GLR1/YPL091W Protein Information

Standard Name	Glr1p
Systematic Name	Ypl091wp
Alias	Lpg17p
ORF Classification	Verified
Description	Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; mitochondrial but not cytosolic form has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress (1, 2, 3, 4)

Experimental Data
Molecules/cell	7600 5

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	483
Molecular Weight (Da)	53,441
Isoelectric Point (pI)	7.88

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Glr1p (InterPro)
Physical Interactions	There are 9 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012BC08 \| P41921 MIPS: YPL091W NCBI: 1151235 \| 149242065 \| 149242066 \| 1708060 \| 529102 \| 531000 \| 6325166 \| NP_015234.1 GenBank/EMBL/DDBJ: DAA11342.1 \| D37871 \| L35342 \| U43281
External Classifications	EC: 1.8.1.7 [Glutathione-disulfide reductase]

Amino Acid Sequence (or in FASTA format)
1 MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL 51 LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH 101 LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ 151 KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV 201 VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK 251 EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG 301 MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR 351 KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN 401 IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ 451 GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR*

Amino Acid Sequence (or in FASTA format)

       1  MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL
      51  LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH
     101  LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ
     151  KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV
     201  VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK
     251  EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG
     301  MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR
     351  KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN
     401  IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ
     451  GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR*

external links for Glr1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Glr1p

1)	Grant CM (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 39(3):533-41
2)	Outten CE and Culotta VC (2004) Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J Biol Chem 279(9):7785-91
3)	Outten CE, et al. (2005) Cellular factors required for protection from hyperoxia toxicity in Saccharomyces cerevisiae. Biochem J 388(Pt 1):93-101
4)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
5)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41