CWH43_YEAST
ID CWH43_YEAST Reviewed; 953 AA.
AC P25618; D6VR25; Q8NIM1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein CWH43;
DE AltName: Full=Calcofluor white hypersensitive protein;
GN Name=CWH43; OrderedLocusNames=YCR017C; ORFNames=YCR17C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION TO 229; 329; 634 AND 873.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-57.
RX PubMed=11427965; DOI=10.1002/yea.731;
RA Martin-Yken H., Dagkessamanskaia A., De Groot P., Ram A., Klis F.,
RA Francois J.;
RT "Saccharomyces cerevisiae YCRO17c/CWH43 encodes a putative
RT sensor/transporter protein upstream of the BCK2 branch of the PKC1-
RT dependent cell wall integrity pathway.";
RL Yeast 18:827-840(2001).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLY-57; HIS-472;
RP ASP-693; HIS-770; HIS-771; GLU-807; ASP-862 AND ARG-882.
RX PubMed=17761529; DOI=10.1091/mbc.e07-05-0482;
RA Umemura M., Fujita M., Yoko-O T., Fukamizu A., Jigami Y.;
RT "Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid
RT moiety of GPI anchors to ceramides.";
RL Mol. Biol. Cell 18:4304-4316(2007).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-713 AND HIS-802.
RX PubMed=17714445; DOI=10.1111/j.1365-2958.2007.05883.x;
RA Ghugtyal V., Vionnet C., Roubaty C., Conzelmann A.;
RT "CWH43 is required for the introduction of ceramides into GPI anchors in
RT Saccharomyces cerevisiae.";
RL Mol. Microbiol. 65:1493-1502(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in the maintenance of cell wall integrity. Required
CC for the replacement of the diacylglycerol moiety by ceramides during
CC GPI-anchor maturation. {ECO:0000269|PubMed:11427965,
CC ECO:0000269|PubMed:17714445, ECO:0000269|PubMed:17761529}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC Note=Concentrates to the bud tip of small budded cells and to the neck
CC of dividing cells.
CC -!- DOMAIN: The PGAP2-like region interacts with the PGAP2IP-like region.
CC {ECO:0000269|PubMed:17761529}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PGAP2 family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PGAP2IP family.
CC {ECO:0000305}.
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DR EMBL; X59720; CAC42972.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07494.1; -; Genomic_DNA.
DR PIR; S19427; S19427.
DR RefSeq; NP_009943.2; NM_001178730.1.
DR AlphaFoldDB; P25618; -.
DR SMR; P25618; -.
DR BioGRID; 30996; 180.
DR STRING; 4932.YCR017C; -.
DR TCDB; 9.B.131.1.1; the post-gpi attachment protein (p-gap2) family.
DR iPTMnet; P25618; -.
DR MaxQB; P25618; -.
DR PaxDb; P25618; -.
DR PRIDE; P25618; -.
DR EnsemblFungi; YCR017C_mRNA; YCR017C; YCR017C.
DR GeneID; 850376; -.
DR KEGG; sce:YCR017C; -.
DR SGD; S000000610; CWH43.
DR VEuPathDB; FungiDB:YCR017C; -.
DR eggNOG; KOG3979; Eukaryota.
DR GeneTree; ENSGT00510000048509; -.
DR HOGENOM; CLU_009808_0_0_1; -.
DR InParanoid; P25618; -.
DR OMA; ITAGIWT; -.
DR BioCyc; YEAST:G3O-29332-MON; -.
DR PRO; PR:P25618; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25618; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
DR GO; GO:0005934; C:cellular bud tip; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IGI:UniProtKB.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0006505; P:GPI anchor metabolic process; IMP:SGD.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR027317; PGAP2IP.
DR PANTHER; PTHR14859:SF1; PTHR14859:SF1; 1.
DR Pfam; PF10277; Frag1; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..953
FT /note="Protein CWH43"
FT /id="PRO_0000021052"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..953
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..229
FT /note="PGAP2-like"
FT REGION 230..953
FT /note="PGAP2IP-like"
FT REGION 862..882
FT /note="Required for function in lipid remodeling"
FT ACT_SITE 802
FT /evidence="ECO:0000305"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 57
FT /note="G->R: Causes destabilization of the protein and
FT induces the release of cell wall proteins in the culture
FT medium."
FT /evidence="ECO:0000269|PubMed:11427965,
FT ECO:0000269|PubMed:17761529"
FT MUTAGEN 472
FT /note="H->A: No effect on introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 693
FT /note="D->A: No effect on introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 713
FT /note="D->A: Impairs the introduction of ceramides into the
FT GPI anchor."
FT /evidence="ECO:0000269|PubMed:17714445"
FT MUTAGEN 770
FT /note="H->A: No effect on introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 771
FT /note="H->A: No effect on introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 802
FT /note="H->A: Abrogates the introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17714445"
FT MUTAGEN 807
FT /note="E->A: No effect on introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 862
FT /note="D->A: Impairs the introduction of ceramides into the
FT GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
FT MUTAGEN 882
FT /note="R->A: Abrogates the introduction of ceramides into
FT the GPI anchor."
FT /evidence="ECO:0000269|PubMed:17761529"
SQ SEQUENCE 953 AA; 107883 MW; 9F56CCD85824E848 CRC64;
MLIINGKIIP IAHTICAFSA FFAALVTGYS LHFHKIVTNA HYTYPDEWFP SVSATIGDRY
PERSIFQILI ALTAFPRFLL LLGHYYLNQS KVCFLVGVLR TVSCGGWVYI TSTDDHDIHD
IFMITYIVLT LPWDIMITRY SSPLTSKNKG LTATIFFGTL FPMIYWYIQH SVQQRAGAYS
IYAYFEWSLI LLDIAFDAFA YADFKKIDIV LAFNEKPGNT SFFQIRDSSP INYGEEKSSE
LQKSGEKKVE KEKPVARSAT GSYFRFDSFF YLLTNIFNGF LFWSNVTSLL CSIWHFPLWY
MGISGYEAAI LGYLGPIFLY LPFVSEAFTQ YGVLLGGIIA IGAYIVQMPE LRLISVAVGT
SITVATFVQN LRYITNAETS FSFALTWLLG LVASVILKMG FYTNNPTWVI LDERNGGYNK
TALVLTVLFG MLSPYVNSIN FEGKRNAQAK SASLIGKLFL AVGFGSLLFG IHQLLTDSST
TIYWAWEGYN ESHGPLPWPW GALTCTVMLF ASLSSVKFMG KPLVPCLLLL ISTAVLSARS
ITQWPKYIFG GLLYAIAMLW LVPSYFSALG QVQNIWVYVL SFSVYIIFVL AHVWVVAYAF
VPMGWVLREK IETVLAFSST FIIIGALTCK NLNIQLVTMG KKFFIYVFFF AVALLSLTAR
FVYDIRPTGI PQPYHPDSQL ITAGIWTIHF GLDNDMWASE DRMINLIKDM ELDVVGLLET
DTQRITMGNR DLTSKLAHDL NMYADFGPGP NKHTWGCVLL SKFPIVNSTH HLLPSPVGEL
APAIHATLQT YNDTLVDVFV FHSGQEEDEE DRRLQSNYMA KLMGNTTRPA ILLSYLVVDP
GEGNYNTYVS ETSGMHDIDP SDDDRWCEYI LYRGLRRTGY ARVARGTITD TELQVGKFQV
LSEQALVEHS DSMYEYGHMS EPEYEDMKFP DKFLGEGERG HFYHVFDEPR YYL
