PHOS_HORSE
ID PHOS_HORSE Reviewed; 245 AA.
AC Q9XS39;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phosducin;
DE Short=PHD;
GN Name=PDC;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Icelandic; TISSUE=Pineal gland, and Retina;
RX PubMed=11197562; DOI=10.2460/ajvr.2001.62.61;
RA Keller C., Schulz R.;
RT "Nucleotide and deduced amino acid sequence of equine retinal and pineal
RT gland phosducin.";
RL Am. J. Vet. Res. 62:61-66(2001).
CC -!- FUNCTION: May participate in the regulation of visual phototransduction
CC or in the integration of photoreceptor metabolism. Inhibits the
CC transcriptional activation activity of the cone-rod homeobox CRX (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-
CC binding protein, transducin. Interacts with CRX (By similarity).
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 -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; AF135443; AAD26865.1; -; mRNA.
DR EMBL; AF155881; AAD38848.1; -; mRNA.
DR EMBL; AF162703; AAD47064.1; -; mRNA.
DR RefSeq; NP_001075317.1; NM_001081848.1.
DR RefSeq; XP_005609800.1; XM_005609743.1.
DR AlphaFoldDB; Q9XS39; -.
DR SMR; Q9XS39; -.
DR STRING; 9796.ENSECAP00000013414; -.
DR PaxDb; Q9XS39; -.
DR Ensembl; ENSECAT00000016604; ENSECAP00000013414; ENSECAG00000015729.
DR GeneID; 100033898; -.
DR KEGG; ecb:100033898; -.
DR CTD; 5132; -.
DR VGNC; VGNC:50858; PDC.
DR GeneTree; ENSGT00940000156236; -.
DR HOGENOM; CLU_085598_1_0_1; -.
DR InParanoid; Q9XS39; -.
DR OrthoDB; 1324495at2759; -.
DR Proteomes; UP000002281; Chromosome 5.
DR Bgee; ENSECAG00000015729; Expressed in retina and 2 other tissues.
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 2: Evidence at transcript level;
KW Cell projection; Cilium; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..245
FT /note="Phosducin"
FT /id="PRO_0000163751"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..245
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
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"
SQ SEQUENCE 245 AA; 28214 MW; 60C58E0DEBA63C3A CRC64;
MEEARRQSLE EDFEGQATHT GPKGVINDWR KFKLESEDSD SIPPCKKEIL KQMSSPQSRD
DKDSKERFSR KMSIQEYELI HQDKEDENCL RKYRRQCMQD MHQKLSFGPR YGFVYELETG
EQFLETIEKE QKITTIVVHI YEDGIKGCDA LNSSLACLAA EYPMVKFCKI KASNTGAGDR
FSSDVLPTLL VYKGGELISN FLSVAEQFAE EFFAGDVESF LNEYGLLPER EIHALEQTSM
EEDVE