PHOS_HUMAN
ID PHOS_HUMAN Reviewed; 246 AA.
AC P20941; Q14816; Q9UP22; Q9UP23;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Phosducin;
DE Short=PHD;
DE AltName: Full=33 kDa phototransducing protein;
DE AltName: Full=Protein MEKA;
GN Name=PDC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2383274; DOI=10.1016/0006-291x(90)92183-z;
RA Watanabe Y., Kawasaki K., Miki N., Kuo C.H.;
RT "Isolation and analysis of the human MEKA gene encoding a retina-specific
RT protein.";
RL Biochem. Biophys. Res. Commun. 170:951-956(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH
RP CRX, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000269|PubMed:10866677}.
CC -!- SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-
CC binding protein, transducin. Interacts with CRX.
CC {ECO:0000269|PubMed:10866677}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10866677}.
CC Nucleus {ECO:0000269|PubMed:10866677}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:P19632}.
CC Photoreceptor inner segment {ECO:0000250|UniProtKB:P19632}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:10866677}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P20941-1; Sequence=Displayed;
CC Name=2; Synonyms=PhLOP1;
CC IsoId=P20941-2; Sequence=VSP_043880;
CC Name=3;
CC IsoId=P20941-3; Sequence=VSP_053778;
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}.
CC -!- WEB RESOURCE: Name=Mutations of the PDC gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/pdcmut.htm";
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DR EMBL; M33478; AAA35486.1; -; mRNA.
DR EMBL; M38059; AAA36210.1; -; Genomic_DNA.
DR EMBL; M60720; AAA36210.1; JOINED; Genomic_DNA.
DR EMBL; M38058; AAA36210.1; JOINED; Genomic_DNA.
DR EMBL; AF076463; AAD43141.1; -; mRNA.
DR EMBL; AF076464; AAD43142.1; -; mRNA.
DR EMBL; AL596220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91212.1; -; Genomic_DNA.
DR CCDS; CCDS1370.1; -. [P20941-1]
DR CCDS; CCDS41447.1; -. [P20941-2]
DR PIR; A35422; A35422.
DR RefSeq; NP_002588.3; NM_002597.4. [P20941-1]
DR RefSeq; NP_072098.1; NM_022576.3. [P20941-2]
DR RefSeq; XP_011507905.1; XM_011509603.2. [P20941-1]
DR AlphaFoldDB; P20941; -.
DR SMR; P20941; -.
DR BioGRID; 111159; 10.
DR STRING; 9606.ENSP00000375855; -.
DR iPTMnet; P20941; -.
DR PhosphoSitePlus; P20941; -.
DR BioMuta; PDC; -.
DR DMDM; 130134; -.
DR jPOST; P20941; -.
DR MassIVE; P20941; -.
DR PaxDb; P20941; -.
DR PeptideAtlas; P20941; -.
DR PRIDE; P20941; -.
DR ProteomicsDB; 53830; -. [P20941-1]
DR ProteomicsDB; 53831; -. [P20941-2]
DR Antibodypedia; 34456; 108 antibodies from 20 providers.
DR DNASU; 5132; -.
DR Ensembl; ENST00000391997.3; ENSP00000375855.2; ENSG00000116703.14. [P20941-1]
DR Ensembl; ENST00000497198.1; ENSP00000422775.1; ENSG00000116703.14. [P20941-2]
DR GeneID; 5132; -.
DR KEGG; hsa:5132; -.
DR MANE-Select; ENST00000391997.3; ENSP00000375855.2; NM_002597.5; NP_002588.3.
DR UCSC; uc001grz.4; human. [P20941-1]
DR CTD; 5132; -.
DR DisGeNET; 5132; -.
DR GeneCards; PDC; -.
DR HGNC; HGNC:8759; PDC.
DR HPA; ENSG00000116703; Tissue enriched (retina).
DR MIM; 171490; gene.
DR neXtProt; NX_P20941; -.
DR OpenTargets; ENSG00000116703; -.
DR PharmGKB; PA33109; -.
DR VEuPathDB; HostDB:ENSG00000116703; -.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000156236; -.
DR HOGENOM; CLU_085598_1_0_1; -.
DR InParanoid; P20941; -.
DR OMA; CRKMSMQ; -.
DR PhylomeDB; P20941; -.
DR TreeFam; TF315179; -.
DR PathwayCommons; P20941; -.
DR SignaLink; P20941; -.
DR SIGNOR; P20941; -.
DR BioGRID-ORCS; 5132; 19 hits in 1040 CRISPR screens.
DR ChiTaRS; PDC; human.
DR GeneWiki; Phosducin; -.
DR GenomeRNAi; 5132; -.
DR Pharos; P20941; Tbio.
DR PRO; PR:P20941; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P20941; protein.
DR Bgee; ENSG00000116703; Expressed in pigmented layer of retina and 85 other tissues.
DR ExpressionAtlas; P20941; baseline and differential.
DR Genevisible; P20941; HS.
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:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007602; P:phototransduction; TAS:ProtInc.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
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 Alternative splicing; Cell projection; Cilium; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..246
FT /note="Phosducin"
FT /id="PRO_0000163752"
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 MOD_RES 73
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P19632"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10866677"
FT /id="VSP_043880"
FT VAR_SEQ 1
FT /note="M -> MPESLDSPTSGRPGVTTHSTRTPGTEIQTIISNPVPKM (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10866677"
FT /id="VSP_053778"
FT CONFLICT 140
FT /note="I -> L (in Ref. 2; AAA36210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 28246 MW; DF59C2C7C3308C90 CRC64;
MEEAKSQSLE EDFEGQATHT GPKGVINDWR KFKLESQDSD SIPPSKKEIL RQMSSPQSRN
GKDSKERVSR KMSIQEYELI HKEKEDENCL RKYRRQCMQD MHQKLSFGPR YGFVYELETG
KQFLETIEKE LKITTIVVHI YEDGIKGCDA LNSSLTCLAA EYPIVKFCKI KASNTGAGDR
FSLDVLPTLL IYKGGELISN FISVAEQFAE EFFAGDVESF LNEYGLLPER EVHVLEHTKI
EEEDVE
