P41277 (GPP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
(DL)-glycerol-3-phosphatase 1
EC=3.1.3.-

Alternative name(s):
Related to HOR2 protein 2

Gene names

Name:	RHR2
Synonyms:	GPP1
Ordered Locus Names:	YIL053W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Major isoform of DL-glycerol-3-phosphatase involved in glycerol biosynthesis. Plays a role in osmoadaptation and required for adaptation to anaerobic conditions. Ref.5 Ref.10 Ref.15 Ref.16 Ref.18
Catalytic activity	Glycerol 3-phosphate + H2O = glycerol + phosphate.
Subunit structure	Monomer.
Subcellular location	Cytoplasm. Nucleus Ref.11.
Induction	In response to both anaerobic and osmotic stress. Expression seems to be under the control of YIG1. Ref.9 Ref.10 Ref.13 Ref.16 Ref.19 Ref.21
Disruption phenotype	Leads to osmosensitivity. Ref.8
Miscellaneous	Present with 193000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the DOG/GPP family.
Sequence caution	The sequence CAA86169.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Hydrolase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycerol biosynthetic process Inferred from mutant phenotype Ref.10. Source: SGD response to osmotic stress Traceable author statement PubMed 11676566. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.11. Source: SGD nucleus Inferred from direct assay Ref.11. Source: SGD
Molecular_function	glycerol-1-phosphatase activity Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YIG1	Q08956	3	EBI-7829,EBI-30385

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 250

249

(DL)-glycerol-3-phosphatase 1

PRO_0000087560

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.20

Modified residue

58

1

Phosphothreonine Ref.17

Cross-link

64

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Experimental info

Sequence conflict

91

1

I → IK AA sequence Ref.4

Secondary structure

1

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250

Helix Strand Turn

Details...

Beta strand

6 – 17

12

Turn

21 – 23

3

Helix

27 – 38

12

Helix

46 – 52

7

Helix

58 – 65

8

Helix

67 – 69

3

Helix

72 – 80

9

Helix

82 – 86

5

Helix

96 – 104

9

Helix

108 – 110

3

Beta strand

111 – 114

4

Helix

119 – 129

11

Beta strand

135 – 138

4

Helix

140 – 142

3

Helix

151 – 159

9

Helix

169 – 171

3

Beta strand

174 – 180

7

Helix

181 – 189

9

Beta strand

193 – 201

9

Helix

203 – 206

4

Beta strand

212 – 217

6

Helix

218 – 220

3

Beta strand

221 – 223

3

Turn

228 – 231

4

Beta strand

232 – 238

7

Beta strand

241 – 243

3

Turn

245 – 248

4

Sequences

	Sequence		Length	Mass (Da)
	P41277 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9494B158A937413C	FASTA	250	27,947
	10 20 30 40 50 60 MPLTTKPLSL KINAALFDVD GTIIISQPAI AAFWRDFGKD KPYFDAEHVI HISHGWRTYD 70 80 90 100 110 120 AIAKFAPDFA DEEYVNKLEG EIPEKYGEHS IEVPGAVKLC NALNALPKEK WAVATSGTRD 130 140 150 160 170 180 MAKKWFDILK IKRPEYFITA NDVKQGKPHP EPYLKGRNGL GFPINEQDPS KSKVVVFEDA 190 200 210 220 230 240 PAGIAAGKAA GCKIVGIATT FDLDFLKEKG CDIIVKNHES IRVGEYNAET DEVELIFDDY 250 LYAKDDLLKW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of seven cDNAs for hyperosmolarity-responsive (HOR) genes of Saccharomyces cerevisiae." Hirayama T., Maeda T., Saito H., Shinozaki K. Mol. Gen. Genet. 249:127-138(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: RS16.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 86-97 AND 173-188. Strain: ATCC 204508 / S288c.
[5]	"Purification and characterization of two isoenzymes of DL-glycerol-3-phosphatase from Saccharomyces cerevisiae. Identification of the corresponding GPP1 and GPP2 genes and evidence for osmotic regulation of Gpp2p expression by the osmosensing mitogen-activated protein kinase signal transduction pathway." Norbeck J., Paehlman A.-K., Akhtar N., Blomberg A., Adler L. J. Biol. Chem. 271:13875-13881(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, CHARACTERIZATION.
[6]	"Metabolic and regulatory changes associated with growth of Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol dissimilation via the dihydroxyacetone pathway." Norbeck J., Blomberg A. J. Biol. Chem. 272:5544-5554(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Strain: ATCC 44827 / SKQ2N.
[7]	"Identification of two-dimensional gel electrophoresis resolved yeast proteins by matrix-assisted laser desorption ionization mass spectrometry." Larsson T., Norbeck J., Karlsson H., Karlsson K.-A., Blomberg A. Electrophoresis 18:418-423(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"The control of intracellular glycerol in Saccharomyces cerevisiae influences osmotic stress response and resistance to increased temperature." Siderius M., Van Wuytswinkel O., Reijenga K.A., Kelders M., Mager W.H. Mol. Microbiol. 36:1381-1390(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[9]	"Microaerobic glycerol formation in Saccharomyces cerevisiae." Costenoble R., Valadi H., Gustafsson L., Niklasson C., Franzen C.J. Yeast 16:1483-1495(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[10]	"The yeast glycerol 3-phosphatases Gpp1p and Gpp2p are required for glycerol biosynthesis and differentially involved in the cellular responses to osmotic, anaerobic, and oxidative stress." Pahlman A.K., Granath K., Ansell R., Hohmann S., Adler L. J. Biol. Chem. 276:3555-3563(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[11]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]	"Molecular basis for anaerobic growth of Saccharomyces cerevisiae on xylose, investigated by global gene expression and metabolic flux analysis." Sonderegger M., Jeppsson M., Hahn-Hagerdal B., Sauer U. Appl. Environ. Microbiol. 70:2307-2317(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[14]	"Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses." Zhou W., Ryan J.J., Zhou H. J. Biol. Chem. 279:32262-32268(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64, MASS SPECTROMETRY.
[15]	"Engineering of Saccharomyces cerevisiae for the production of L-glycerol 3-phosphate." Nguyen H.T., Dieterich A., Athenstaedt K., Truong N.H., Stahl U., Nevoigt E. Metab. Eng. 6:155-163(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"The YIG1 (YPL201c) encoded protein is involved in regulating anaerobic glycerol metabolism in Saccharomyces cerevisiae." Granath K., Modig T., Forsmark A., Adler L., Liden G. Yeast 22:1257-1268(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[17]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, MASS SPECTROMETRY.
[18]	"Fermentative production of L-glycerol 3-phosphate utilizing a Saccharomyces cerevisiae strain with an engineered glycerol biosynthetic pathway." Popp A., Nguyen H.T., Boulahya K., Bideaux C., Alfenore S., Guillouet S.E., Nevoigt E. Biotechnol. Bioeng. 100:497-505(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Central carbon metabolism of Saccharomyces cerevisiae in anaerobic, oxygen-limited and fully aerobic steady-state conditions and following a shift to anaerobic conditions." Wiebe M.G., Rintala E., Tamminen A., Simolin H., Salusjarvi L., Toivari M., Kokkonen J.T., Kiuru J., Ketola R.A., Jouhten P., Huuskonen A., Maaheimo H., Ruohonen L., Penttila M. FEMS Yeast Res. 8:140-154(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[20]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
[21]	"Metabolic regulation rather than de novo enzyme synthesis dominates the osmo-adaptation of yeast." Bouwman J., Kiewiet J., Lindenbergh A., van Eunen K., Siderius M., Bakker B.M. Yeast 28:43-53(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[22]	"The crystal structure of an isoform of dl-glycerol-3-phosphatase, rhr2p from saccharomyces cerevisiae." Midwest center for structural genomics (MCSG) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D50471 mRNA. Translation: BAA09060.1.
Z38060 Genomic DNA. Translation: CAA86169.1. Different initiation.
BK006942 Genomic DNA. Translation: DAA08494.1.

PIR

S48426.

RefSeq

NP_012211.2. NM_001179403.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QLT	X-ray	1.60	A	1-250	[»]

ProteinModelPortal

P41277.

SMR

P41277. Positions 1-250.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4713N.

IntAct

P41277. 11 interactions.

MINT

MINT-487007.

Proteomic databases

PaxDb

P41277.

PeptideAtlas

P41277.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YIL053W; YIL053W; YIL053W.

GeneID

854758.

KEGG

sce:YIL053W.

Organism-specific databases

SGD

S000001315. RHR2.

Phylogenomic databases

eggNOG

COG0637.

GeneTree

ENSGT00530000065392.

HOGENOM

HOG000248341.

KO

K06116.

OMA

ITETHAT.

OrthoDB

EOG4NGKWQ.

Gene expression databases

ArrayExpress

P41277.

Genevestigator

P41277.

GermOnline

YIL053W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.

InterPro

IPR023214. HAD-like_dom.
IPR006402. HAD-SF_hydro_IA_v3.
IPR023198. PGP_dom2.
[Graphical view]

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR01509. HAD-SF-IA-v3. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P41277.

NextBio

977496.

Entry information

Entry name

GPP1_YEAST

Accession

Primary (citable) accession number: P41277
Secondary accession number(s): D6VVM8, P38012

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program