P40092 (SPI1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Uncharacterized cell wall protein SPI1

Alternative name(s):
Stationary phase-induced protein 1

Gene names

Name:	SPI1
Ordered Locus Names:	YER150W

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

General annotation (Comments)

Function	Cell wall protein that plays a role in adaptation and resistance to cell wall stress. Ref.8
Subcellular location	Secreted › cell wall. Membrane; Lipid-anchor › GPI-anchor. Note: Covalently-linked GPI-modified cell wall protein (GPI-CWP). Ref.4 Ref.5
Induction	Induced by transcription factors MSN2 and MSN4 in stationary phase and by transcription factors MSN2, MSN4 and HAA1 upon weak-acid stress. Up-regulated by low pH. Ref.6 Ref.7 Ref.8
Post-translational modification	The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Sequence similarities	Belongs to the SED1 family.

Ontologies

Keywords
Cellular component	Cell wall Membrane Secreted
Domain	Signal
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to acid Inferred from mutant phenotype Ref.8. Source: SGD
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-KW fungal-type cell wall Inferred from direct assay Ref.4. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 127	108	Uncharacterized cell wall protein SPI1		PRO_0000014317
	Propeptide	128 – 148	21	Removed in mature form Potential		PRO_0000372448
Regions
	Compositional bias	61 – 124	64	Thr-rich
Amino acid modifications
	Lipidation	127	1	GPI-anchor amidated asparagine Potential
	Glycosylation	41	1	N-linked (GlcNAc...) Potential
	Glycosylation	59	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P40092 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: F65B20225FE2A5ED	FASTA	148	14,996
	10 20 30 40 50 60 MLSNAKLLLS LAMASTALGL VSNSSSSVIV VPSSDATIAG NDTATPAPEP SSAAPIFYNS 70 80 90 100 110 120 TATATQYEVV SEFTTYCPEP TTFVTNGATF TVTAPTTLTI TNCPCTIEKP TSETSVSSTH 130 140 DVETNSNAAN ARAIPGALGL AGAVMMLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall proteins in Saccharomyces cerevisiae." Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K. Mol. Gen. Genet. 258:53-59(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins." Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K. J. Bacteriol. 181:3886-3889(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Stress response and expression patterns in wine fermentations of yeast genes induced at the diauxic shift." Puig S., Perez-Ortin J.E. Yeast 16:139-148(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[7]	"Low external pH induces HOG1-dependent changes in the organization of the Saccharomyces cerevisiae cell wall." Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H., Van Den Ende H., Klis F.M. Mol. Microbiol. 39:469-479(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[8]	"The SPI1 gene, encoding a glycosylphosphatidylinositol-anchored cell wall protein, plays a prominent role in the development of yeast resistance to lipophilic weak-acid food preservatives." Simoes T., Mira N.P., Fernandes A.R., Sa-Correia I. Appl. Environ. Microbiol. 72:7168-7175(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18917 Genomic DNA. Translation: AAB64677.1. AY557784 Genomic DNA. Translation: AAS56110.1. BK006939 Genomic DNA. Translation: DAA07811.1.
PIR	S50653.
RefSeq	NP_011077.1. NM_001179040.1.
3D structure databases
ProteinModelPortal	P40092.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2064N.
IntAct	P40092. 3 interactions.
MINT	MINT-556565.
STRING	4932.YER150W.
Proteomic databases
PaxDb	P40092.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER150W; YER150W; YER150W.
GeneID	856893.
KEGG	sce:YER150W.
Organism-specific databases
CYGD	YER150w.
SGD	S000000952. SPI1.
Phylogenomic databases
eggNOG	NOG78166.
GeneTree	ENSGT00700000105795.
OrthoDB	EOG4MPN0Z.
Gene expression databases
Genevestigator	P40092.
GermOnline	YER150W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	983302.

Entry information

Entry name

SPI1_YEAST

Accession

Primary (citable) accession number: P40092
Secondary accession number(s): D3DM57

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program