P47001 (CIS3_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (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	227 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	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.11 Ref.12
Subcellular location	Secreted › cell wall. Note: Covalently attached to the cell wall. Localizes predominantly on the surface of growing buds. Ref.4 Ref.6 Ref.7 Ref.9 Ref.14
Induction	Positively regulated by signaling through MPK1 in response to cell wall perturbation. Ref.10 Ref.13 Ref.16
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. Ref.5 Ref.6 Ref.8
Miscellaneous	Present with 12500 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the PIR protein family. Contains 1 PIR1/2/3 repeat.

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 Reference proteome
Gene Ontology (GO)
Biological_process	fungal-type cell wall organization Inferred from mutant phenotype Ref.11. Source: SGD
Cellular_component	cellular bud tip Inferred from direct assay Ref.4. Source: SGD endoplasmic reticulum Inferred from direct assay PubMed 11914276. Source: SGD extracellular region Inferred from direct assay PubMed 12702350PubMed 19129178. Source: SGD fungal-type cell wall Inferred from direct assay Ref.4Ref.14. Source: SGD plasma membrane Inferred from direct assay PubMed 11914276. Source: SGD
Molecular_function	structural constituent of cell wall Inferred from sequence or structural similarity 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 – 21	21	Ref.4
	Propeptide	22 – 64	43			PRO_0000033258
	Chain	65 – 227	163	Cell wall mannoprotein CIS3		PRO_0000033259
Regions
	Repeat	65 – 78	14	PIR1/2/3
Sites
	Site	64 – 65	2	Cleavage; by KEX2
	Site	74	1	Covalent attachment to cell wall glycan
Amino acid modifications
	Modified residue	93	1	Phosphothreonine Ref.17
	Glycosylation	68	1	O-linked (Man) Ref.8
	Glycosylation	78	1	O-linked (Man) Ref.8
	Glycosylation	105	1	O-linked (Man) Ref.5
	Glycosylation	106	1	O-linked (Man) Ref.5
	Glycosylation	107	1	O-linked (Man) Ref.5
	Glycosylation	109	1	O-linked (Man) Ref.5
	Glycosylation	111	1	O-linked (Man) Ref.5
	Glycosylation	112	1	O-linked (Man) Ref.5
	Glycosylation	113	1	O-linked (Man) Ref.5
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	116	1	O-linked (Man) Ref.5
	Glycosylation	117	1	O-linked (Man) Ref.5
	Glycosylation	118	1	O-linked (Man) Ref.5
Experimental info
	Mutagenesis	65	1	D → N: Does not affect cell wall incorporation. Ref.8
	Mutagenesis	68	1	S → A: Does not affect cell wall incorporation. Ref.8
	Mutagenesis	69	1	Q → A: Results in complete loss of cell wall incorporation. Ref.8
	Mutagenesis	72	1	D → N: Results in complete loss of cell wall incorporation. Ref.8
	Mutagenesis	74	1	Q → A: Results in complete loss of cell wall incorporation. Ref.8
	Mutagenesis	76	1	Q → A: Results in complete loss of cell wall incorporation. Ref.8
	Mutagenesis	78	1	T → A: Does not affect cell wall incorporation. Ref.8
	Mutagenesis	79	1	S → A: Does not affect cell wall incorporation. Ref.8
	Mutagenesis	82	1	T → A: Does not affect cell wall incorporation. Ref.8
	Mutagenesis	130	1	C → S: Does not affect cell wall incorporation. Ref.7
	Mutagenesis	197	1	C → S: Results in the incorporation of KEX2-unprocessed precursor protein into the cell wall. Ref.7
	Mutagenesis	208 – 227	20	QNVAE…SLVDC → LDC in PIR4t18; destabilizes the protein. Ref.7
	Mutagenesis	227	1	Missing: Does not affect cell wall incorporation. Ref.7
	Sequence conflict	43 – 44	2	AA → SS AA sequence Ref.4
	Sequence conflict	68	1	S → T AA sequence Ref.6
	Sequence conflict	88	1	S → E AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P47001 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 9777D644CFF81880	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

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. , 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-47 AND 65-89, CLEAVAGE BY KEX2, SUBCELLULAR LOCATION.
[5]	"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] [Europe PMC] [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.
[6]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION, SUBCELLULAR LOCATION.
[7]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-77, MUTAGENESIS OF CYS-130; CYS-197; 208-GLN--CYS-227 AND CYS-227, SUBCELLULAR LOCATION.
[8]	"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] [Europe PMC] [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.
[9]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 65-75, SUBCELLULAR LOCATION. Strain: ATCC 96099 / S288c / SEY6210.
[10]	"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] [Europe PMC] [Abstract] Cited for: INDUCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Increased mortality of Saccharomyces cerevisiae cell wall protein mutants." Teparic R., Stuparevic I., Mrsa V. Microbiology 150:3145-3150(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"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] [Europe PMC] [Abstract] Cited for: INDUCTION.
[14]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[15]	"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].
[16]	"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] [Europe PMC] [Abstract] Cited for: INDUCTION.
[17]	"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 THR-93, MASS SPECTROMETRY.
[18]	"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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49433 Genomic DNA. Translation: CAA89453.1. AY693027 Genomic DNA. Translation: AAT93046.1. BK006943 Genomic DNA. Translation: DAA08645.1.
PIR	S56941.
RefSeq	NP_012377.1. NM_001181591.1.
3D structure databases
ProteinModelPortal	P47001.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4788N.
IntAct	P47001. 1 interaction.
MINT	MINT-507442.
STRING	4932.YJL158C.
Proteomic databases
PaxDb	P47001.
PeptideAtlas	P47001.
PRIDE	P47001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL158C; YJL158C; YJL158C.
GeneID	853282.
KEGG	sce:YJL158C.
Organism-specific databases
CYGD	YJL158c.
SGD	S000003694. CIS3.
Phylogenomic databases
eggNOG	NOG38801.
GeneTree	ENSGT00390000008137.
HOGENOM	HOG000248193.
OMA	QFKNVAL.
OrthoDB	EOG4GMZ6K.
Gene expression databases
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
NextBio	973576.
PMAP-CutDB	P47001.

Entry information

Entry name

CIS3_YEAST

Accession

Primary (citable) accession number: P47001
Secondary accession number(s): D6VW29

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program