KAPR_YEAST
ID KAPR_YEAST Reviewed; 416 AA.
AC P07278; D6VVP9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=cAMP-dependent protein kinase regulatory subunit;
DE Short=cAPK regulatory subunit;
DE AltName: Full=Bypass of cyclase mutations protein 1;
DE AltName: Full=Protein kinase A regulatory subunit;
DE Short=PKA regulatory subunit;
GN Name=BCY1; Synonyms=REG1, SRA1; OrderedLocusNames=YIL033C;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-80; 83-126;
RP 139-177; 195-203; 227-275; 291-298; 310-340; 345-377 AND 387-399, FUNCTION,
RP AND SUBUNIT.
RX PubMed=3037314; DOI=10.1128/mcb.7.4.1371-1377.1987;
RA Toda T., Cameron S., Sass P., Zoller M., Scott J.D., McMullen B.,
RA Hurwitz M., Krebs E.G., Wigler M.;
RT "Cloning and characterization of BCY1, a locus encoding a regulatory
RT subunit of the cyclic AMP-dependent protein kinase in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 7:1371-1377(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2823100; DOI=10.1128/mcb.7.8.2653-2663.1987;
RA Cannon J.F., Tatchell K.;
RT "Characterization of Saccharomyces cerevisiae genes encoding subunits of
RT cyclic AMP-dependent protein kinase.";
RL Mol. Cell. Biol. 7:2653-2663(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3547325; DOI=10.1093/nar/15.1.368;
RA Kunisawa R., Davis T.N., Urdea M.S., Thorner J.;
RT "Complete nucleotide sequence of the gene encoding the regulatory subunit
RT of 3',5'-cyclic AMP-dependent protein kinase from the yeast Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 15:368-369(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
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 [7]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=6243658; DOI=10.1016/s0021-9258(19)86004-0;
RA Hixson C.S., Krebs E.G.;
RT "Characterization of a cyclic AMP-binding protein from bakers' yeast.
RT Identification as a regulatory subunit of cyclic AMP-dependent protein
RT kinase.";
RL J. Biol. Chem. 255:2137-2145(1980).
RN [8]
RP PROTEIN SEQUENCE OF 2-19.
RX PubMed=1339314; DOI=10.1016/0092-8674(92)90246-9;
RA Sachs A.B., Deardorff J.A.;
RT "Translation initiation requires the PAB-dependent poly(A) ribonuclease in
RT yeast.";
RL Cell 70:961-973(1992).
RN [9]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11134339; DOI=10.1128/mcb.21.2.511-523.2001;
RA Griffioen G., Branduardi P., Ballarini A., Anghileri P., Norbeck J.,
RA Baroni M.D., Ruis H.;
RT "Nucleocytoplasmic distribution of budding yeast protein kinase A
RT regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent
RT phosphorylation of its targeting domain.";
RL Mol. Cell. Biol. 21:511-523(2001).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12704202; DOI=10.1074/jbc.m210691200;
RA Griffioen G., Swinnen S., Thevelein J.M.;
RT "Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3
RT phosphorylation of a cAMP-dependent protein kinase regulatory subunit.";
RL J. Biol. Chem. 278:23460-23471(2003).
RN [11]
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 [12]
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 [13]
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 [14]
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-145 AND THR-150, 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).
RN [17]
RP PHOSPHORYLATION AT SER-68; SER-70; SER-74; SER-77; SER-79; SER-81; SER-83;
RP SER-84; THR-129; SER-130; THR-131; THR-144; SER-145; SER-147; THR-150 AND
RP THR-160, AND MUTAGENESIS OF THR-129.
RX PubMed=20702584; DOI=10.1091/mbc.e10-03-0182;
RA Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.;
RT "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein
RT kinase A toward some but not all substrates.";
RL Mol. Biol. Cell 21:3475-3486(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 171-416 IN COMPLEX WITH CAMP.
RX PubMed=21070946; DOI=10.1016/j.str.2010.08.013;
RA Rinaldi J., Wu J., Yang J., Ralston C.Y., Sankaran B., Moreno S.,
RA Taylor S.S.;
RT "Structure of yeast regulatory subunit: a glimpse into the evolution of PKA
RT signaling.";
RL Structure 18:1471-1482(2010).
CC -!- FUNCTION: Regulatory subunit of the cyclic AMP-dependent protein kinase
CC (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in
CC the absence of cAMP. cAMP activates PKA and promotes growth and
CC proliferation in response to good nutrient conditions. Together with
CC ZDS1, provides a negative feedback control on the cell wall integrity-
CC signaling pathway by acting as a negative regulator of MAP kinase
CC SLT2/MPK1. {ECO:0000269|PubMed:12704202, ECO:0000269|PubMed:2823100,
CC ECO:0000269|PubMed:3037314, ECO:0000269|PubMed:6243658}.
CC -!- SUBUNIT: The inactive holoenzyme of cAMP-dependent protein kinase is a
CC tetramer, composed of 2 regulatory subunits (R, encoded by BCY1) and
CC two catalytic subunits (C, encoded by the 3 partially redundant TPK1,
CC TPK2, and TPK3 genes). Activation by cAMP causes dissociation of the
CC holoenzyme, producing 2 active catalytic monomers C and a regulatory
CC dimer R(2). {ECO:0000269|PubMed:21070946, ECO:0000269|PubMed:3037314}.
CC -!- INTERACTION:
CC P07278; P07278: BCY1; NbExp=3; IntAct=EBI-9475, EBI-9475;
CC P07278; P22696: ESS1; NbExp=2; IntAct=EBI-9475, EBI-6679;
CC P07278; P06244: TPK1; NbExp=7; IntAct=EBI-9475, EBI-9458;
CC P07278; P06245: TPK2; NbExp=6; IntAct=EBI-9475, EBI-9465;
CC P07278; P05986: TPK3; NbExp=4; IntAct=EBI-9475, EBI-9470;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic when
CC phosphorylated. Nuclear when not phosphorylated.
CC -!- DOMAIN: The inhibitor sequence (IS) is a substrate recognition motif
CC that docks to the active site cleft of the catalytic subunit rendering
CC the holoenzyme inactive.
CC -!- DOMAIN: Binding of cAMP to the 2 tandem cyclic-nucleotide binding
CC domains (CNB-A and CNB-B) induces a conformational change in BCY1,
CC causing the interaction surface with the catalytic subunit to be
CC destroyed and eventually the dissociation of the R dimer from the C
CC subunits.
CC -!- PTM: Phosphorylated by YAK1 in response to glucose starvation.
CC Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1)
CC inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA.
CC TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on
CC Ser-145 phosphorylation. The phosphorylation sites can be clustered in
CC several groups, all localized in the N-terminal part. The first cluster
CC termed cluster I (CI) is located close to the N-terminus and includes
CC Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second
CC includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and
CC Ser-84. This cluster of phosphorylation sites, termed cluster II (CII),
CC is important for BCY1 cytoplasmic localization and function
CC (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster
CC of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-
CC 150, and Thr-160. This cluster falls within or near the so-called
CC autoinhibitory domain where the catalytic subunit of PKA
CC autophosphorylates the highly conserved Ser-145 to inhibit BCY1
CC (PubMed:20702584). A last cluster of phosphorylated residues included
CC Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites
CC in CIII (and to a lesser extent in CII) are hyperphosphorylated in
CC response to rapamycin (PubMed:20702584). {ECO:0000269|PubMed:11134339,
CC ECO:0000269|PubMed:12704202, ECO:0000269|PubMed:20702584}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; M15756; AAA34468.1; -; Genomic_DNA.
DR EMBL; M17223; AAA66934.1; -; Genomic_DNA.
DR EMBL; X05051; CAA28726.1; -; Genomic_DNA.
DR EMBL; Z46861; CAA86918.1; -; Genomic_DNA.
DR EMBL; AY558087; AAS56413.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08515.1; -; Genomic_DNA.
DR PIR; A25868; OKBYRC.
DR RefSeq; NP_012231.1; NM_001179383.1.
DR PDB; 3OF1; X-ray; 2.21 A; A=171-416.
DR PDB; 6XQK; X-ray; 2.56 A; A/B/C/D/E/F/G/H=1-50.
DR PDBsum; 3OF1; -.
DR PDBsum; 6XQK; -.
DR AlphaFoldDB; P07278; -.
DR SMR; P07278; -.
DR BioGRID; 34957; 370.
DR ComplexPortal; CPX-536; cAMP-dependent protein kinase complex variant 1.
DR ComplexPortal; CPX-537; cAMP-dependent protein kinase complex variant 2.
DR ComplexPortal; CPX-571; cAMP-dependent protein kinase complex variant 3.
DR ComplexPortal; CPX-572; cAMP-dependent protein kinase complex variant 4.
DR ComplexPortal; CPX-573; cAMP-dependent protein kinase complex variant 5.
DR ComplexPortal; CPX-574; cAMP-dependent protein kinase complex variant 6.
DR DIP; DIP-551N; -.
DR IntAct; P07278; 23.
DR MINT; P07278; -.
DR STRING; 4932.YIL033C; -.
DR iPTMnet; P07278; -.
DR MaxQB; P07278; -.
DR PaxDb; P07278; -.
DR PRIDE; P07278; -.
DR TopDownProteomics; P07278; -.
DR EnsemblFungi; YIL033C_mRNA; YIL033C; YIL033C.
DR GeneID; 854778; -.
DR KEGG; sce:YIL033C; -.
DR SGD; S000001295; BCY1.
DR VEuPathDB; FungiDB:YIL033C; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000168302; -.
DR HOGENOM; CLU_018310_0_1_1; -.
DR InParanoid; P07278; -.
DR OMA; YDNWSPP; -.
DR BioCyc; YEAST:G3O-31305-MON; -.
DR Reactome; R-SCE-163615; PKA activation.
DR Reactome; R-SCE-164378; PKA activation in glucagon signalling.
DR Reactome; R-SCE-180024; DARPP-32 events.
DR Reactome; R-SCE-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-SCE-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-SCE-5610787; Hedgehog 'off' state.
DR Reactome; R-SCE-9634597; GPER1 signaling.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR ChiTaRS; REG1; yeast.
DR PRO; PR:P07278; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P07278; protein.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IBA:GO_Central.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:SGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IGI:SGD.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IMP:SGD.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IMP:SGD.
DR GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IMP:SGD.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; cAMP; cAMP-binding; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1339314,
FT ECO:0000269|PubMed:3037314, ECO:0000269|PubMed:6243658"
FT CHAIN 2..416
FT /note="cAMP-dependent protein kinase regulatory subunit"
FT /id="PRO_0000205418"
FT REGION 2..183
FT /note="Dimerization and phosphorylation"
FT REGION 8..45
FT /note="Dimerization/docking domain (D/D)"
FT REGION 65..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..146
FT /note="Inhibitor sequence (IS)"
FT COMPBIAS 69..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..301
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21070946"
FT BINDING 249
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21070946"
FT BINDING 258
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21070946"
FT BINDING 302..416
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21070946"
FT BINDING 368
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21070946"
FT BINDING 377
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21070946"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 144
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 145
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20702584,
FT ECO:0000269|PubMed:3037314, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20702584,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20702584"
FT MUTAGEN 129
FT /note="T->D: Confers increased sensitivity to rapamycin and
FT enhanced accumulation of glycogen upon TORC1 inhibition."
FT /evidence="ECO:0000269|PubMed:20702584"
FT CONFLICT 264
FT /note="A -> P (in Ref. 3; CAA28726)"
FT /evidence="ECO:0000305"
FT HELIX 7..23
FT /evidence="ECO:0007829|PDB:6XQK"
FT HELIX 28..48
FT /evidence="ECO:0007829|PDB:6XQK"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:3OF1"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:3OF1"
FT TURN 281..286
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3OF1"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 378..385
FT /evidence="ECO:0007829|PDB:3OF1"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:3OF1"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:3OF1"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:3OF1"
SQ SEQUENCE 416 AA; 47219 MW; 6D7D97D8E4340AF3 CRC64;
MVSSLPKESQ AELQLFQNEI NAANPSDFLQ FSANYFNKRL EQQRAFLKAR EPEFKAKNIV
LFPEPEESFS RPQSAQSQSR SRSSVMFKSP FVNEDPHSNV FKSGFNLDPH EQDTHQQAQE
EQQHTREKTS TPPLPMHFNA QRRTSVSGET LQPNNFDDWT PDHYKEKSEQ QLQRLEKSIR
NNFLFNKLDS DSKRLVINCL EEKSVPKGAT IIKQGDQGDY FYVVEKGTVD FYVNDNKVNS
SGPGSSFGEL ALMYNSPRAA TVVATSDCLL WALDRLTFRK ILLGSSFKKR LMYDDLLKSM
PVLKSLTTYD RAKLADALDT KIYQPGETII REGDQGENFY LIEYGAVDVS KKGQGVINKL
KDHDYFGEVA LLNDLPRQAT VTATKRTKVA TLGKSGFQRL LGPAVDVLKL NDPTRH
