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

 CIS3_YEAST              Reviewed;         227 AA.
P47001; D6VW29;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Cell wall mannoprotein CIS3;
AltName: Full=Covalently-linked cell wall protein 5/11;
AltName: Full=Protein with internal repeats 4;
AltName: Full=Soluble cell wall protein 8;
Flags: Precursor;
Name=CIS3; Synonyms=CCW11, CCW5, PIR4, SCW8;
OrderedLocusNames=YJL158C; ORFNames=J0561;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8641269;
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.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X.";
EMBO J. 15:2031-2049(1996).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
PROTEIN SEQUENCE OF 22-47 AND 65-89, CLEAVAGE BY KEX2, AND SUBCELLULAR
LOCATION.
PubMed=10438739;
Moukadiri I., Jaafar L., Zueco J.;
"Identification of two mannoproteins released from cell walls of a
Saccharomyces cerevisiae mnn1 mnn9 double mutant by reducing agents.";
J. Bacteriol. 181:4741-4745(1999).
[5]
PROTEIN SEQUENCE OF 65-118, AND GLYCOSYLATION AT SER-105; SER-106;
SER-107; SER-109; THR-111; SER-112; THR-113; THR-116; SER-117 AND
SER-118.
PubMed=12776183; DOI=10.1038/sj.embor.embor864;
Ecker M., Mrsa V., Hagen I., Deutzmann R., Strahl S., Tanner W.;
"O-mannosylation precedes and potentially controls the N-glycosylation
of a yeast cell wall glycoprotein.";
EMBO Rep. 4:628-632(2003).
[6]
PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=9301021;
DOI=10.1002/(SICI)1097-0061(19970930)13:12<1145::AID-YEA163>3.3.CO;2-P;
Mrsa V., Seidl T., Gentzsch M., Tanner W.;
"Specific labelling of cell wall proteins by biotinylation.
Identification of four covalently linked O-mannosylated proteins of
Saccharomyces cerevisiae.";
Yeast 13:1145-1154(1997).
[7]
PROTEIN SEQUENCE OF 65-77, MUTAGENESIS OF CYS-130; CYS-197;
208-GLN--CYS-227 AND CYS-227, AND SUBCELLULAR LOCATION.
PubMed=12898712; DOI=10.1002/yea.1016;
Castillo L., Martinez A.I., Garcera A., Elorza M.V., Valentin E.,
Sentandreu R.;
"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.";
Yeast 20:973-983(2003).
[8]
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, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16495216; DOI=10.1074/jbc.M600314200;
Ecker M., Deutzmann R., Lehle L., Mrsa V., Tanner W.;
"Pir proteins of Saccharomyces cerevisiae are attached to beta-1,3-
glucan by a new protein-carbohydrate linkage.";
J. Biol. Chem. 281:11523-11529(2006).
[9]
PROTEIN SEQUENCE OF 65-75, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 96099 / S288c / SEY6210;
PubMed=9748433;
Cappellaro C., Mrsa V., Tanner W.;
"New potential cell wall glucanases of Saccharomyces cerevisiae and
their involvement in mating.";
J. Bacteriol. 180:5030-5037(1998).
[10]
INDUCTION.
PubMed=10594829; DOI=10.1046/j.1365-2958.1999.01667.x;
Jung U.S., Levin D.E.;
"Genome-wide analysis of gene expression regulated by the yeast cell
wall integrity signalling pathway.";
Mol. Microbiol. 34:1049-1057(1999).
[11]
FUNCTION.
PubMed=10407261;
DOI=10.1002/(SICI)1097-0061(199907)15:10A<813::AID-YEA421>3.0.CO;2-Y;
Mrsa V., Tanner W.;
"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.";
Yeast 15:813-820(1999).
[12]
FUNCTION.
PubMed=15470095; DOI=10.1099/mic.0.27296-0;
Teparic R., Stuparevic I., Mrsa V.;
"Increased mortality of Saccharomyces cerevisiae cell wall protein
mutants.";
Microbiology 150:3145-3150(2004).
[13]
INDUCTION.
PubMed=15116342; DOI=10.1002/yea.1109;
Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
Hellingwerf K.J., Klis F.M.;
"Characterization of the transcriptional response to cell wall stress
in Saccharomyces cerevisiae.";
Yeast 21:413-427(2004).
[14]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15781460; DOI=10.1074/jbc.M500334200;
Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
de Koster C.G.;
"Comprehensive proteomic analysis of Saccharomyces cerevisiae cell
walls: identification of proteins covalently attached via
glycosylphosphatidylinositol remnants or mild alkali-sensitive
linkages.";
J. Biol. Chem. 280:20894-20901(2005).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
INDUCTION.
PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
"Mass spectrometric quantitation of covalently bound cell wall
proteins in Saccharomyces cerevisiae.";
FEMS Yeast Res. 7:887-896(2007).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS].
PubMed=19756047; DOI=10.1038/msb.2009.64;
Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
"Global analysis of the glycoproteome in Saccharomyces cerevisiae
reveals new roles for protein glycosylation in eukaryotes.";
Mol. Syst. Biol. 5:308-308(2009).
-!- 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. {ECO:0000269|PubMed:10407261,
ECO:0000269|PubMed:15470095}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:10438739, ECO:0000269|PubMed:12898712,
ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9301021,
ECO:0000269|PubMed:9748433}. Note=Covalently attached to the cell
wall. Localizes predominantly on the surface of growing buds.
-!- INDUCTION: Positively regulated by signaling through MPK1 in
response to cell wall perturbation. {ECO:0000269|PubMed:10594829,
ECO:0000269|PubMed:15116342, ECO:0000269|PubMed:17617218}.
-!- DOMAIN: The PIR1/2/3 repeat is required for the covalent linkage
to the cell wall.
-!- PTM: 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.
-!- PTM: Extensively O-mannosylated. Also N-glycosylated.
{ECO:0000269|PubMed:12776183, ECO:0000269|PubMed:16495216,
ECO:0000269|PubMed:19756047, ECO:0000269|PubMed:9301021}.
-!- MISCELLANEOUS: Present with 12500 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; Z49433; CAA89453.1; -; Genomic_DNA.
EMBL; AY693027; AAT93046.1; -; Genomic_DNA.
EMBL; BK006943; DAA08645.1; -; Genomic_DNA.
PIR; S56941; S56941.
RefSeq; NP_012377.1; NM_001181591.1.
ProteinModelPortal; P47001; -.
SMR; P47001; -.
BioGrid; 33602; 83.
DIP; DIP-4788N; -.
ELM; P47001; -.
IntAct; P47001; 1.
MINT; MINT-507442; -.
STRING; 4932.YJL158C; -.
iPTMnet; P47001; -.
MaxQB; P47001; -.
PRIDE; P47001; -.
EnsemblFungi; YJL158C; YJL158C; YJL158C.
GeneID; 853282; -.
KEGG; sce:YJL158C; -.
EuPathDB; FungiDB:YJL158C; -.
SGD; S000003694; CIS3.
GeneTree; ENSGT00390000008137; -.
HOGENOM; HOG000248193; -.
InParanoid; P47001; -.
OMA; QFKNVAL; -.
OrthoDB; EOG092C3AY6; -.
BioCyc; YEAST:G3O-31598-MONOMER; -.
PMAP-CutDB; P47001; -.
PRO; PR:P47001; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0005576; C:extracellular region; IDA:SGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
GO; GO:0005199; F:structural constituent of cell wall; ISS:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
InterPro; IPR000420; Yeast_PIR.
Pfam; PF00399; PIR; 1.
PROSITE; PS00929; PIR_REPEAT_1; 1.
PROSITE; PS50256; PIR_REPEAT_2; 1.
1: Evidence at protein level;
Cell wall; Cell wall biogenesis/degradation;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Glycoprotein; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:10438739}.
PROPEP 22 64 {ECO:0000269|PubMed:10438739,
ECO:0000269|PubMed:12776183,
ECO:0000269|PubMed:12898712,
ECO:0000269|PubMed:16495216,
ECO:0000269|PubMed:9301021,
ECO:0000269|PubMed:9748433}.
/FTId=PRO_0000033258.
CHAIN 65 227 Cell wall mannoprotein CIS3.
/FTId=PRO_0000033259.
REPEAT 65 78 PIR1/2/3.
SITE 64 65 Cleavage; by KEX2.
SITE 74 74 Covalent attachment to cell wall glycan.
CARBOHYD 68 68 O-linked (Man) serine.
{ECO:0000269|PubMed:16495216}.
CARBOHYD 78 78 O-linked (Man) threonine.
{ECO:0000269|PubMed:16495216}.
CARBOHYD 105 105 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 106 106 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 107 107 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 109 109 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 111 111 O-linked (Man) threonine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 112 112 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 113 113 O-linked (Man) threonine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 O-linked (Man) threonine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 117 117 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
CARBOHYD 118 118 O-linked (Man) serine.
{ECO:0000269|PubMed:12776183}.
MUTAGEN 65 65 D->N: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 68 68 S->A: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 69 69 Q->A: Results in complete loss of cell
wall incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 72 72 D->N: Results in complete loss of cell
wall incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 74 74 Q->A: Results in complete loss of cell
wall incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 76 76 Q->A: Results in complete loss of cell
wall incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 78 78 T->A: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 79 79 S->A: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 82 82 T->A: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:16495216}.
MUTAGEN 130 130 C->S: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:12898712}.
MUTAGEN 197 197 C->S: Results in the incorporation of
KEX2-unprocessed precursor protein into
the cell wall.
{ECO:0000269|PubMed:12898712}.
MUTAGEN 208 227 QNVAEQCSAIHLEAVSLVDC->LDC: In PIR4t18;
destabilizes the protein.
{ECO:0000269|PubMed:12898712}.
MUTAGEN 227 227 Missing: Does not affect cell wall
incorporation.
{ECO:0000269|PubMed:12898712}.
CONFLICT 43 44 AA -> SS (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 68 68 S -> T (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 88 88 S -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 227 AA; 23242 MW; 9777D644CFF81880 CRC64;
MQFKNVALAA SVAALSATAS AEGYTPGEPW STLTPTGSIS CGAAEYTTTF GIAVQAITSS
KAKRDVISQI GDGQVQATSA ATAQATDSQA QATTTATPTS SEKISSSASK TSTNATSSSC
ATPSLKDSSC KNSGTLELTL KDGVLTDAKG RIGSIVANRQ FQFDGPPPQA GAIYAAGWSI
TEDGYLALGD SDVFYQCLSG NFYNLYDQNV AEQCSAIHLE AVSLVDC


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