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3.E.1.4.6
Possible chaperone membrane protein related to Hsp30, Mrh1 (320 aas; 33% identical to Hsp30p). This protein and its two paralogues, Hsp30 and YR02, are induced by heat shock and are present primarily in the plasma membrane (Wu et al. 2000).  It plays a role in acetic acid tolerance and may be an acetic acid exporter (Takabatake et al. 2015).

Accession Number:Q12117
Protein Name:Protein MRH1
Length:320
Molecular Weight:36191.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Acetic acid

Cross database links:

Genevestigator: Q12117
eggNOG: fuNOG11168
HEGENOM: HBG395442
Entrez Gene ID: 851597   
Pfam: PF01036   
KEGG: sce:YDR033W   

Gene Ontology

GO:0005933 C:cellular bud
GO:0016021 C:integral to membrane
GO:0005739 C:mitochondrion
GO:0005886 C:plasma membrane
GO:0001950 C:plasma membrane enriched fraction
GO:0005216 F:ion channel activity

References (15)

[1] “The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.”  Jacq C.et.al.   9169867
[2] “Expression and subcellular localization of a membrane protein related to Hsp30p in Saccharomyces cerevisiae.”  Wu K.et.al.   10675524
[3] “Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.”  Ficarro S.B.et.al.   11875433
[4] “Subproteomics: identification of plasma membrane proteins from the yeast Saccharomyces cerevisiae.”  Navarre C.et.al.   12469340
[5] “Global analysis of protein localization in budding yeast.”  Huh W.-K.et.al.   14562095
[6] “Global analysis of protein expression in yeast.”  Ghaemmaghami S.et.al.   14562106
[7] “A proteomics approach to understanding protein ubiquitination.”  Peng J.et.al.   12872131
[8] “The proteome of Saccharomyces cerevisiae mitochondria.”  Sickmann A.et.al.   14576278
[9] “Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.”  Gruhler A.et.al.   15665377
[10] “A global topology map of the Saccharomyces cerevisiae membrane proteome.”  Kim H.et.al.   16847258
[11] “Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.”  Li X.et.al.   17330950
[12] “Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.”  Reinders J.et.al.   17761666
[13] “Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.”  Chi A.et.al.   17287358
[14] “Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.”  Smolka M.B.et.al.   17563356
[15] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSTFETLIKR GGNEAIKINP PTGADFHITS RGSDWFWTCF CCYLLFGLIL TFLMFRKPVN 
61:	DRFFYLTGIA PNFFMCIAYF TMASNLGWIP VKAKYNHVQT STQKEHPGYR QIFYSRFVGW 
121:	FLALPWPIIQ ICMLAGTPFW QMAFNVCITE FFTVCWLIAA CVHSTYKWGY YTIGLGAAIV 
181:	VSISVMTTSY NLVKQRDNDI RLTFLVFFSI IMFLWIIAYP TCFGITDGGN VLQPDSAGIF 
241:	YGIIDLILMC FIPTLLVPIA NHFGADKLGY HFGPSDAEAV MAPKAPVASP RPAATPNLSK 
301:	DKKKKSKKSK KSKKSKKSEE