CRP1_YEAST
ID CRP1_YEAST Reviewed; 465 AA.
AC P38845; D3DL95;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cruciform DNA-recognizing protein 1;
DE Contains:
DE RecName: Full=CRP1 short N-terminal subpeptide;
DE Contains:
DE RecName: Full=CRP1 short C-terminal subpeptide;
GN Name=CRP1; OrderedLocusNames=YHR146W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP CRUCIFORM DNA-BINDING, FUNCTION, DOMAIN, AND PROTEOLYTIC AUTOCLEAVAGE.
RX PubMed=12419258; DOI=10.1016/s0022-2836(02)00993-2;
RA Rass U., Kemper B.;
RT "Crp1p, a new cruciform DNA-binding protein in the yeast Saccharomyces
RT cerevisiae.";
RL J. Mol. Biol. 323:685-700(2002).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-156 AND SER-440, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271; THR-295; SER-319;
RP SER-394 AND SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; SER-271; THR-295;
RP SER-343; THR-366 AND SER-440, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Cruciform DNA-binding protein which exerts an enhancing
CC effect on the cleavage of cruciform DNA (X-DNA) by endonuclease VII
CC from bacteriophage T4. {ECO:0000269|PubMed:12419258}.
CC -!- PTM: Cleaved in the vicinity of position 160 to give an X-DNA-binding
CC N-terminal subpeptide and a non-DNA-binding C-terminal subpeptide.
CC -!- MISCELLANEOUS: Present with 2990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CRP1/MDG1 family. {ECO:0000305}.
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DR EMBL; U10397; AAB68982.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06839.1; -; Genomic_DNA.
DR PIR; S46759; S46759.
DR RefSeq; NP_012016.1; NM_001179277.1.
DR AlphaFoldDB; P38845; -.
DR SMR; P38845; -.
DR BioGRID; 36580; 141.
DR IntAct; P38845; 27.
DR MINT; P38845; -.
DR STRING; 4932.YHR146W; -.
DR iPTMnet; P38845; -.
DR MaxQB; P38845; -.
DR PaxDb; P38845; -.
DR PRIDE; P38845; -.
DR EnsemblFungi; YHR146W_mRNA; YHR146W; YHR146W.
DR GeneID; 856551; -.
DR KEGG; sce:YHR146W; -.
DR SGD; S000001189; CRP1.
DR VEuPathDB; FungiDB:YHR146W; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000176749; -.
DR HOGENOM; CLU_594765_0_0_1; -.
DR InParanoid; P38845; -.
DR OMA; TFSWPAG; -.
DR BioCyc; YEAST:G3O-31181-MON; -.
DR Reactome; R-SCE-1632852; Macroautophagy.
DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SCE-200425; Carnitine metabolism.
DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR PRO; PR:P38845; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38845; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..465
FT /note="Cruciform DNA-recognizing protein 1"
FT /id="PRO_0000202923"
FT CHAIN 1..160
FT /note="CRP1 short N-terminal subpeptide"
FT /id="PRO_0000409594"
FT CHAIN 161..465
FT /note="CRP1 short C-terminal subpeptide"
FT /id="PRO_0000409595"
FT REGION 107..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..161
FT /note="X-DNA-binding"
FT REGION 247..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..148
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 366
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 465 AA; 51116 MW; 30880758F37991C7 CRC64;
MSSELMFNYT FSWPAGPKDV ILTGTFDDWR GTLPLVKTAK GNFEITMPVK LANKDDTFQF
KFIVDGVWCV SDSYKKEHVS EGIENNFLQI TDLVETQEVA GASRIPEAGG LLCGKPPRSA
GPPSTSNRKK NKRNNKKRRS KLKKKSTKNN KKSNESLDDN EEEDGVTGTT TEDVTGTSRE
ETPLAEPTNV SKEAPGNFHI LPIDQSADTT QSNGIIGGPG PVLVPNPGEI KEFTEIRDVD
ARELNERLNK KEEVPEPVAG PIVESSVTEK SPALPQADDP IVETKEVAHN VQELTPQVEA
VTPLINEPEP LPTPEAQISI PESSKVEPVE GSLQSKLVEK RESTEGVLDG SKKVENKAKK
DEEVFTLDPI VNKAPKLPLT DEQTAEGRKS PAVSEEKEKK KKQEKGSKEV KRSETSKEKK
PSAKEVKKQT VKAPKKQTAS PLSSSTEEPK KKKTGFFGKL KKLFK
