CCW22_YEAST
ID CCW22_YEAST Reviewed; 136 AA.
AC Q7LHD1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Putative covalently bound cell wall protein 22;
DE Flags: Precursor;
GN Name=CCW22; OrderedLocusNames=YDR134C; ORFNames=YD9302.09C/YD9302.10C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 SUBCELLULAR LOCATION.
RX PubMed=9613572; DOI=10.1007/s004380050706;
RA Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 258:53-59(1998).
CC -!- FUNCTION: Cell wall protein necessary for cell wall integrity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:9613572}.
CC Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PGA59 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene unlikely to encode a
CC functional protein. Strain S288c has a stop codon in position 67, which
CC disrupts the gene coding for this protein and produces two ORFs.
CC Because of that it is not part of the S.cerevisiae S288c
CC complete/reference proteome set. {ECO:0000305|PubMed:24374639}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88216.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z48179; CAA88216.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q7LHD1; -.
DR MaxQB; Q7LHD1; -.
DR SGD; S000002541; YDR134C.
DR InParanoid; Q7LHD1; -.
DR ChiTaRS; YDR134C; yeast.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR Pfam; PF13928; Flocculin_t3; 1.
PE 5: Uncertain;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..115
FT /note="Putative covalently bound cell wall protein 22"
FT /id="PRO_0000226148"
FT PROPEP 116..136
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000226149"
FT REGION 73..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 115
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 136 AA; 13713 MW; 5A8B961BC8553D01 CRC64;
MQFSTVASIA AIAAVASAAS NITTATVTEE STTLVTITSC EDHVCSETVS PALVSTATVT
VNDVITQYTT WCPLPTTEAP KNTTSPAPTE KPTEKPTEKP TQQGSSTQTV TSYTGAAVKA
LPAAGALLAG AAALLL
