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PHLP_DROME
ID   PHLP_DROME              Reviewed;         276 AA.
AC   Q9VUR7; Q8T3W9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Phosducin-like protein;
DE            Short=PHLP;
GN   ORFNames=CG7650;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-74.
RC   STRAIN=Berkeley; TISSUE=Testis;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-19 AND SER-20, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
CC   -!- FUNCTION: Functions as a co-chaperone for CCT in the assembly of
CC       heterotrimeric G protein complexes, facilitates the assembly of both
CC       Gbeta-Ggamma and RGS-Gbeta5 heterodimers. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-
CC       binding proteins. Interacts with the CCT chaperonin complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR   EMBL; AE014296; AAF49608.2; -; Genomic_DNA.
DR   EMBL; BT009952; AAQ22421.1; -; mRNA.
DR   EMBL; AY089459; AAL90197.1; -; mRNA.
DR   RefSeq; NP_648786.1; NM_140529.3.
DR   AlphaFoldDB; Q9VUR7; -.
DR   SMR; Q9VUR7; -.
DR   BioGRID; 65012; 2.
DR   STRING; 7227.FBpp0075344; -.
DR   iPTMnet; Q9VUR7; -.
DR   PaxDb; Q9VUR7; -.
DR   DNASU; 39694; -.
DR   EnsemblMetazoa; FBtr0075591; FBpp0075344; FBgn0036519.
DR   GeneID; 39694; -.
DR   KEGG; dme:Dmel_CG7650; -.
DR   UCSC; CG7650-RA; d. melanogaster.
DR   FlyBase; FBgn0036519; CG7650.
DR   VEuPathDB; VectorBase:FBgn0036519; -.
DR   eggNOG; KOG3171; Eukaryota.
DR   GeneTree; ENSGT00940000168834; -.
DR   HOGENOM; CLU_085598_0_0_1; -.
DR   InParanoid; Q9VUR7; -.
DR   OMA; RQTGHNQ; -.
DR   OrthoDB; 1324495at2759; -.
DR   PhylomeDB; Q9VUR7; -.
DR   Reactome; R-DME-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   BioGRID-ORCS; 39694; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39694; -.
DR   PRO; PR:Q9VUR7; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036519; Expressed in testis and 23 other tissues.
DR   Genevisible; Q9VUR7; DM.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd02987; Phd_like_Phd; 1.
DR   Gene3D; 1.10.168.10; -; 1.
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   Chaperone; Phosphoprotein; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Phosducin-like protein"
FT                   /id="PRO_0000372652"
FT   REGION          18..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..276
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        38..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   CONFLICT        30
FT                   /note="G -> D (in Ref. 4; AAL90197)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        41
FT                   /note="C -> S (in Ref. 4; AAL90197)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="D -> N (in Ref. 4; AAL90197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   276 AA;  30976 MW;  B23C69D5366BF4A5 CRC64;
     MATLEDKLLG EKLEYYCSSS EGEDNGDEGG DNKGASGKSR CSGLTIDTNP DATPAGGFRQ
     QSSTNTGPKG VVKDWQRFKQ LEAERRDETE RQRLALAKKL TITATTSAED EERKRQEELD
     AELDELMSED FLQQYQKQRM AEMLRQTGHH QQFGQVQQLT SHEEFLACVE QENKHTTIII
     HIYERQLAAC ATLNKCLDSL ASDYPSIKFA KICSSVAGMS RDFRTKGLPA LLVYKAQAVI
     GNFVRLTDDL SDDFFASDVE SFLIEHGIIV DRALYN
 
 
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