-ray; 3.00 A; C=1-246.
DR PDB; 2TRC; X-ray; 2.40 A; P=14-230.
DR PDBsum; 1B9X; -.
DR PDBsum; 1B9Y; -.
DR PDBsum; 2TRC; -.
DR AlphaFoldDB; P20942; -.
DR SMR; P20942; -.
DR BioGRID; 247382; 1.
DR DIP; DIP-41816N; -.
DR IntAct; P20942; 1.
DR MINT; P20942; -.
DR STRING; 10116.ENSRNOP00000003405; -.
DR iPTMnet; P20942; -.
DR PhosphoSitePlus; P20942; -.
DR PaxDb; P20942; -.
DR Ensembl; ENSRNOT00000003405; ENSRNOP00000003405; ENSRNOG00000002517.
DR GeneID; 25343; -.
DR KEGG; rno:25343; -.
DR UCSC; RGD:3277; rat.
DR CTD; 5132; -.
DR RGD; 3277; Pdc.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000156236; -.
DR HOGENOM; CLU_085598_1_0_1; -.
DR InParanoid; P20942; -.
DR OMA; CRKMSMQ; -.
DR OrthoDB; 1324495at2759; -.
DR PhylomeDB; P20942; -.
DR TreeFam; TF315179; -.
DR EvolutionaryTrace; P20942; -.
DR PRO; PR:P20942; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002517; Expressed in cerebellum and 2 other tissues.
DR Genevisible; P20942; RN.
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; ISO:RGD.
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 3D-structure; Cell projection; Cilium; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..246
FT /note="Phosducin"
FT /id="PRO_0000163754"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..246
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..70
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 191
FT /note="V -> I"
FT CONFLICT 39
FT /note="G -> S (in Ref. 2; AAA41841)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="G -> V (in Ref. 2; AAA41841)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="T -> S (in Ref. 2; AAA41841)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="D -> E (in Ref. 2; AAA41841)"
FT /evidence="ECO:0000305"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 87..105
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2TRC"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:1B9X"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:2TRC"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:2TRC"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:2TRC"
SQ SEQUENCE 246 AA; 28129 MW; 3C48ABCB4E5E3D04 CRC64;
MEEAASQSLE EDFEGQATHT GPKGVINDWR KFKLESEDGD SIPPSKKEIL RQMSSPQSRD
DKDSKERMSR KMSIQEYELI HQDKEDEGCL RKYRRQCMQD MHQKLSFGPR YGFVYELETG
EQFLETIEKE QKVTTIVVNI YEDGVRGCDA LNSSLECLAA EYPMVKFCKI RASNTGAGDR
FSSDVLPTLL VYKGGELISN FISVAEQFAE DFFAADVESF LNEYGLLPER EIHDLGQTNT
EDEDIE
