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LST8_DICDI
ID   LST8_DICDI              Reviewed;         304 AA.
AC   Q54D08;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein LST8 homolog;
DE   AltName: Full=Lethal with sec thirteen 8 protein;
GN   Name=lst8; ORFNames=DDB_G0292592;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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   [2]
RP   FUNCTION, IDENTIFICATION IN A TORC1 AND TORC2 COMPLEX, DISRUPTION
RP   PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16079174; DOI=10.1091/mbc.e05-04-0342;
RA   Lee S., Comer F.I., Sasaki A., McLeod I.X., Duong Y., Okumura K.,
RA   Yates J.R. III, Parent C.A., Firtel R.A.;
RT   "TOR complex 2 integrates cell movement during chemotaxis and signal relay
RT   in Dictyostelium.";
RL   Mol. Biol. Cell 16:4572-4583(2005).
CC   -!- FUNCTION: Plays a role in regulation of adenylate cyclase and protein
CC       kinase B (PKB) activation during aggregation. Involved in both
CC       chemotaxis and signal relay. {ECO:0000269|PubMed:16079174}.
CC   -!- SUBUNIT: Part of a complex, TORC1, consisting of tor, raptor and lst8.
CC       Part of a complex, TORC2, consisting of tor, lst8, piaA and ripA.
CC       Additional proteins, such as 14-3-3 and heat-shock proteins, may also
CC       belong to the TORC2 complex. {ECO:0000269|PubMed:16079174}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells have serious developmental defects, because
CC       they are unable to activate the aggregation-stage adenylyl cyclase acaA
CC       in response to chemoattractant and are defective in chemotaxis.
CC       {ECO:0000269|PubMed:16079174}.
CC   -!- SIMILARITY: Belongs to the WD repeat LST8 family. {ECO:0000305}.
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DR   EMBL; AAFI02000194; EAL61099.1; -; Genomic_DNA.
DR   RefSeq; XP_629512.1; XM_629510.1.
DR   AlphaFoldDB; Q54D08; -.
DR   SMR; Q54D08; -.
DR   STRING; 44689.DDB0233210; -.
DR   PaxDb; Q54D08; -.
DR   EnsemblProtists; EAL61099; EAL61099; DDB_G0292592.
DR   GeneID; 8628763; -.
DR   KEGG; ddi:DDB_G0292592; -.
DR   dictyBase; DDB_G0292592; lst8.
DR   eggNOG; KOG0315; Eukaryota.
DR   HOGENOM; CLU_000288_57_5_1; -.
DR   InParanoid; Q54D08; -.
DR   OMA; VQRNYKH; -.
DR   PhylomeDB; Q54D08; -.
DR   Reactome; R-DDI-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DDI-1632852; Macroautophagy.
DR   Reactome; R-DDI-165159; MTOR signalling.
DR   Reactome; R-DDI-166208; mTORC1-mediated signalling.
DR   Reactome; R-DDI-3371571; HSF1-dependent transactivation.
DR   Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-DDI-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DDI-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-DDI-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-DDI-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-DDI-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:Q54D08; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005776; C:autophagosome; IDA:dictyBase.
DR   GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031931; C:TORC1 complex; IBA:GO_Central.
DR   GO; GO:0031932; C:TORC2 complex; IDA:dictyBase.
DR   GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; IMP:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; IDA:dictyBase.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:dictyBase.
DR   GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   GO; GO:0038203; P:TORC2 signaling; IDA:dictyBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR037588; MLST8.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19842; PTHR19842; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Cytoplasm; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..304
FT                   /note="Protein LST8 homolog"
FT                   /id="PRO_0000326507"
FT   REPEAT          1..28
FT                   /note="WD 1"
FT   REPEAT          31..69
FT                   /note="WD 2"
FT   REPEAT          74..113
FT                   /note="WD 3"
FT   REPEAT          115..154
FT                   /note="WD 4"
FT   REPEAT          158..197
FT                   /note="WD 5"
FT   REPEAT          205..244
FT                   /note="WD 6"
FT   REPEAT          247..286
FT                   /note="WD 7"
SQ   SEQUENCE   304 AA;  33481 MW;  EE6F2E5DBCCA7070 CRC64;
     MPGIILATAS YDHTIKFWDP PSGGCYRSID CGEFHINRLE ITHDKLYIAA AGNPQTRLFE
     VNTNNNSPAM SFDGHKGNVT GVGFQKEGKW MYTGSEDGTV KIWDLKAPGC QRDYECSAPV
     NTVVLHPNQA ELISGDQNGS IRVWDLISNT CSRELVPDGE VGITSLTISS DGGLVVASNT
     KGKCFVWRLG EDDTSRFEPL QKIEAHNAPI LKTLFSPDTK LLATCSADHT VKIWNTKKFN
     VVQTLNGHQR WVWDCAFSND SAYLVTGSSD HLSRLWDLHQ GDAVKTYSGH IKAVNAVALN
     DLPR
 
 
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