| General information | | DisProt: | DP00705 | | Name: | 12 kDa heat shock protein | | Synonym(s): | HSP12_YEAST
Glucose and lipid-regulated protein
| | First appeared in release: | Release 5.6 (01/10/2011) | | UniProt: | P22943 | | UniGene: | | | SwissProt: | HSP12_YEAST | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Saccharomyces cerevisiae (Baker\'s yeast) | | Sequence length: | 109 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSDAGRKGFG EKASEALKPD SQKSYAEQGK EYITDKADKV AGKVQPEDNK GVFQGVHDSA - 60
EKGKDNAEGQ GESLADQARD YMGAAKSKLN DAVEYVSGRV HGEEDPTKK
|
| Functional narrative |
Function: May play a role in a switch from carbohydrate utilizing metabolism to fatty acid utilizing metabolism. P31787:ACB1; NbExp=1; IntAct=EBI-8548, EBI-2060; P54113:ADE16; NbExp=1; IntAct=EBI-8548, EBI-14213; P54783:ALO1; NbExp=1; IntAct=EBI-8548, EBI-2519; P12962:CAF20; NbExp=1; IntAct=EBI-8548, EBI-9010; P14832:CPR1; NbExp=1; IntAct=EBI-8548, EBI-5463; P36156:ECM4; NbExp=1; IntAct=EBI-8548, EBI-2042717; Q07651:FMP45; NbExp=1; IntAct=EBI-8548, EBI-2051056; P33892:GCN1; NbExp=1; IntAct=EBI-8548, EBI-7442; Q05584:GLO2; NbExp=1; IntAct=EBI-8548, EBI-7672; Q07653:HBT1; NbExp=1; IntAct=EBI-8548, EBI-35419; Q6Q5K6:HUG1; NbExp=1; IntAct=EBI-8548, EBI-392766; P11986:INO1; NbExp=1; IntAct=EBI-8548, EBI-9257; P46673:NUP85; NbExp=1; IntAct=EBI-8548, EBI-12345; P10963:PCK1; NbExp=1; IntAct=EBI-8548, EBI-13770; P37012:PGM2; NbExp=1; IntAct=EBI-8548, EBI-13296; P21243:SCL1; NbExp=1; IntAct=EBI-8548, EBI-13975; P33338:SLA2; NbExp=1; IntAct=EBI-8548, EBI-17323; P33328:SNC2; NbExp=1; IntAct=EBI-8548, EBI-17512; P33315:TKL2; NbExp=1; IntAct=EBI-8548, EBI-19297; P28274:URA7; NbExp=1; IntAct=EBI-8548, EBI-20128; P41807:VMA13; NbExp=1; IntAct=EBI-8548, EBI-20281; P39111:VMA7; NbExp=1; IntAct=EBI-8548, EBI-20272; Q12402:YOP1; NbExp=1; IntAct=EBI-8548, EBI-37092;
INDUCTION: Strong, by heat shock, by entry in the stationary growth phase, and by cAMP, probably via the activity of a cAMP- dependent protein kinase. By glucose starvation and by fatty acids.
MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
SIMILARITY: To S.pombe hsp9 and C.albicans WH11.
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|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 7 | | Length: | 7 | | Region sequence: |
MSDAGRK | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Hsp12; SDS 300 mM; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts))
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| Region 2 | | Type: | Disordered w/ Residual Structure | | Name: | Helix 1 | | Location: | 8 - 18 | | Length: | 11 | | Region sequence: |
GFGEKASEALK | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| Region 3 | | Type: | Disordered | | Name: | | | Location: | 19 - 23 | | Length: | 5 | | Region sequence: |
PDSQK | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| Region 4 | | Type: | Disordered w/ Residual Structure | | Name: | Helix 2 | | Location: | 24 - 43 | | Length: | 20 | | Region sequence: |
SYAEQGKEYITDKADKVAGK | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| Region 5 | | Type: | Disordered | | Name: | | | Location: | 44 - 73 | | Length: | 30 | | Region sequence: |
VQPEDNKGVFQGVHDSAEKGKDNAEGQGES | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (310 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.4; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:According to Welker et al (2010), Region 5 contains a predicted disorder-to-order helix (Helix 3) at aa 52-61.
|
| Region 6 | | Type: | Disordered w/ Residual Structure | | Name: | Helix 4 | | Location: | 74 - 98 | | Length: | 25 | | Region sequence: |
LADQARDYMGAAKSKLNDAVEYVSG | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.5; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| Region 7 | | Type: | Disordered | | Name: | | | Location: | 99 - 109 | | Length: | 11 | | Region sequence: |
RVHGEEDPTKK | | Modification type: | Monomeric
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | | | Functional subclasses: | Protein-lipid interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7.4; Hsp12 0.13 uM; NaH2PO4 (buffer) 10 mM; SDS (in absence or presence of) 10 mM; SUV-DMPG (in absence or presence of) 4.3 mM)
- Nuclear magnetic resonance (NMR) (310 K; pH: 7.4; Gd (DTPA-BMA) (paramagnetic agent, in increasing amts); Hsp12; SDS 300 mM)
| References:
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
| Comments:
|
| References |
- Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. "Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function." Mol. Cell. 2010; 39(4): 507-20. PubMed: 20797624
|
| Comments |
AV 2/03/2011 (PubMed: 20797624)
Welker et al (2010) found that Hsp12 is a monomeric and fully disordered protein that gains structure when associating with negatively charged lipids. High concentrations of Hsp12 (such as in stress conditions) led to membrane association for the purpose of membrane stabilization.
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