PLP2_YEAST
ID PLP2_YEAST Reviewed; 286 AA.
AC Q12017; D6W2Y0;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosducin-like protein 2;
DE AltName: Full=Viral IAP-associated factor 1 homolog;
GN Name=PLP2 {ECO:0000312|SGD:S000005807};
GN Synonyms=VIAF1 {ECO:0000312|EMBL:AAG21890.1}; OrderedLocusNames=YOR281C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG21890.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15371430; DOI=10.1074/jbc.m409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E., Rumble J.M.,
RA Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that
RT modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2] {ECO:0000312|EMBL:CAA61786.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA99507.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH THE STE4-STE18 COMPLEX.
RX PubMed=10749875; DOI=10.1074/jbc.m002163200;
RA Flanary P.L., DiBello P.R., Estrada P., Dohlman H.G.;
RT "Functional analysis of Plp1 and Plp2, two homologues of phosducin in
RT yeast.";
RL J. Biol. Chem. 275:18462-18469(2000).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP FUNCTION, INTERACTION WITH CCT2, AND DISRUPTION PHENOTYPE.
RX PubMed=17429077; DOI=10.1091/mbc.e07-01-0069;
RA Stirling P.C., Srayko M., Takhar K.S., Pozniakovsky A., Hyman A.A.,
RA Leroux M.R.;
RT "Functional interaction between phosducin-like protein 2 and cytosolic
RT chaperonin is essential for cytoskeletal protein function and cell cycle
RT progression.";
RL Mol. Biol. Cell 18:2336-2345(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-62, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Essential for cell growth (PubMed:10749875). Inhibits early
CC G-protein signaling events following pheromone stimulation
CC (PubMed:10749875). Inhibits the folding activity of the chaperonin-
CC containing T-complex (CCT) CCT2 which leads to inhibition of
CC cytoskeletal actin folding (PubMed:17429077). Plays a role in cell
CC cycle progression in G1/S phase (PubMed:17429077).
CC {ECO:0000269|PubMed:10749875, ECO:0000269|PubMed:17429077}.
CC -!- SUBUNIT: Interacts with the G protein beta-gamma subunit complex (STE4-
CC STE18 complex) (PubMed:10749875). Interacts with CCT2; this interaction
CC leads to inhibition of CCT complex mediated actin folding
CC (PubMed:17429077). {ECO:0000269|PubMed:10749875,
CC ECO:0000269|PubMed:17429077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Impaired growth, cytoskeletal disruptions caused
CC by actin polarization defects, and abberent nuclear segregation caused
CC by misoriented mitotic spindles (PubMed:17429077). Cells are enlarged
CC or do not bud, caused by cell cycle arrest in G1/S phase
CC (PubMed:17429077). {ECO:0000269|PubMed:17429077}.
CC -!- MISCELLANEOUS: Present with 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; AF110514; AAG21890.1; -; mRNA.
DR EMBL; X89633; CAA61786.1; -; Genomic_DNA.
DR EMBL; Z75189; CAA99507.1; -; Genomic_DNA.
DR EMBL; AY558032; AAS56358.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11046.1; -; Genomic_DNA.
DR PIR; S67183; S67183.
DR RefSeq; NP_014924.3; NM_001183700.3.
DR AlphaFoldDB; Q12017; -.
DR SMR; Q12017; -.
DR BioGRID; 34669; 53.
DR DIP; DIP-5004N; -.
DR IntAct; Q12017; 11.
DR MINT; Q12017; -.
DR STRING; 4932.YOR281C; -.
DR iPTMnet; Q12017; -.
DR MaxQB; Q12017; -.
DR PaxDb; Q12017; -.
DR PRIDE; Q12017; -.
DR EnsemblFungi; YOR281C_mRNA; YOR281C; YOR281C.
DR GeneID; 854456; -.
DR KEGG; sce:YOR281C; -.
DR SGD; S000005807; PLP2.
DR VEuPathDB; FungiDB:YOR281C; -.
DR eggNOG; KOG3170; Eukaryota.
DR GeneTree; ENSGT00940000175722; -.
DR HOGENOM; CLU_072604_1_0_1; -.
DR InParanoid; Q12017; -.
DR OMA; QKPDYSR; -.
DR BioCyc; YEAST:G3O-33768-MON; -.
DR PRO; PR:Q12017; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12017; protein.
DR GO; GO:0005737; C:cytoplasm; IPI:SGD.
DR GO; GO:0003779; F:actin binding; IDA:SGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; IMP:UniProtKB.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Pheromone response; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..286
FT /note="Phosducin-like protein 2"
FT /id="PRO_0000163762"
FT REGION 96..286
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 286 AA; 32793 MW; 414A696FFBDBD833 CRC64;
MQNEPMFQVQ VDESEDSEWN DILRAKGVIP ERAPSPTAKL EEALEEAIAK QHENRLEDKD
LSDLEELEDD EDEDFLEAYK IKRLNEIRKL QERSKFGEVF HINKPEYNKE VTLASQGKKY
EGAQTNDNGE EDDGGVYVFV HLSLQSKLQS RILSHLFQSA ACKFREIKFV EIPANRAIEN
YPESNCPTLI VYYRGEVIKN MITLLELGGN NSKMEDFEDF MVKVGAVAEG DNRLIMNRDD
EESREERKLH YGEKKSIRSG IRGKFNVGIG GNDDGNINDD DDGFFD
