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Reviewed, UniProtKB/Swiss-Prot P32478 (HS150_YEAST)

Last modified December 15, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cell wall mannoprotein HSP150
Alternative name(s):
    150 kDa heat shock glycoprotein
    Protein with internal repeats 2
    Covalently-linked cell wall protein 7
Gene names
Name: HSP150
Synonyms: CCW7, ORE1, PIR2
Ordered Locus Names: YJL159W
ORF Names: J0558
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents and for tolerance to heat shock. Ref.12 Ref.13 Ref.15 Ref.18

Subcellular location

Secretedcell wall. Note: Covalently attached to the cell wall. Ref.12 Ref.13 Ref.5 Ref.20

Induction

Positively regulated by signaling through MPK1 in response to cell wall perturbation. Induced by heat shock and nitrogen starvation. Expression is also regulated by the ACE2 and SWI5 transcription factors. Ref.12 Ref.14 Ref.16 Ref.19 Ref.22

Domain

The PIR1/2/3 repeats are required for the covalent linkage to the cell wall By similarity. Their number varies among different strains of S.cerevisiae.

Post-translational modification

Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensitive ester linkage between the gamma-carboxyl group of glutamic acids, arising from specific glutamines within the PIR1/2/3 repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains By similarity.

The propeptide is cleaved off in the late Golgi. While both peptides are secreted, only a fraction of the mature glycoprotein is incorporated into the cell wall. Ref.5

O-glycosylated. Extensively O-mannosylated. Ref.5

Miscellaneous

Present with 14600 molecules/cell in log phase SD medium. Ref.17

Sequence similarities

Belongs to the PIR protein family.

Contains 11 PIR1/2/3 repeats.

Sequence caution

The sequence CAA89454.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.5 Ref.1
Propeptide19 – 7254
PRO_0000033260
Chain73 – 413341Cell wall mannoprotein HSP150
PRO_0000033261

Regions

Repeat73 – 8917PIR1/2/3 1
Repeat97 – 11519PIR1/2/3 2
Repeat116 – 13419PIR1/2/3 3
Repeat140 – 15819PIR1/2/3 4
Repeat164 – 18219PIR1/2/3 5
Repeat188 – 20619PIR1/2/3 6
Repeat207 – 22519PIR1/2/3 7
Repeat226 – 24419PIR1/2/3 8
Repeat245 – 26319PIR1/2/3 9
Repeat264 – 28219PIR1/2/3 10
Repeat283 – 30018PIR1/2/3 11

Sites

Site72 – 732Cleavage; by KEX2
Site811Covalent attachment to cell wall glycan By similarity
Site1071Covalent attachment to cell wall glycan By similarity
Site1261Covalent attachment to cell wall glycan By similarity
Site1501Covalent attachment to cell wall glycan By similarity
Site1741Covalent attachment to cell wall glycan By similarity
Site1981Covalent attachment to cell wall glycan By similarity
Site2171Covalent attachment to cell wall glycan By similarity
Site2361Covalent attachment to cell wall glycan By similarity
Site2551Covalent attachment to cell wall glycan By similarity
Site2741Covalent attachment to cell wall glycan By similarity
Site2921Covalent attachment to cell wall glycan By similarity

Natural variations

Natural variant961T → S in strain: B1, TD04/1a and TD04/1b. Ref.6
Natural variant116 – 16348Missing in strain: B1, TD04/1a and TD04/1b.
Natural variant1751V → I in strain: TD04/1a and TD04/1b. Ref.6
Natural variant1761Q → QAATTTASVSTKSSAAAVSQ IGDGQIQATTKTTAAAVSQI GDGQIQ in strain: TD04/1b.
Natural variant1991V → I in strain: B1, TD04/1a and TD04/1b. Ref.6
Natural variant226 – 24419Missing in strain: B1, TD04/1a and TD04/1b.
Natural variant2971T → S in strain: B1, TD04/1a and TD04/1b. Ref.6

Experimental info

Sequence conflict471G → A in BAA02886. Ref.3
Sequence conflict121 – 1233QIG → R in CAA89454. Ref.4
Sequence conflict152 – 17524Missing in CAA89454. Ref.4
Sequence conflict2111S → F in AAA17683. Ref.1
Sequence conflict2111S → F in AAB23364. Ref.2
Sequence conflict2191Q → L in AAA17683. Ref.1
Sequence conflict2191Q → L in AAB23364. Ref.2
Sequence conflict2261A → R in AAA17683. Ref.1
Sequence conflict2261A → R in AAB23364. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32478-1 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 5EAF10136E25132A

FASTA41341,059
        10         20         30         40         50         60 
MQYKKTLVAS ALAATTLAAY APSEPWSTLT PTATYSGGVT DYASTFGIAV QPISTTSSAS 

        70         80         90        100        110        120 
SAATTASSKA KRAASQIGDG QVQAATTTAS VSTKSTAAAV SQIGDGQIQA TTKTTAAAVS 

       130        140        150        160        170        180 
QIGDGQIQAT TKTTSAKTTA AAVSQISDGQ IQATTTTLAP KSTAAAVSQI GDGQVQATTT 

       190        200        210        220        230        240 
TLAPKSTAAA VSQIGDGQVQ ATTKTTAAAV SQIGDGQVQA TTKTTAAAVS QIGDGQVQAT 

       250        260        270        280        290        300 
TKTTAAAVSQ IGDGQVQATT KTTAAAVSQI TDGQVQATTK TTQAASQVSD GQVQATTATS 

       310        320        330        340        350        360 
ASAAATSTDP VDAVSCKTSG TLEMNLKGGI LTDGKGRIGS IVANRQFQFD GPPPQAGAIY 

       370        380        390        400        410 
AAGWSITPDG NLAIGDNDVF YQCLSGTFYN LYDEHIGSQC TPVHLEAIDL IDC 

« Hide

References

« Hide 'large scale' references
[1]"A heat shock gene from Saccharomyces cerevisiae encoding a secretory glycoprotein."
Russo P., Kalkkinen N., Sareneva H., Paakkola J., Makarow M.
Proc. Natl. Acad. Sci. U.S.A. 89:3671-3675(1992) [PubMed: 1570286] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 19-39; 73-94; 114-132; 243-261; 346-370 AND 390-412.
[2]Erratum
Russo P., Kalkkinen N., Sareneva H., Paakkola J., Makarow M.
Proc. Natl. Acad. Sci. U.S.A. 89:8857-8857(1992) [PubMed: 1528903] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock."
Toh-e A., Yasunaga S., Nisogi H., Tanaka K., Oguchi T., Matsui Y.
Yeast 9:481-494(1993) [PubMed: 8322511] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RAY-3AD.
[4]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[5]"Specific labelling of cell wall proteins by biotinylation. Identification of four covalently linked O-mannosylated proteins of Saccharomyces cerevisiae."
Mrsa V., Seidl T., Gentzsch M., Tanner W.
Yeast 13:1145-1154(1997) [PubMed: 9301021] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-29 AND 73-87, CLEAVAGE BY KEX2, GLYCOSYLATION, SUBCELLULAR LOCATION.
[6]"Characterization of Ccw7p cell wall proteins and the encoding genes of Saccharomyces cerevisiae wine yeast strains: relevance for flor formation."
Kovacs M., Stuparevic I., Mrsa V., Maraz A.
FEMS Yeast Res. 8:1115-1126(2008) [PubMed: 18657192] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-393, PROTEIN SEQUENCE OF 73-84, VARIANTS SER-96; 116-ALA--THR-163 DEL ILE-175; ILE-199; 226-ALA--THR-244 DEL AND SER-297.
Strain: B1, TD04/1a and TD04/1b.
[7]"Two-dimensional analysis of proteins secreted by Saccharomyces cerevisiae regenerating protoplasts: a novel approach to study the cell wall."
Pardo M., Monteoliva L., Pla J., Sanchez M., Gil C., Nombela C.
Yeast 15:459-472(1999) [PubMed: 10234784] [Abstract]
Cited for: PROTEIN SEQUENCE OF 73-82.
[8]"Minisatellites in Saccharomyces cerevisiae genes encoding cell wall proteins: a new way towards wine strain characterisation."
Marinangeli P., Angelozzi D., Ciani M., Clementi F., Mannazzu I.
FEMS Yeast Res. 4:427-435(2004) [PubMed: 14734023] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-366.
Strain: ATCC 204508 / S288c.
[9]"YJL159w does encode Pir2/Hsp150."
Moukadiri I., Zueco J.
Yeast 18:323-324(2001) [PubMed: 11223941] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 267-413.
Strain: ATCC 204508 / S288c.
[10]"Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii."
Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P.
Genome Biol. 4:R45.1-R45.13(2003) [PubMed: 12844361] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 289-406.
Strain: ATCC 204511 / S288c / AB972.
[11]"A proteomic approach for the study of Saccharomyces cerevisiae cell wall biogenesis."
Pardo M., Ward M., Bains S., Molina M., Blackstock W., Gil C., Nombela C.
Electrophoresis 21:3396-3410(2000) [PubMed: 11079560] [Abstract]
Cited for: PROTEIN SEQUENCE OF 318-327 AND 338-345.
[12]"Stress proteins on the yeast cell surface determine resistance to osmotin, a plant antifungal protein."
Yun D.-J., Zhao Y., Pardo J.M., Narasimhan M.L., Damsz B., Lee H., Abad L.R., D'Urzo M.P., Hasegawa P.M., Bressan R.A.
Proc. Natl. Acad. Sci. U.S.A. 94:7082-7087(1997) [PubMed: 9192695] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[13]"The contribution of the O-glycosylated protein Pir2p/Hsp150 to the construction of the yeast cell wall in wild-type cells and beta 1,6-glucan-deficient mutants."
Kapteyn J.C., Van Egmond P., Sievi E., Van Den Ende H., Makarow M., Klis F.M.
Mol. Microbiol. 31:1835-1844(1999) [PubMed: 10209754] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Genome-wide analysis of gene expression regulated by the yeast cell wall integrity signalling pathway."
Jung U.S., Levin D.E.
Mol. Microbiol. 34:1049-1057(1999) [PubMed: 10594829] [Abstract]
Cited for: INDUCTION.
[15]"Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall."
Mrsa V., Tanner W.
Yeast 15:813-820(1999) [PubMed: 10407261] [Abstract]
Cited for: FUNCTION.
[16]"Overlapping and distinct roles of the duplicated yeast transcription factors Ace2p and Swi5p."
Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.
Mol. Microbiol. 40:422-432(2001) [PubMed: 11309124] [Abstract]
Cited for: INDUCTION.
[17]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]"Increased mortality of Saccharomyces cerevisiae cell wall protein mutants."
Teparic R., Stuparevic I., Mrsa V.
Microbiology 150:3145-3150(2004) [PubMed: 15470095] [Abstract]
Cited for: FUNCTION.
[19]"Characterization of the transcriptional response to cell wall stress in Saccharomyces cerevisiae."
Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S., Hellingwerf K.J., Klis F.M.
Yeast 21:413-427(2004) [PubMed: 15116342] [Abstract]
Cited for: INDUCTION.
[20]"Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages."
Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M., de Koster C.G.
J. Biol. Chem. 280:20894-20901(2005) [PubMed: 15781460] [Abstract]
Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[21]"Intragenic tandem repeats generate functional variability."
Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.
Nat. Genet. 37:986-990(2005) [PubMed: 16086015] [Abstract]
Cited for: REPEATS.
[22]"Mass spectrometric quantitation of covalently bound cell wall proteins in Saccharomyces cerevisiae."
Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.
FEMS Yeast Res. 7:887-896(2007) [PubMed: 17617218] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

M88698 Unassigned DNA. Translation: AAA17683.1.
S45000 Genomic DNA. Translation: AAB23364.1.
D13741 Genomic DNA. Translation: BAA02886.1.
Z49434 Genomic DNA. Translation: CAA89454.1. Sequence problems.
EU220722 Genomic DNA. Translation: ABY67720.1.
EU220723 Genomic DNA. Translation: ABY67721.1.
EU220724 Genomic DNA. Translation: ABY67722.1.
AY321583 Genomic DNA. Translation: AAQ83898.1.
AY260881 Genomic DNA. Translation: AAP21749.1.
PIRA46183.
S56942.
RefSeqNP_012376.3.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2035N.
IntActP32478. 6 interactions.
STRINGP32478.

2-D gel databases

COMPLUYEAST-2DPAGEP32478.

Proteomic databases

PeptideAtlasP32478.

Genome annotation databases

EnsemblYJL159W; YJL159W; YJL159W; Saccharomyces cerevisiae. [Genome view]
GeneID853281.
KEGGsce:YJL159W.

Organism-specific databases

CYGDYJL159w.
SGDS000003695. HSP150.

Phylogenomic databases

OrthoDBEOG9JDJQC.

Gene expression databases

ArrayExpressP32478.
GenevestigatorP32478.
GermOnlineYJL159W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000420. Yeast_PIR.
[Graphical view]
PfamPF00399. PIR. 11 hits.
[Graphical view]
PROSITEPS00929. PIR_REPEAT_1. 11 hits.
PS50256. PIR_REPEAT_2. 11 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio973573.

Entry information

Entry nameHS150_YEAST
AccessionPrimary (citable) accession number: P32478
Secondary accession number(s): B6RI02 expand/collapse secondary AC list , B6RI03, B6RI04, P47000, Q03179, Q6VXX4, Q86ZT2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: August 30, 2005
Last modified: December 15, 2009
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents