PHOS_BOVIN
ID PHOS_BOVIN Reviewed; 245 AA.
AC P19632; P20940; Q28160;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Phosducin;
DE Short=PHD;
DE AltName: Full=33 kDa phototransducing protein;
DE AltName: Full=Protein MEKA;
GN Name=PDC;
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 PROTEIN SEQUENCE, AND NUCLEOTIDE SEQUENCE [MRNA] OF 228-245.
RC TISSUE=Retina;
RX PubMed=2203790; DOI=10.1016/s0021-9258(18)55479-x;
RA Lee R.H., Fowler A., McGinnis J.F., Lolley R.N., Craft C.M.;
RT "Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein
RT from photoreceptor cells.";
RL J. Biol. Chem. 265:15867-15873(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2770450; DOI=10.1016/0169-328x(89)90022-3;
RA Kuo C.-H., Akiyama M., Miki N.;
RT "Isolation of a novel retina-specific clone (MEKA cDNA) encoding a
RT photoreceptor soluble protein.";
RL Brain Res. Mol. Brain Res. 6:1-10(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-245.
RC 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 [4]
RP PHOSPHORYLATION AT SER-73.
RX PubMed=2394752; DOI=10.1016/s0021-9258(18)55478-8;
RA Lee R.H., Brown B.M., Lolley R.N.;
RT "Protein kinase A phosphorylates retinal phosducin on serine 73 in situ.";
RL J. Biol. Chem. 265:15860-15866(1990).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10866677; DOI=10.1128/mcb.20.14.5216-5226.2000;
RA Zhu X., Craft C.M.;
RT "Modulation of CRX transactivation activity by phosducin isoforms.";
RL Mol. Cell. Biol. 20:5216-5226(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH G-BETA AND G-GAMMA.
RX PubMed=9739091; DOI=10.1016/s0969-2126(98)00102-6;
RA Loew A., Ho Y.K., Blundell T., Bax B.;
RT "Phosducin induces a structural change in transducin beta gamma.";
RL Structure 6:1007-1019(1998).
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:0000269|PubMed:10866677}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:10866677}.
CC -!- PTM: Light-induced changes in cyclic nucleotide levels modulate the
CC phosphorylation of this protein by cAMP kinase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62716.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M58170; AAA62716.1; ALT_FRAME; mRNA.
DR EMBL; M33529; AAA30349.1; -; mRNA.
DR PIR; A38379; A38379.
DR PDB; 1A0R; X-ray; 2.80 A; P=1-245.
DR PDBsum; 1A0R; -.
DR AlphaFoldDB; P19632; -.
DR SMR; P19632; -.
DR CORUM; P19632; -.
DR IntAct; P19632; 2.
DR MINT; P19632; -.
DR STRING; 9913.ENSBTAP00000005468; -.
DR iPTMnet; P19632; -.
DR PaxDb; P19632; -.
DR PRIDE; P19632; -.
DR eggNOG; KOG3171; Eukaryota.
DR InParanoid; P19632; -.
DR EvolutionaryTrace; P19632; -.
DR Proteomes; UP000009136; Unplaced.
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; IEA:UniProtKB-SubCell.
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;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Sensory transduction; Vision.
FT CHAIN 1..245
FT /note="Phosducin"
FT /id="PRO_0000163748"
FT REGION 1..70
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..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:0000269|PubMed:2394752"
FT CONFLICT 44
FT /note="H -> P (in Ref. 3; AAA30349)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..239
FT /note="TN -> SK (in Ref. 3; AAA30349)"
FT /evidence="ECO:0000305"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 87..105
FT /evidence="ECO:0007829|PDB:1A0R"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1A0R"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:1A0R"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:1A0R"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1A0R"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:1A0R"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1A0R"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:1A0R"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1A0R"
SQ SEQUENCE 245 AA; 28231 MW; 5CA621610401D550 CRC64;
MEKAKSQSLE EDFEGQASHT GPKGVINDWR KFKLESEDSD SVAHSKKEIL RQMSSPQSRD
DKDSKERFSR KMSVQEYELI HKDKEDENCL RKYRRQCMQD MHQKLSFGPR YGFVYELESG
EQFLETIEKE QKITTIVVHI YEDGIKGCDA LNSSLICLAA EYPMVKFCKI KASNTGAGDR
FSSDVLPTLL VYKGGELLSN FISVTEQLAE EFFTGDVESF LNEYGLLPEK EMHVLEQTNM
EEDME
