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CWP1_YEAST
ID   CWP1_YEAST              Reviewed;         239 AA.
AC   P28319; D6VXJ2; Q70DB4; Q70DB5;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Cell wall protein CWP1;
DE   AltName: Full=Glycoprotein GP40;
DE   Flags: Precursor;
GN   Name=CWP1; OrderedLocusNames=YKL096W; ORFNames=YJU1, YKL443;
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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 26786 / X2180-1A;
RX   PubMed=8543563; DOI=10.1093/oxfordjournals.jbchem.a124907;
RA   Shimoi H., Iimura Y., Obata T.;
RT   "Molecular cloning of CWP1: a gene encoding a Saccharomyces cerevisiae cell
RT   wall protein solubilized with Rarobacter faecitabidus protease I.";
RL   J. Biochem. 118:302-311(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC   CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX   PubMed=15087486; DOI=10.1093/nar/gkh529;
RA   Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA   Souciet J.-L.;
RT   "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT   implication of recombination in phylogeny.";
RL   Nucleic Acids Res. 32:2069-2078(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8256524; DOI=10.1002/yea.320091016;
RA   Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA   Bolotin-Fukuhara M.;
RT   "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT   physically localizes the MRB1 gene and reveals eight new open reading
RT   frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL   Yeast 9:1149-1155(1993).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-239.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1626433; DOI=10.1002/yea.320080509;
RA   Forrova H., Kolarov J., Ghislain M., Goffeau A.;
RT   "Sequence of the novel essential gene YJU2 and two flanking reading frames
RT   located within a 3.2 kb EcoRI fragment from chromosome X of Saccharomyces
RT   cerevisiae.";
RL   Yeast 8:419-422(1992).
RN   [7]
RP   PROTEIN SEQUENCE OF 21-30, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=7768807; DOI=10.1128/jb.177.11.3104-3110.1995;
RA   van der Vaart J.M., Caro L.H.P., Chapman J.W., Klis F.M., Verrips C.T.;
RT   "Identification of three mannoproteins in the cell wall of Saccharomyces
RT   cerevisiae.";
RL   J. Bacteriol. 177:3104-3110(1995).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8724141; DOI=10.1093/glycob/6.3.337;
RA   Kapteyn J.C., Montijn R.C., Vink E., de la Cruz J., Llobell A.,
RA   Douwes J.E., Shimoi H., Lipke P.N., Klis F.M.;
RT   "Retention of Saccharomyces cerevisiae cell wall proteins through a
RT   phosphodiester-linked beta-1,3-/beta-1,6-glucan heteropolymer.";
RL   Glycobiology 6:337-345(1996).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10209754; DOI=10.1046/j.1365-2958.1999.01320.x;
RA   Kapteyn J.C., Van Egmond P., Sievi E., Van Den Ende H., Makarow M.,
RA   Klis F.M.;
RT   "The contribution of the O-glycosylated protein Pir2p/Hsp150 to the
RT   construction of the yeast cell wall in wild-type cells and beta 1,6-glucan-
RT   deficient mutants.";
RL   Mol. Microbiol. 31:1835-1844(1999).
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   INDUCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11016834; DOI=10.1007/s004380000285;
RA   Terashima H., Yabuki N., Arisawa M., Hamada K., Kitada K.;
RT   "Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-
RT   attached proteins in response to cell wall damage caused by disruption of
RT   FKS1 in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 264:64-74(2000).
RN   [12]
RP   INDUCTION.
RX   PubMed=11292809; DOI=10.1128/jb.183.9.2881-2887.2001;
RA   Abramova N.E., Sertil O., Mehta S., Lowry C.V.;
RT   "Reciprocal regulation of anaerobic and aerobic cell wall mannoprotein gene
RT   expression in Saccharomyces cerevisiae.";
RL   J. Bacteriol. 183:2881-2887(2001).
RN   [13]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11136466; DOI=10.1046/j.1365-2958.2001.02242.x;
RA   Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H., Van Den Ende H.,
RA   Klis F.M.;
RT   "Low external pH induces HOG1-dependent changes in the organization of the
RT   Saccharomyces cerevisiae cell wall.";
RL   Mol. Microbiol. 39:469-479(2001).
RN   [14]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR.
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   SUBCELLULAR LOCATION.
RX   PubMed=16672383; DOI=10.1091/mbc.e05-08-0738;
RA   Smits G.J., Schenkman L.R., Brul S., Pringle J.R., Klis F.M.;
RT   "Role of cell cycle-regulated expression in the localized incorporation of
RT   cell wall proteins in yeast.";
RL   Mol. Biol. Cell 17:3267-3280(2006).
RN   [16]
RP   LEVEL OF PROTEIN EXPRESSION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: Component of the cell wall.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC       anchor. Note=Identified as covalently-linked GPI-modified cell wall
CC       protein (GPI-CWP) as well as protein covalently linked via an alkali-
CC       sensitive bond not requiring the GPI-derived structure. Can also be
CC       double-anchored to the cell wall through both types of linkages.
CC       Incorporated into the birth scar of a daughter cell.
CC   -!- INDUCTION: Positively regulated by cell integrity signaling through
CC       MPK1 in response to cell wall perturbation. Induction is dependent on
CC       transcription factor RLM1. Down-regulated during anaerobic growth. Up-
CC       regulated by low pH. {ECO:0000269|PubMed:10594829,
CC       ECO:0000269|PubMed:11016834, ECO:0000269|PubMed:11136466,
CC       ECO:0000269|PubMed:11292809}.
CC   -!- PTM: Extensively O-glycosylated. {ECO:0000269|PubMed:7768807}.
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.
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 acids, arising from a specific glutamine within the
CC       PIR1/2/3 repeat, and hydroxyl groups of glucoses of beta-1,3-glucan
CC       chains (By similarity). The alkali-sensitive linkage is induced by low
CC       pH. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The strains CLIB 410 and CLIB 630 haplotype Ha2, contain
CC       large deletions that remove most of the protein.
CC   -!- MISCELLANEOUS: Present with 67000 wall-bound molecules/cell in log
CC       phase YPD medium. {ECO:0000269|PubMed:17617218}.
CC   -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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DR   EMBL; D37975; BAA07193.1; -; Genomic_DNA.
DR   EMBL; AJ585652; CAE52172.1; -; Genomic_DNA.
DR   EMBL; AJ585653; CAE52173.1; -; Genomic_DNA.
DR   EMBL; AJ585654; CAE52174.1; -; Genomic_DNA.
DR   EMBL; AJ585655; CAE52175.1; -; Genomic_DNA.
DR   EMBL; AJ585656; CAE52176.1; -; Genomic_DNA.
DR   EMBL; AJ585657; CAE52177.1; -; Genomic_DNA.
DR   EMBL; AJ585658; CAE52178.1; -; Genomic_DNA.
DR   EMBL; AJ585659; CAE52179.1; -; Genomic_DNA.
DR   EMBL; AJ585660; CAE52180.1; -; Genomic_DNA.
DR   EMBL; AJ585661; CAE52181.1; -; Genomic_DNA.
DR   EMBL; AJ585662; CAE52182.1; -; Genomic_DNA.
DR   EMBL; AJ585663; CAE52183.1; -; Genomic_DNA.
DR   EMBL; AJ585664; CAE52184.1; -; Genomic_DNA.
DR   EMBL; AJ585665; CAE52185.1; -; Genomic_DNA.
DR   EMBL; AJ585666; CAE52186.1; -; Genomic_DNA.
DR   EMBL; X71133; CAA50461.1; -; Genomic_DNA.
DR   EMBL; Z28096; CAA81934.1; -; Genomic_DNA.
DR   EMBL; X66245; CAA46969.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09062.1; -; Genomic_DNA.
DR   PIR; S37923; S37923.
DR   RefSeq; NP_012827.1; NM_001179662.1.
DR   AlphaFoldDB; P28319; -.
DR   BioGRID; 34037; 35.
DR   IntAct; P28319; 2.
DR   STRING; 4932.YKL096W; -.
DR   MaxQB; P28319; -.
DR   PaxDb; P28319; -.
DR   PRIDE; P28319; -.
DR   EnsemblFungi; YKL096W_mRNA; YKL096W; YKL096W.
DR   GeneID; 853766; -.
DR   KEGG; sce:YKL096W; -.
DR   SGD; S000001579; CWP1.
DR   VEuPathDB; FungiDB:YKL096W; -.
DR   eggNOG; ENOG502S09G; Eukaryota.
DR   HOGENOM; CLU_054077_0_0_1; -.
DR   InParanoid; P28319; -.
DR   OMA; TSCENNG; -.
DR   BioCyc; YEAST:G3O-31887-MON; -.
DR   PRO; PR:P28319; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P28319; protein.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0071597; C:cellular birth scar; IDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR   GO; GO:0005199; F:structural constituent of cell wall; IDA:SGD.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IGI:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IDA:SGD.
DR   InterPro; IPR000420; Yeast_PIR.
DR   Pfam; PF00399; PIR; 1.
DR   PROSITE; PS50256; PIR_REPEAT_2; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:7768807"
FT   CHAIN           21..217
FT                   /note="Cell wall protein CWP1"
FT                   /id="PRO_0000033250"
FT   PROPEP          218..239
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033251"
FT   REPEAT          194..212
FT                   /note="PIR1/2/3"
FT   REGION          131..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            204
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   LIPID           217
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         19..27
FT                   /note="IADSEEFGL -> LPIPKNSAW (in strain: CLIB 410)"
FT   CONFLICT        189
FT                   /note="A -> V (in Ref. 2; CAE52173/CAE52175/CAE52179/
FT                   CAE52180/CAE52181/CAE52182/CAE52183/CAE52185/CAE52186 and
FT                   5; CAA46969)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   239 AA;  24268 MW;  A85906180D630BAE CRC64;
     MKFSTALSVA LFALAKMVIA DSEEFGLVSI RSGSDLQYLS VYSDNGTLKL GSGSGSFEAT
     ITDDGKLKFD DDKYAVVNED GSFKEGSESD AATGFSIKDG HLNYKSSSGF YAIKDGSSYI
     FSSKQSDDAT GVAIRPTSKS GSVAADFSPS DSSSSSSASA SSASASSSTK HSSSIESVET
     STTVETSSAS SPTASVISQI TDGQIQAPNT VYEQTENAGA KAAVGMGAGA LAVAAAYLL
 
 
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