XBP1_YEAST
ID XBP1_YEAST Reviewed; 647 AA.
AC P40489; D6VVI7; Q12688;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcriptional repressor XBP1;
DE AltName: Full=XhoI site-binding protein 1;
GN Name=XBP1; OrderedLocusNames=YIL101C;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-241.
RC STRAIN=SPX101-1C;
RX PubMed=3141213; DOI=10.1016/0014-5793(88)80912-8;
RA Pardo J.M., Ianez E., Zalacain M., Claros M.G., Jimenez A.;
RT "Similar short elements in the 5' regions of the STA2 and SGA genes from
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 239:179-184(1988).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=9343412; DOI=10.1128/mcb.17.11.6491;
RA Mai B., Breeden L.;
RT "Xbp1, a stress-induced transcriptional repressor of the Saccharomyces
RT cerevisiae Swi4/Mbp1 family.";
RL Mol. Cell. Biol. 17:6491-6501(1997).
RN [5]
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 [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).
CC -!- FUNCTION: Transcriptional repressor which binds to the consensus
CC sequence 5'-GCCTCGA[G/A]G[C/A]-3'. Represses CLN1 transcription.
CC {ECO:0000269|PubMed:9343412}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: By heat shock, high osmolarity, oxidative stress, DNA damage
CC and glucose starvation. {ECO:0000269|PubMed:9343412}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z38125; CAA86279.1; -; Genomic_DNA.
DR EMBL; X13858; CAA32070.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006942; DAA08453.1; -; Genomic_DNA.
DR PIR; S48471; S48471.
DR RefSeq; NP_012165.1; NM_001179449.1.
DR AlphaFoldDB; P40489; -.
DR BioGRID; 34891; 74.
DR DIP; DIP-7587N; -.
DR IntAct; P40489; 5.
DR MINT; P40489; -.
DR STRING; 4932.YIL101C; -.
DR iPTMnet; P40489; -.
DR PaxDb; P40489; -.
DR PRIDE; P40489; -.
DR EnsemblFungi; YIL101C_mRNA; YIL101C; YIL101C.
DR GeneID; 854706; -.
DR KEGG; sce:YIL101C; -.
DR SGD; S000001363; XBP1.
DR VEuPathDB; FungiDB:YIL101C; -.
DR eggNOG; ENOG502S1IW; Eukaryota.
DR HOGENOM; CLU_451446_0_0_1; -.
DR InParanoid; P40489; -.
DR OMA; CESWYLA; -.
DR BioCyc; YEAST:G3O-31358-MON; -.
DR PRO; PR:P40489; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40489; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:SGD.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..647
FT /note="Transcriptional repressor XBP1"
FT /id="PRO_0000066004"
FT DOMAIN 282..395
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT DNA_BIND 318..339
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 138..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 106..107
FT /note="LL -> FV (in Ref. 3; CAA32070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 72687 MW; 5087D00C1D1AC4A5 CRC64;
MKYPAFSINS DTVHLTDNPL DDYQRLYLVS VLDRDSPPAS FSAGLNIRKV NYKSSIAAQF
THPNFIISAR DAGNGEEAAA QNVLNCFEYQ FPNLQTIQSL VHEQTLLSQL ASSATPHSAL
HLHDKNILMG KIILPSRSNK TPVSASPTKQ EKKALSTASR ENATSSLTKN QQFKLTKMDH
NLINDKLINP NNCVIWSHDS GYVFMTGIWR LYQDVMKGLI NLPRGDSVST SQQQFFCKAE
FEKILSFCFY NHSSFTSEES SSVLLSSSTS SPPKRRTSTG STFLDANASS SSTSSTQANN
YIDFHWNNIK PELRDLICQS YKDFLINELG PDQIDLPNLN PANFTKRIRG GYIKIQGTWL
PMEISRLLCL RFCFPIRYFL VPIFGPDFPK DCESWYLAHQ NVTFASSTTG AGAATAATAA
ANTSTNFTST AVARPRQKPR PRPRQRSTSM SHSKAQKLVI EDALPSFDSF VENLGLSSND
KNFIKKNSKR QKSSTYTSQT SSPIGPRDPT VQILSNLASF YNTHGHRYSY PGNIYIPQQR
YSLPPPNQLS SPQRQLNYTY DHIHPVPSQY QSPRHYNVPS SPIAPAPPTF PQPYGDDHYH
FLKYASEVYK QQNQRPAHNT NTNMDTSFSP RANNSLNNFK FKTNSKQ