CIS3_YEAST
ID CIS3_YEAST Reviewed; 227 AA.
AC P47001; D6VW29;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cell wall mannoprotein CIS3;
DE AltName: Full=Covalently-linked cell wall protein 5/11;
DE AltName: Full=Protein with internal repeats 4;
DE AltName: Full=Soluble cell wall protein 8;
DE Flags: Precursor;
GN Name=CIS3; Synonyms=CCW11, CCW5, PIR4, SCW8; OrderedLocusNames=YJL158C;
GN ORFNames=J0561;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 22-47 AND 65-89, CLEAVAGE BY KEX2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10438739; DOI=10.1128/jb.181.16.4741-4745.1999;
RA Moukadiri I., Jaafar L., Zueco J.;
RT "Identification of two mannoproteins released from cell walls of a
RT Saccharomyces cerevisiae mnn1 mnn9 double mutant by reducing agents.";
RL J. Bacteriol. 181:4741-4745(1999).
RN [5]
RP PROTEIN SEQUENCE OF 65-118, AND GLYCOSYLATION AT SER-105; SER-106; SER-107;
RP SER-109; THR-111; SER-112; THR-113; THR-116; SER-117 AND SER-118.
RX PubMed=12776183; DOI=10.1038/sj.embor.embor864;
RA Ecker M., Mrsa V., Hagen I., Deutzmann R., Strahl S., Tanner W.;
RT "O-mannosylation precedes and potentially controls the N-glycosylation of a
RT yeast cell wall glycoprotein.";
RL EMBO Rep. 4:628-632(2003).
RN [6]
RP PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=9301021;
RX DOI=10.1002/(sici)1097-0061(19970930)13:12<1145::aid-yea163>3.0.co;2-y;
RA Mrsa V., Seidl T., Gentzsch M., Tanner W.;
RT "Specific labelling of cell wall proteins by biotinylation. Identification
RT of four covalently linked O-mannosylated proteins of Saccharomyces
RT cerevisiae.";
RL Yeast 13:1145-1154(1997).
RN [7]
RP PROTEIN SEQUENCE OF 65-77, MUTAGENESIS OF CYS-130; CYS-197;
RP 208-GLN--CYS-227 AND CYS-227, AND SUBCELLULAR LOCATION.
RX PubMed=12898712; DOI=10.1002/yea.1016;
RA Castillo L., Martinez A.I., Garcera A., Elorza M.V., Valentin E.,
RA Sentandreu R.;
RT "Functional analysis of the cysteine residues and the repetitive sequence
RT of Saccharomyces cerevisiae Pir4/Cis3: the repetitive sequence is needed
RT for binding to the cell wall beta-1,3-glucan.";
RL Yeast 20:973-983(2003).
RN [8]
RP PROTEIN SEQUENCE OF 65-77, GLYCOSYLATION AT SER-68 AND THR-78, MUTAGENESIS
RP OF ASP-65; SER-68; GLN-69; ASP-72; GLN-74; GLN-76; THR-78; SER-79 AND
RP THR-82, CELL WALL ATTACHMENT SITE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16495216; DOI=10.1074/jbc.m600314200;
RA Ecker M., Deutzmann R., Lehle L., Mrsa V., Tanner W.;
RT "Pir proteins of Saccharomyces cerevisiae are attached to beta-1,3-glucan
RT by a new protein-carbohydrate linkage.";
RL J. Biol. Chem. 281:11523-11529(2006).
RN [9]
RP PROTEIN SEQUENCE OF 65-75, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 96099 / S288c / SEY6210;
RX PubMed=9748433; DOI=10.1128/jb.180.19.5030-5037.1998;
RA Cappellaro C., Mrsa V., Tanner W.;
RT "New potential cell wall glucanases of Saccharomyces cerevisiae and their
RT involvement in mating.";
RL J. Bacteriol. 180:5030-5037(1998).
RN [10]
RP INDUCTION.
RX PubMed=10594829; DOI=10.1046/j.1365-2958.1999.01667.x;
RA Jung U.S., Levin D.E.;
RT "Genome-wide analysis of gene expression regulated by the yeast cell wall
RT integrity signalling pathway.";
RL Mol. Microbiol. 34:1049-1057(1999).
RN [11]
RP FUNCTION.
RX PubMed=10407261;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<813::aid-yea421>3.0.co;2-y;
RA Mrsa V., Tanner W.;
RT "Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p
RT (members of the Pir protein family) in stability of the Saccharomyces
RT cerevisiae cell wall.";
RL Yeast 15:813-820(1999).
RN [12]
RP FUNCTION.
RX PubMed=15470095; DOI=10.1099/mic.0.27296-0;
RA Teparic R., Stuparevic I., Mrsa V.;
RT "Increased mortality of Saccharomyces cerevisiae cell wall protein
RT mutants.";
RL Microbiology 150:3145-3150(2004).
RN [13]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
RN [14]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA de Koster C.G.;
RT "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT identification of proteins covalently attached via
RT glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL J. Biol. Chem. 280:20894-20901(2005).
RN [15]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [16]
RP INDUCTION.
RX PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
RA Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
RT "Mass spectrometric quantitation of covalently bound cell wall proteins in
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:887-896(2007).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Component of the outer cell wall layer. Required for
CC stability of the cell wall and for optimal growth. Required for
CC resistance against several antifungal and cell wall-perturbing agents.
CC {ECO:0000269|PubMed:10407261, ECO:0000269|PubMed:15470095}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10438739,
CC ECO:0000269|PubMed:12898712, ECO:0000269|PubMed:15781460,
CC ECO:0000269|PubMed:9301021, ECO:0000269|PubMed:9748433}.
CC Note=Covalently attached to the cell wall. Localizes predominantly on
CC the surface of growing buds.
CC -!- INDUCTION: Positively regulated by signaling through MPK1 in response
CC to cell wall perturbation. {ECO:0000269|PubMed:10594829,
CC ECO:0000269|PubMed:15116342, ECO:0000269|PubMed:17617218}.
CC -!- DOMAIN: The PIR1/2/3 repeat is required for the covalent linkage to the
CC cell wall.
CC -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC of glutamic acid, arising from Gln-74 within the PIR1/2/3 repeat, and
CC hydroxyl groups of glucoses of beta-1,3-glucan chains.
CC -!- PTM: Extensively O-mannosylated. Also N-glycosylated.
CC {ECO:0000269|PubMed:12776183, ECO:0000269|PubMed:16495216,
CC ECO:0000269|PubMed:19756047, ECO:0000269|PubMed:9301021}.
CC -!- MISCELLANEOUS: Present with 12500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR EMBL; Z49433; CAA89453.1; -; Genomic_DNA.
DR EMBL; AY693027; AAT93046.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08645.1; -; Genomic_DNA.
DR PIR; S56941; S56941.
DR RefSeq; NP_012377.1; NM_001181591.1.
DR AlphaFoldDB; P47001; -.
DR BioGRID; 33602; 91.
DR DIP; DIP-4788N; -.
DR ELM; P47001; -.
DR IntAct; P47001; 1.
DR STRING; 4932.YJL158C; -.
DR iPTMnet; P47001; -.
DR MaxQB; P47001; -.
DR PaxDb; P47001; -.
DR PRIDE; P47001; -.
DR EnsemblFungi; YJL158C_mRNA; YJL158C; YJL158C.
DR GeneID; 853282; -.
DR KEGG; sce:YJL158C; -.
DR SGD; S000003694; CIS3.
DR VEuPathDB; FungiDB:YJL158C; -.
DR eggNOG; ENOG502RKR1; Eukaryota.
DR GeneTree; ENSGT00940000176741; -.
DR HOGENOM; CLU_039662_2_0_1; -.
DR InParanoid; P47001; -.
DR OMA; NTMWSNN; -.
DR BioCyc; YEAST:G3O-31598-MON; -.
DR PRO; PR:P47001; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47001; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; ISS:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR InterPro; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 1.
DR PROSITE; PS00929; PIR_REPEAT_1; 1.
DR PROSITE; PS50256; PIR_REPEAT_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10438739"
FT PROPEP 22..64
FT /evidence="ECO:0000269|PubMed:10438739,
FT ECO:0000269|PubMed:12776183, ECO:0000269|PubMed:12898712,
FT ECO:0000269|PubMed:16495216, ECO:0000269|PubMed:9301021,
FT ECO:0000269|PubMed:9748433"
FT /id="PRO_0000033258"
FT CHAIN 65..227
FT /note="Cell wall mannoprotein CIS3"
FT /id="PRO_0000033259"
FT REPEAT 65..78
FT /note="PIR1/2/3"
FT REGION 83..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 64..65
FT /note="Cleavage; by KEX2"
FT SITE 74
FT /note="Covalent attachment to cell wall glycan"
FT CARBOHYD 68
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:16495216"
FT CARBOHYD 78
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:16495216"
FT CARBOHYD 105
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 106
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 107
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 109
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 111
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 112
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 113
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 117
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT CARBOHYD 118
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:12776183"
FT MUTAGEN 65
FT /note="D->N: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 68
FT /note="S->A: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 69
FT /note="Q->A: Results in complete loss of cell wall
FT incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 72
FT /note="D->N: Results in complete loss of cell wall
FT incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 74
FT /note="Q->A: Results in complete loss of cell wall
FT incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 76
FT /note="Q->A: Results in complete loss of cell wall
FT incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 78
FT /note="T->A: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 79
FT /note="S->A: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 82
FT /note="T->A: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:16495216"
FT MUTAGEN 130
FT /note="C->S: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:12898712"
FT MUTAGEN 197
FT /note="C->S: Results in the incorporation of KEX2-
FT unprocessed precursor protein into the cell wall."
FT /evidence="ECO:0000269|PubMed:12898712"
FT MUTAGEN 208..227
FT /note="QNVAEQCSAIHLEAVSLVDC->LDC: In PIR4t18; destabilizes
FT the protein."
FT /evidence="ECO:0000269|PubMed:12898712"
FT MUTAGEN 227
FT /note="Missing: Does not affect cell wall incorporation."
FT /evidence="ECO:0000269|PubMed:12898712"
FT CONFLICT 43..44
FT /note="AA -> SS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="S -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="S -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
