HSP12_YEAST
ID HSP12_YEAST Reviewed; 109 AA.
AC P22943; D6VTL5; Q8X145;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=12 kDa heat shock protein;
DE AltName: Full=Glucose and lipid-regulated protein;
GN Name=HSP12; Synonyms=GLP1, HOR5; OrderedLocusNames=YFL014W;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2129531; DOI=10.1016/0378-1119(90)90249-q;
RA Stone R.L., Matarese V., Magee B.B., Magee P.T., Bernlohr D.A.;
RT "Cloning, sequencing and chromosomal assignment of a gene from
RT Saccharomyces cerevisiae which is negatively regulated by glucose and
RT positively by lipids.";
RL Gene 96:171-176(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2175390; DOI=10.1007/bf00315801;
RA Praekelt U.M., Meacock P.A.;
RT "HSP12, a new small heat shock gene of Saccharomyces cerevisiae: analysis
RT of structure, regulation and function.";
RL Mol. Gen. Genet. 223:97-106(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Barrell B.G., Churcher C., Rajandream M.A.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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.
RC STRAIN=KBY001;
RA Sone H., Tomizuka K., Suda H., Iwamatsu A., Kondo K., Inouye M., Tanaka J.;
RT "Transcriptional regulation of bottom-fermenting yeast specific HSP12
RT gene.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ar5-H12 / Arvisionadu wine isolate;
RX PubMed=11816034; DOI=10.1002/yea.831.abs;
RA Zara S., Farris G.A., Budroni M., Bakalinsky A.T.;
RT "HSP12 is essential for biofilm formation by a Sardinian wine strain of
RT Saccharomyces cerevisiae.";
RL Yeast 19:269-276(2002).
RN [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-59; SER-73 AND
RP SER-97, AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-59; SER-73
RP AND SER-97, AND 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).
CC -!- FUNCTION: May play a role in a switch from carbohydrate utilizing
CC metabolism to fatty acid utilizing metabolism.
CC -!- INDUCTION: Strong, by heat shock, by entry in the stationary growth
CC phase, and by cAMP, probably via the activity of a cAMP-dependent
CC protein kinase. By glucose starvation and by fatty acids.
CC -!- MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To S.pombe hsp9 and C.albicans WH11. {ECO:0000305}.
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DR EMBL; M60827; AAA34647.1; -; Genomic_DNA.
DR EMBL; X55785; CAA39306.1; -; mRNA.
DR EMBL; Z46255; CAA86349.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09224.1; -; Genomic_DNA.
DR EMBL; D89864; BAA14033.1; -; Genomic_DNA.
DR EMBL; AY046957; AAL06077.1; -; Genomic_DNA.
DR EMBL; AY558464; AAS56790.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12425.1; -; Genomic_DNA.
DR PIR; S11179; HHBY12.
DR RefSeq; NP_116640.1; NM_001179952.1.
DR PDB; 2L9Q; NMR; -; A=1-109.
DR PDB; 2LJL; NMR; -; A=1-109.
DR PDB; 4AXP; NMR; -; A=1-109.
DR PDBsum; 2L9Q; -.
DR PDBsum; 2LJL; -.
DR PDBsum; 4AXP; -.
DR AlphaFoldDB; P22943; -.
DR BMRB; P22943; -.
DR SMR; P22943; -.
DR BioGRID; 31132; 66.
DR DIP; DIP-6408N; -.
DR IntAct; P22943; 5.
DR MINT; P22943; -.
DR STRING; 4932.YFL014W; -.
DR iPTMnet; P22943; -.
DR MaxQB; P22943; -.
DR PaxDb; P22943; -.
DR PRIDE; P22943; -.
DR TopDownProteomics; P22943; -.
DR EnsemblFungi; YFL014W_mRNA; YFL014W; YFL014W.
DR GeneID; 850532; -.
DR KEGG; sce:YFL014W; -.
DR SGD; S000001880; HSP12.
DR VEuPathDB; FungiDB:YFL014W; -.
DR eggNOG; ENOG502S44P; Eukaryota.
DR HOGENOM; CLU_102617_1_1_1; -.
DR InParanoid; P22943; -.
DR OMA; NKGVFQG; -.
DR BioCyc; YEAST:G3O-30442-MON; -.
DR PRO; PR:P22943; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P22943; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0007155; P:cell adhesion; IDA:SGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:SGD.
DR GO; GO:0071470; P:cellular response to osmotic stress; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0007009; P:plasma membrane organization; IMP:SGD.
DR InterPro; IPR007250; HSP9_HSP12.
DR PANTHER; PTHR28145; PTHR28145; 1.
DR Pfam; PF04119; HSP9_HSP12; 1.
DR PIRSF; PIRSF002590; HSP9/HSP12_fun; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..109
FT /note="12 kDa heat shock protein"
FT /id="PRO_0000084081"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT VARIANT 46
FT /note="P -> T (in strain: Ar5-H12)"
FT HELIX 8..17
FT /evidence="ECO:0007829|PDB:2L9Q"
FT HELIX 25..42
FT /evidence="ECO:0007829|PDB:2L9Q"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2L9Q"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:2L9Q"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2LJL"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2LJL"
FT HELIX 74..100
FT /evidence="ECO:0007829|PDB:2L9Q"
SQ SEQUENCE 109 AA; 11693 MW; 7C73862689759B4A CRC64;
MSDAGRKGFG EKASEALKPD SQKSYAEQGK EYITDKADKV AGKVQPEDNK GVFQGVHDSA
EKGKDNAEGQ GESLADQARD YMGAAKSKLN DAVEYVSGRV HGEEDPTKK
