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NCW2_YEAST
ID   NCW2_YEAST              Reviewed;         254 AA.
AC   Q05777; D6VYJ7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cell wall biogenesis protein NCW2 {ECO:0000303|PubMed:27246500};
DE   AltName: Full=New cell wall protein 2 {ECO:0000303|PubMed:27246500};
DE   Flags: Precursor;
GN   Name=NCW2 {ECO:0000303|PubMed:27246500}; OrderedLocusNames=YLR194C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA   Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT   "Amino acid residues in the omega-minus region participate in cellular
RT   localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL   J. Bacteriol. 181:3886-3889(1999).
RN   [4]
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   [5]
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   [6]
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   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX   PubMed=27246500; DOI=10.1007/s00284-016-1067-z;
RA   Elsztein C., de Lima R.C.P., de Barros Pita W., de Morais M.A. Jr.;
RT   "NCW2, a gene involved in the tolerance to polyhexamethylene biguanide
RT   (PHMB), may help in the organisation of beta-1,3-glucan structure of
RT   Saccharomyces cerevisiae cell wall.";
RL   Curr. Microbiol. 73:341-345(2016).
CC   -!- FUNCTION: Cell wall biogenesis protein that participates in the
CC       organization of the beta-glucan assembly (PubMed:27246500). Involved in
CC       the mechanism responsible for cell tolerance to polyhexamethylene
CC       biguanide (PHMB), an antifungal agent (PubMed:27246500).
CC       {ECO:0000269|PubMed:27246500}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383953,
CC       ECO:0000269|PubMed:11016834}; Lipid-anchor, GPI-anchor
CC       {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:11016834}.
CC   -!- INDUCTION: Positively regulated by cell integrity signaling through
CC       MPK1 in response to cell wall perturbation (PubMed:10594829,
CC       PubMed:11016834). Induction is dependent on transcription factor RLM1
CC       (PubMed:10594829, PubMed:11016834). Expression is also up-regulated 7-
CC       fold upon exposure to polyhexamethylene biguanide (PHMB)
CC       (PubMed:27246500). {ECO:0000269|PubMed:10594829,
CC       ECO:0000269|PubMed:11016834, ECO:0000269|PubMed:27246500}.
CC   -!- DISRUPTION PHENOTYPE: Reduces significantly the growth rate of cells
CC       exposed to polyhexamethylene biguanide (PHMB) (PubMed:27246500). Leads
CC       to increased resistance to zymolyase treatment, indicating alterations
CC       in the beta-glucan network (PubMed:27246500).
CC       {ECO:0000269|PubMed:27246500}.
CC   -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; U14913; AAB67435.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09513.1; -; Genomic_DNA.
DR   PIR; S48547; S48547.
DR   RefSeq; NP_013295.1; NM_001182081.1.
DR   AlphaFoldDB; Q05777; -.
DR   BioGRID; 31464; 71.
DR   DIP; DIP-4921N; -.
DR   IntAct; Q05777; 1.
DR   MINT; Q05777; -.
DR   STRING; 4932.YLR194C; -.
DR   PaxDb; Q05777; -.
DR   EnsemblFungi; YLR194C_mRNA; YLR194C; YLR194C.
DR   GeneID; 850891; -.
DR   KEGG; sce:YLR194C; -.
DR   SGD; S000004184; NCW2.
DR   VEuPathDB; FungiDB:YLR194C; -.
DR   eggNOG; ENOG502S9J5; Eukaryota.
DR   HOGENOM; CLU_1094809_0_0_1; -.
DR   InParanoid; Q05777; -.
DR   OMA; CANFIAT; -.
DR   BioCyc; YEAST:G3O-32316-MON; -.
DR   PRO; PR:Q05777; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q05777; protein.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:SGD.
DR   GO; GO:0005935; C:cellular bud neck; HDA: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:0005199; F:structural constituent of cell wall; IDA:SGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..232
FT                   /note="Cell wall biogenesis protein NCW2"
FT                   /id="PRO_0000247130"
FT   PROPEP          233..254
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000247131"
FT   REGION          19..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           232
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   254 AA;  25762 MW;  D960873D7441802F CRC64;
     MKACSILFTT LITLAAAQKD SGSLDGQNSE DSSQKESSNS QEITPTTTKE AQESASTVVS
     TGKSLVQTSN VVSNTYAVAP STTVVTTDAQ GKTTTQYLWW VAESNSAVST TSTASVQPTG
     ETSSGITNSA SSSTTSTSTD GPVTIVTTTN SLGETYTSTV WWLPSSATTD NTASSSKSSS
     GSSSKPESST KVVSTIKSTY TTTSGSTVET LTTTYKSTVN GKVASVMSNS TNGAFAGTHI
     AYGAGAFAVG ALLL
 
 
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