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P25618 (CWH43_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein CWH43
Alternative name(s):
Calcofluor white hypersensitive protein
Gene names
Name:CWH43
Ordered Locus Names:YCR017C
ORF Names:YCR17C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation. Ref.4 Ref.6 Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: Concentrates to the bud tip of small budded cells and to the neck of dividing cells. Ref.4 Ref.6

Domain

The PGAP2-like region interacts with the PGAP2IP-like region. Ref.6

Sequence similarities

In the N-terminal section; belongs to the PGAP2 family.

In the C-terminal section; belongs to the PGAP2IP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Protein CWH43
PRO_0000021052

Regions

Topological domain1 – 77Cytoplasmic Potential
Topological domain29 – 6436Extracellular Potential
Transmembrane65 – 8521Helical; Potential
Topological domain86 – 916Cytoplasmic Potential
Transmembrane92 – 11221Helical; Potential
Topological domain113 – 1175Extracellular Potential
Transmembrane118 – 13821Helical; Potential
Topological domain139 – 14911Cytoplasmic Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 1755Extracellular Potential
Transmembrane176 – 19621Helical; Potential
Topological domain197 – 27882Cytoplasmic Potential
Transmembrane279 – 29921Helical; Potential
Topological domain300 – 3078Extracellular Potential
Transmembrane308 – 32821Helical; Potential
Topological domain329 – 3302Cytoplasmic Potential
Transmembrane331 – 35121Helical; Potential
Topological domain3521Extracellular Potential
Transmembrane353 – 36816Helical; Potential
Topological domain369 – 38012Cytoplasmic Potential
Transmembrane381 – 40121Helical; Potential
Topological domain402 – 42019Extracellular Potential
Transmembrane421 – 44121Helical; Potential
Topological domain442 – 4509Cytoplasmic Potential
Transmembrane451 – 47121Helical; Potential
Topological domain472 – 49524Extracellular Potential
Transmembrane496 – 51621Helical; Potential
Topological domain5171Cytoplasmic Potential
Transmembrane518 – 53821Helical; Potential
Topological domain539 – 5479Extracellular Potential
Transmembrane548 – 56821Helical; Potential
Topological domain569 – 58517Cytoplasmic Potential
Transmembrane586 – 60621Helical; Potential
Topological domain607 – 6137Extracellular Potential
Transmembrane614 – 63421Helical; Potential
Topological domain635 – 6428Cytoplasmic Potential
Transmembrane643 – 66321Helical; Potential
Topological domain664 – 953290Extracellular Potential
Region1 – 229229PGAP2-like
Region230 – 953724PGAP2IP-like
Region862 – 88221Required for function in lipid remodeling

Sites

Active site8021 Probable

Amino acid modifications

Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4901N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation7921N-linked (GlcNAc...) Potential
Glycosylation8251N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis571G → R: Causes destabilization of the protein and induces the release of cell wall proteins in the culture medium. Ref.4 Ref.6
Mutagenesis4721H → A: No effect on introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis6931D → A: No effect on introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis7131D → A: Impairs the introduction of ceramides into the GPI anchor. Ref.7
Mutagenesis7701H → A: No effect on introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis7711H → A: No effect on introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis8021H → A: Abrogates the introduction of ceramides into the GPI anchor. Ref.7
Mutagenesis8071E → A: No effect on introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis8621D → A: Impairs the introduction of ceramides into the GPI anchor. Ref.6
Mutagenesis8821R → A: Abrogates the introduction of ceramides into the GPI anchor. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P25618 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: 9F56CCD85824E848

FASTA953107,883
        10         20         30         40         50         60 
MLIINGKIIP IAHTICAFSA FFAALVTGYS LHFHKIVTNA HYTYPDEWFP SVSATIGDRY 

        70         80         90        100        110        120 
PERSIFQILI ALTAFPRFLL LLGHYYLNQS KVCFLVGVLR TVSCGGWVYI TSTDDHDIHD 

       130        140        150        160        170        180 
IFMITYIVLT LPWDIMITRY SSPLTSKNKG LTATIFFGTL FPMIYWYIQH SVQQRAGAYS 

       190        200        210        220        230        240 
IYAYFEWSLI LLDIAFDAFA YADFKKIDIV LAFNEKPGNT SFFQIRDSSP INYGEEKSSE 

       250        260        270        280        290        300 
LQKSGEKKVE KEKPVARSAT GSYFRFDSFF YLLTNIFNGF LFWSNVTSLL CSIWHFPLWY 

       310        320        330        340        350        360 
MGISGYEAAI LGYLGPIFLY LPFVSEAFTQ YGVLLGGIIA IGAYIVQMPE LRLISVAVGT 

       370        380        390        400        410        420 
SITVATFVQN LRYITNAETS FSFALTWLLG LVASVILKMG FYTNNPTWVI LDERNGGYNK 

       430        440        450        460        470        480 
TALVLTVLFG MLSPYVNSIN FEGKRNAQAK SASLIGKLFL AVGFGSLLFG IHQLLTDSST 

       490        500        510        520        530        540 
TIYWAWEGYN ESHGPLPWPW GALTCTVMLF ASLSSVKFMG KPLVPCLLLL ISTAVLSARS 

       550        560        570        580        590        600 
ITQWPKYIFG GLLYAIAMLW LVPSYFSALG QVQNIWVYVL SFSVYIIFVL AHVWVVAYAF 

       610        620        630        640        650        660 
VPMGWVLREK IETVLAFSST FIIIGALTCK NLNIQLVTMG KKFFIYVFFF AVALLSLTAR 

       670        680        690        700        710        720 
FVYDIRPTGI PQPYHPDSQL ITAGIWTIHF GLDNDMWASE DRMINLIKDM ELDVVGLLET 

       730        740        750        760        770        780 
DTQRITMGNR DLTSKLAHDL NMYADFGPGP NKHTWGCVLL SKFPIVNSTH HLLPSPVGEL 

       790        800        810        820        830        840 
APAIHATLQT YNDTLVDVFV FHSGQEEDEE DRRLQSNYMA KLMGNTTRPA ILLSYLVVDP 

       850        860        870        880        890        900 
GEGNYNTYVS ETSGMHDIDP SDDDRWCEYI LYRGLRRTGY ARVARGTITD TELQVGKFQV 

       910        920        930        940        950 
LSEQALVEHS DSMYEYGHMS EPEYEDMKFP DKFLGEGERG HFYHVFDEPR YYL 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 229; 329; 634 AND 873.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Saccharomyces cerevisiae YCRO17c/CWH43 encodes a putative sensor/transporter protein upstream of the BCK2 branch of the PKC1-dependent cell wall integrity pathway."
Martin-Yken H., Dagkessamanskaia A., De Groot P., Ram A., Klis F., Francois J.
Yeast 18:827-840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-57.
[5]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[6]"Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides."
Umemura M., Fujita M., Yoko-O T., Fukamizu A., Jigami Y.
Mol. Biol. Cell 18:4304-4316(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF GLY-57; HIS-472; ASP-693; HIS-770; HIS-771; GLU-807; ASP-862 AND ARG-882.
[7]"CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae."
Ghugtyal V., Vionnet C., Roubaty C., Conzelmann A.
Mol. Microbiol. 65:1493-1502(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-713 AND HIS-802.
[8]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59720 Genomic DNA. Translation: CAC42972.1.
BK006937 Genomic DNA. Translation: DAA07494.1.
PIRS19427.
RefSeqNP_009943.2. NM_001178730.1.

3D structure databases

ProteinModelPortalP25618.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30996. 83 interactions.
MINTMINT-4478332.
STRING4932.YCR017C.

Protein family/group databases

TCDB9.B.131.1.1. the post-gpi attachment protein (p-gap2) family.

Proteomic databases

PaxDbP25618.
PeptideAtlasP25618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR017C; YCR017C; YCR017C.
GeneID850376.
KEGGsce:YCR017C.

Organism-specific databases

CYGDYCR017c.
SGDS000000610. CWH43.

Phylogenomic databases

eggNOGNOG309644.
GeneTreeENSGT00510000048509.
HOGENOMHOG000196377.
OMAGNRDTTQ.
OrthoDBEOG77DJF6.

Enzyme and pathway databases

BioCycYEAST:G3O-29332-MONOMER.

Gene expression databases

GenevestigatorP25618.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR019402. Frag1/DRAM/Sfk1.
IPR027317. PGAP2IP.
[Graphical view]
PANTHERPTHR14859:SF0. PTHR14859:SF0. 1 hit.
PfamPF10277. Frag1. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
ProtoNetSearch...

Other

NextBio965875.
PROP25618.

Entry information

Entry nameCWH43_YEAST
AccessionPrimary (citable) accession number: P25618
Secondary accession number(s): D6VR25, Q8NIM1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 24, 2003
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families