Cell wall mannoprotein CIS3 precursor - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P47001 (CIS3_YEAST)

Last modified December 15, 2009. Version 85. History...

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

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Names and origin

Protein names

Recommended name:
    Cell wall mannoprotein CIS3
Alternative name(s):
    Covalently-linked cell wall protein 5/11
    Protein with internal repeats 4
    Soluble cell wall protein 8

Gene names

Name:	CIS3
Synonyms:	CCW11, CCW5, PIR4, SCW8
Ordered Locus Names:	YJL158C
ORF Names:	J0561

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	227 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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. Ref.10 Ref.11
Subcellular location	Secreted › cell wall. Note: Covalently attached to the cell wall. Localizes predominantly on the surface of growing buds. Ref.3 Ref.5 Ref.6 Ref.8 Ref.13
Induction	Positively regulated by signaling through MPK1 in response to cell wall perturbation. Ref.9 Ref.12 Ref.15
Domain	The PIR1/2/3 repeat is required for the covalent linkage to the cell wall.
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 acid, arising from Gln-74 within the PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan chains. Extensively O-mannosylated. Also N-glycosylated.
Miscellaneous	Present with 12500 molecules/cell in log phase SD medium. Ref.14
Sequence similarities	Belongs to the PIR protein family. Contains 1 PIR1/2/3 repeat.

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Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Cell wall Secreted
Domain	Repeat Signal
PTM	Cleavage on pair of basic residues Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell wall organization Ref.10 Inferred from mutant phenotype. Source: SGD
Cellular component	cellular bud tip Ref.3 Inferred from direct assay. Source: SGD endoplasmic reticulum Inferred from direct assay. Source: SGD extracellular region Inferred from direct assay. Source: SGD fungal-type cell wall Ref.3 Ref.13 Inferred from direct assay. Source: SGD plasma membrane Inferred from direct assay. Source: SGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Ref.3

Propeptide

22 – 64

PRO_0000033258

Chain

65 – 227

163

Cell wall mannoprotein CIS3

PRO_0000033259

Regions

Repeat

65 – 78

PIR1/2/3

Sites

Site

64 – 65

Cleavage; by KEX2

Site

Covalent attachment to cell wall glycan

Amino acid modifications

Modified residue

Phosphothreonine Ref.16

Glycosylation

O-linked (Man) Ref.7

Glycosylation

O-linked (Man) Ref.7

Glycosylation

105

O-linked (Man) Ref.4

Glycosylation

106

O-linked (Man) Ref.4

Glycosylation

107

O-linked (Man) Ref.4

Glycosylation

109

O-linked (Man) Ref.4

Glycosylation

111

O-linked (Man) Ref.4

Glycosylation

112

O-linked (Man) Ref.4

Glycosylation

113

O-linked (Man) Ref.4

Glycosylation

114

N-linked (GlcNAc...) Potential

Glycosylation

116

O-linked (Man) Ref.4

Glycosylation

117

O-linked (Man) Ref.4

Glycosylation

118

O-linked (Man) Ref.4

Experimental info

Mutagenesis

D → N: Does not affect cell wall incorporation. Ref.7

Mutagenesis

S → A: Does not affect cell wall incorporation. Ref.7

Mutagenesis

Q → A: Results in complete loss of cell wall incorporation. Ref.7

Mutagenesis

D → N: Results in complete loss of cell wall incorporation. Ref.7

Mutagenesis

Q → A: Results in complete loss of cell wall incorporation. Ref.7

Mutagenesis

Q → A: Results in complete loss of cell wall incorporation. Ref.7

Mutagenesis

T → A: Does not affect cell wall incorporation. Ref.7

Mutagenesis

S → A: Does not affect cell wall incorporation. Ref.7

Mutagenesis

T → A: Does not affect cell wall incorporation. Ref.7

Mutagenesis

130

C → S: Does not affect cell wall incorporation. Ref.6

Mutagenesis

197

C → S: Results in the incorporation of KEX2-unprocessed precursor protein into the cell wall. Ref.6

Mutagenesis

208 – 227

QNVAE…SLVDC → LDC in PIR4t18; destabilizes the protein. Ref.6

Mutagenesis

227

Missing: Does not affect cell wall incorporation. Ref.6

Sequence conflict

43 – 44

AA → SS Ref.3

Sequence conflict

S → T Ref.5

Sequence conflict

S → E Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P47001-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9777D644CFF81880
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FASTA

227

23,242

        10         20         30         40         50         60 
MQFKNVALAA SVAALSATAS AEGYTPGEPW STLTPTGSIS CGAAEYTTTF GIAVQAITSS 

        70         80         90        100        110        120 
KAKRDVISQI GDGQVQATSA ATAQATDSQA QATTTATPTS SEKISSSASK TSTNATSSSC 

       130        140        150        160        170        180 
ATPSLKDSSC KNSGTLELTL KDGVLTDAKG RIGSIVANRQ FQFDGPPPQA GAIYAAGWSI 

       190        200        210        220 
TEDGYLALGD SDVFYQCLSG NFYNLYDQNV AEQCSAIHLE AVSLVDC

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. 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.
[2]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Identification of two mannoproteins released from cell walls of a Saccharomyces cerevisiae mnn1 mnn9 double mutant by reducing agents." Moukadiri I., Jaafar L., Zueco J. J. Bacteriol. 181:4741-4745(1999) [PubMed: 10438739] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-47 AND 65-89, CLEAVAGE BY KEX2, SUBCELLULAR LOCATION.
[4]	"O-mannosylation precedes and potentially controls the N-glycosylation of a yeast cell wall glycoprotein." Ecker M., Mrsa V., Hagen I., Deutzmann R., Strahl S., Tanner W. EMBO Rep. 4:628-632(2003) [PubMed: 12776183] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-118, GLYCOSYLATION AT SER-105; SER-106; SER-107; SER-109; THR-111; SER-112; THR-113; THR-116; SER-117 AND SER-118.
[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 65-77, GLYCOSYLATION, SUBCELLULAR LOCATION.
[6]	"Functional analysis of the cysteine residues and the repetitive sequence of Saccharomyces cerevisiae Pir4/Cis3: the repetitive sequence is needed for binding to the cell wall beta-1,3-glucan." Castillo L., Martinez A.I., Garcera A., Elorza M.V., Valentin E., Sentandreu R. Yeast 20:973-983(2003) [PubMed: 12898712] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-77, MUTAGENESIS OF CYS-130; CYS-197; 208-GLN--CYS-227 AND CYS-227, SUBCELLULAR LOCATION.
[7]	"Pir proteins of Saccharomyces cerevisiae are attached to beta-1,3-glucan by a new protein-carbohydrate linkage." Ecker M., Deutzmann R., Lehle L., Mrsa V., Tanner W. J. Biol. Chem. 281:11523-11529(2006) [PubMed: 16495216] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION AT SER-68 AND THR-78, MUTAGENESIS OF ASP-65; SER-68; GLN-69; ASP-72; GLN-74; GLN-76; THR-78; SER-79 AND THR-82, CELL WALL ATTACHMENT SITE, MASS SPECTROMETRY.
[8]	"New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating." Cappellaro C., Mrsa V., Tanner W. J. Bacteriol. 180:5030-5037(1998) [PubMed: 9748433] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-75, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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].
[15]	"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.
[16]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, MASS SPECTROMETRY.
[17]	"Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes." Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H. Mol. Syst. Biol. 5:308-308(2009) [PubMed: 19756047] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Z49433 Genomic DNA. Translation: CAA89453.1. AY693027 Genomic DNA. Translation: AAT93046.1.
PIR	S56941.
RefSeq	NP_012377.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4788N.
IntAct	P47001. 4 interactions.
STRING	P47001.
2-D gel databases
COMPLUYEAST-2DPAGE	P47001.
Proteomic databases
PeptideAtlas	P47001.
Genome annotation databases
Ensembl	YJL158C; YJL158C; YJL158C; Saccharomyces cerevisiae. [Genome view]
GeneID	853282.
KEGG	sce:YJL158C.
NMPDR	fig\|4932.3.peg.3341.
Organism-specific databases
CYGD	YJL158c.
SGD	S000003694. CIS3.
Phylogenomic databases
HOGENOM	HBG626440.
OMA	ETASVVN.
OrthoDB	EOG97H76C.
Gene expression databases
ArrayExpress	P47001.
Genevestigator	P47001.
GermOnline	YJL158C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000420. Yeast_PIR. [Graphical view]
Pfam	PF00399. PIR. 1 hit. [Graphical view]
PROSITE	PS00929. PIR_REPEAT_1. 1 hit. PS50256. PIR_REPEAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973576.
PMAP-CutDB	P47001.

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Entry information

Entry name

CIS3_YEAST

Accession

Primary (citable) accession number: P47001

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 15, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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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)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents