IRS4_YEAST
ID IRS4_YEAST Reviewed; 615 AA.
AC P36115; D6VX84;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Increased rDNA silencing protein 4;
GN Name=IRS4; OrderedLocusNames=YKR019C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(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 DOMAIN.
RX PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
RA Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
RA Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
RT "Recognition specificity of individual EH domains of mammals and yeast.";
RL EMBO J. 17:6541-6550(1998).
RN [4]
RP FUNCTION.
RX PubMed=10082585; DOI=10.1128/mcb.19.4.3184;
RA Smith J.S., Caputo E., Boeke J.D.;
RT "A genetic screen for ribosomal DNA silencing defects identifies multiple
RT DNA replication and chromatin-modulating factors.";
RL Mol. Cell. Biol. 19:3184-3197(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH INP51.
RX PubMed=15265867; DOI=10.1074/jbc.m405589200;
RA Morales-Johansson H., Jenoe P., Cooke F.T., Hall M.N.;
RT "Negative regulation of phosphatidylinositol 4,5-bisphosphate levels by the
RT INP51-associated proteins TAX4 and IRS4.";
RL J. Biol. Chem. 279:39604-39610(2004).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP 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: With TAX4, acts as a positive regulator of INP51 activity and
CC phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates
CC signaling through the cell integrity pathway, including the MAP kinase
CC SLT2. Seems also to be involved in rDNA silencing.
CC {ECO:0000269|PubMed:10082585, ECO:0000269|PubMed:15265867}.
CC -!- SUBUNIT: Interacts with INP51. {ECO:0000269|PubMed:15265867}.
CC -!- INTERACTION:
CC P36115; P40559: INP51; NbExp=3; IntAct=EBI-27090, EBI-24915;
CC -!- SIMILARITY: Belongs to the IRS4 family. {ECO:0000305}.
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DR EMBL; Z28244; CAA82091.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09174.1; -; Genomic_DNA.
DR PIR; S38088; S38088.
DR RefSeq; NP_012944.3; NM_001179809.3.
DR AlphaFoldDB; P36115; -.
DR SMR; P36115; -.
DR BioGRID; 34151; 325.
DR IntAct; P36115; 2.
DR STRING; 4932.YKR019C; -.
DR iPTMnet; P36115; -.
DR MaxQB; P36115; -.
DR PaxDb; P36115; -.
DR PRIDE; P36115; -.
DR EnsemblFungi; YKR019C_mRNA; YKR019C; YKR019C.
DR GeneID; 853889; -.
DR KEGG; sce:YKR019C; -.
DR SGD; S000001727; IRS4.
DR VEuPathDB; FungiDB:YKR019C; -.
DR eggNOG; KOG0998; Eukaryota.
DR GeneTree; ENSGT00940000176414; -.
DR HOGENOM; CLU_454275_0_0_1; -.
DR InParanoid; P36115; -.
DR OMA; CESEPSI; -.
DR BioCyc; YEAST:G3O-31995-MON; -.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P36115; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36115; protein.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IGI:SGD.
DR GO; GO:0009267; P:cellular response to starvation; IGI:SGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IGI:SGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR000261; EH_dom.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..615
FT /note="Increased rDNA silencing protein 4"
FT /id="PRO_0000203199"
FT DOMAIN 460..571
FT /note="EH"
FT REGION 38..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..436
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 615 AA; 68880 MW; 242EBE45978068FD CRC64;
MRLSFGKQRY HGGTTVTLTE QGASDSLRAA QAIFQNHSNE VSSPCPPVTV SRNPQTRLSE
PSLQKSGRKQ EQKKARIRTK QVPKIKTTAP NDVELSKKHR SSPAGKDNVS STAQMAAALA
HSQSKLSSDN NSSHSSALDT LKVLETPNLN GLLGIHSRSS SRNGSNESLT PGQRTPDNRS
QENLLTSFSS GRRLSSSSME PATNKDSNKA LPKRRPSPPL QSSLVGSGQL HENENLSSIS
IDSRHSLNPD TSDVISNRSQ TSLSQTINQL SLCESEPSIA SSNTTTTTSN QGSGLPNLVP
NYSSDMRKKK LVNKFKRKVF GSKPKHLSSQ YEMDASSEEL GQHEQQPSMR FKTTLRKTSV
STNAENDHAS SLHEGNLRYK YNPSNDTYDV YDDTDSDSES DQNQDALTKP RKRDRIKRKI
RNSANKTAHH RPIHRTRDRK FNEDKPWKSH TDITFVTDNE RKRYESMWVS NRHRHLNLLS
WWPSITGDSG AINTLPEDGL ILGIIVRDIW KRSNLPNSLL AEIYTKVDTR KDGTLDRKSF
IVGMWLVDQC LYGRKLPNVV EQCVWDSVDR YASTTVVPVS TLKAMAKQKR KQMKEEIKNI
KKENRVVLVD HNSSS
