RDEA_DICDI
ID RDEA_DICDI Reviewed; 254 AA.
AC Q54RR8; O77083;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphorelay intermediate protein rdeA;
DE AltName: Full=Hpt domain-containing protein rdeA;
DE AltName: Full=Rapid development protein A;
GN Name=rdeA; ORFNames=DDB_G0282923;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-63 AND HIS-65.
RC STRAIN=NC-4;
RX PubMed=9582274; DOI=10.1093/emboj/17.10.2809;
RA Chang W.-T., Thomason P.A., Gross J.D., Neweil P.C.;
RT "Evidence that the RdeA protein is a component of a multistep phosphorelay
RT modulating rate of development in Dictyostelium.";
RL EMBO J. 17:2809-2816(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=6298035; DOI=10.1016/0012-1606(83)90018-0;
RA Abe K., Yanagisawa K.;
RT "A new class of rapidly developing mutants in Dictyostelium discoideum:
RT implications for cyclic AMP metabolism and cell differentiation.";
RL Dev. Biol. 95:200-210(1983).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=9812977; DOI=10.1074/jbc.273.47.30859;
RA Kim H.-J., Chang W.-T., Meima M., Gross J.D., Schaap P.;
RT "A novel adenylyl cyclase detected in rapidly developing mutants of
RT Dictyostelium.";
RL J. Biol. Chem. 273:30859-30862(1998).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF HIS-63
RP AND HIS-65.
RX PubMed=10488068; DOI=10.1074/jbc.274.39.27379;
RA Thomason P.A., Traynor D., Stock J.B., Kay R.R.;
RT "The RdeA-RegA system, a eukaryotic phospho-relay controlling cAMP
RT breakdown.";
RL J. Biol. Chem. 274:27379-27384(1999).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=11060029; DOI=10.1093/emboj/19.21.5782;
RA Ott A., Oehme F., Keller H., Schuster S.C.;
RT "Osmotic stress response in Dictyostelium is mediated by cAMP.";
RL EMBO J. 19:5782-5792(2000).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=16765443; DOI=10.1016/j.plasmid.2006.04.001;
RA Thomason P.A., Brazill D.T., Cox E.C.;
RT "A series of Dictyostelium expression vectors for recombination cloning.";
RL Plasmid 56:145-152(2006).
RN [8]
RP IDENTIFICATION.
RX PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL Genome Biol. 8:R144.1-R144.15(2007).
CC -!- FUNCTION: Phosphorelay protein that supplies phosphate to regA or
CC accepts phosphate from regA; depending on the relative concentration of
CC the phosphodonor proteins. In vitro, acts as a substrate for cheA
CC (bacterial kinase). Plays a role in the development. ypd1 (yeast) can
CC complement rdeA defect. {ECO:0000269|PubMed:10488068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9582274}.
CC -!- DEVELOPMENTAL STAGE: Expressed early in development in the form of
CC precocious cell aggregation. Expressed at a significant level during
CC vegetative growth and peaks at 8-16 hours of development. Even at its
CC peak, the level of expression is low. {ECO:0000269|PubMed:9582274}.
CC -!- PTM: The phosphorelay mechanism involves the sequential transfer of a
CC phosphate group from 'Asp-212' of pde2 to His-65 of rdeA. In vitro,
CC dephosphorylated by dokA.
CC -!- DISRUPTION PHENOTYPE: Final morphogenesis aberrant, rapid development
CC (body formation accelerated), premature spore maturation and elevated
CC levels of cAMP. PkaR and rdeA double mutants are rapidly developing and
CC sporogenous. acaA and rdeA double mutant forms only a very small number
CC of spores and no cAMP synthesis. {ECO:0000269|PubMed:10488068,
CC ECO:0000269|PubMed:11060029, ECO:0000269|PubMed:16765443,
CC ECO:0000269|PubMed:6298035, ECO:0000269|PubMed:9582274,
CC ECO:0000269|PubMed:9812977}.
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DR EMBL; AF051931; AAC61850.1; -; mRNA.
DR EMBL; AAFI02000049; EAL65905.1; -; Genomic_DNA.
DR RefSeq; XP_639283.1; XM_634191.1.
DR AlphaFoldDB; Q54RR8; -.
DR SMR; Q54RR8; -.
DR STRING; 44689.DDB0191140; -.
DR PaxDb; Q54RR8; -.
DR EnsemblProtists; EAL65905; EAL65905; DDB_G0282923.
DR GeneID; 8623852; -.
DR KEGG; ddi:DDB_G0282923; -.
DR dictyBase; DDB_G0282923; rdeA.
DR eggNOG; ENOG502RHQ7; Eukaryota.
DR HOGENOM; CLU_1095938_0_0_1; -.
DR InParanoid; Q54RR8; -.
DR OMA; AYCKNDE; -.
DR PRO; PR:Q54RR8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0043424; F:protein histidine kinase binding; IBA:GO_Central.
DR GO; GO:0046058; P:cAMP metabolic process; IMP:dictyBase.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0061128; P:positive regulation of chemotaxis to cAMP by DIF-2; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IGI:dictyBase.
DR Gene3D; 1.20.120.160; -; 1.
DR InterPro; IPR045871; AHP1-5/YPD1.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR28242; PTHR28242; 1.
DR Pfam; PF01627; Hpt; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR PROSITE; PS50894; HPT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..254
FT /note="Phosphorelay intermediate protein rdeA"
FT /id="PRO_0000377481"
FT DOMAIN 26..123
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT REGION 124..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MUTAGEN 63
FT /note="H->Q: No change."
FT /evidence="ECO:0000269|PubMed:10488068,
FT ECO:0000269|PubMed:9582274"
FT MUTAGEN 65
FT /note="H->Q: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:10488068,
FT ECO:0000269|PubMed:9582274"
FT CONFLICT 162
FT /note="G -> C (in Ref. 1; AAC61850)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="E -> K (in Ref. 1; AAC61850)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="E -> G (in Ref. 1; AAC61850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 254 AA; 27893 MW; E90310BE26924E76 CRC64;
MISDYEGPTP TKKFDQDILF DYSEGEKEFT FELLDSYISS VEEHLPELLN SFEAKDLKGA
VLHSHDIKGS SSYIGCEAVR YVSGKIEAYC KNDELEKAES FYPELKKEVE EVFKILSDFK
KNWDKNHGEG GSDDGGDDNE SEPTENNNND GSSVNNNDSS SGGGGKDIEN KNTDENTGKN
LNERSKSPVP LQTTLKPVTI ETPKTASDKI ATETPTSLAN NTNSSSNNNS KNENGLNSKQ
PQTSSNSPTK IQTK
