CRH1_YEAST
ID CRH1_YEAST Reviewed; 507 AA.
AC P53301; D6VUX2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Probable glycosidase CRH1;
DE EC=3.2.-.-;
DE AltName: Full=Congo red hypersensitive protein 1;
DE Flags: Precursor;
GN Name=CRH1; OrderedLocusNames=YGR189C; ORFNames=G7553;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10757808; DOI=10.1128/mcb.20.9.3245-3255.2000;
RA Rodriguez-Pena J.M., Cid V.J., Arroyo J., Nombela C.;
RT "A novel family of cell wall-related proteins regulated differently during
RT the yeast life cycle.";
RL Mol. Cell. Biol. 20:3245-3255(2000).
RN [7]
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 [8]
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 [9]
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).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY HEAT STRESS.
RX PubMed=17302808; DOI=10.1111/j.1365-2958.2006.05565.x;
RA Cabib E., Blanco N., Grau C., Rodriguez-Pena J.M., Arroyo J.;
RT "Crh1p and Crh2p are required for the cross-linking of chitin to beta(1-
RT 6)glucan in the Saccharomyces cerevisiae cell wall.";
RL Mol. Microbiol. 63:921-935(2007).
CC -!- FUNCTION: Probable glycosidase that plays a role in cell wall
CC architecture. Required for the transfer of chitin to 1,6-beta-glucan in
CC the cell wall. {ECO:0000269|PubMed:10757808,
CC ECO:0000269|PubMed:17302808}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP), localized particularly in chitin-rich areas. Found at the
CC incipient bud site, around the septum area in later stages of budding,
CC and in ascospore envelopes. Redistributes uniformly over the cell
CC cortex upon heat stress.
CC -!- INDUCTION: Positively regulated by cell integrity signaling through
CC MPK1 in response to cell wall perturbation. Induced by heat stress.
CC {ECO:0000269|PubMed:10594829, ECO:0000269|PubMed:11016834,
CC ECO:0000269|PubMed:17302808}.
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 -!- MISCELLANEOUS: Present with 44000 wall-bound molecules/cell in log
CC phase YPD medium. {ECO:0000269|PubMed:17617218}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRH1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z72974; CAA97215.1; -; Genomic_DNA.
DR EMBL; X99074; CAA67525.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08283.1; -; Genomic_DNA.
DR PIR; S64507; S64507.
DR RefSeq; NP_011705.1; NM_001181318.1.
DR AlphaFoldDB; P53301; -.
DR SMR; P53301; -.
DR BioGRID; 33442; 44.
DR DIP; DIP-4360N; -.
DR IntAct; P53301; 1.
DR STRING; 4932.YGR189C; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; P53301; -.
DR MaxQB; P53301; -.
DR PaxDb; P53301; -.
DR PRIDE; P53301; -.
DR EnsemblFungi; YGR189C_mRNA; YGR189C; YGR189C.
DR GeneID; 853102; -.
DR KEGG; sce:YGR189C; -.
DR SGD; S000003421; CRH1.
DR VEuPathDB; FungiDB:YGR189C; -.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_027506_2_1_1; -.
DR InParanoid; P53301; -.
DR OMA; PMNVRIG; -.
DR BioCyc; YEAST:G3O-30879-MON; -.
DR PRO; PR:P53301; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53301; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA: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:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:SGD.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006037; P:cell wall chitin metabolic process; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..482
FT /note="Probable glycosidase CRH1"
FT /id="PRO_0000045430"
FT PROPEP 483..507
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000045431"
FT DOMAIN 34..260
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 329..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 138
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 482
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 52758 MW; 7D7B61F57AEA942C CRC64;
MKVLDLLTVL SASSLLSTFA AAESTATADS TTAASSTASC NPLKTTGCTP DTALATSFSE
DFSSSSKWFT DLKHAGEIKY GSDGLSMTLA KRYDNPSLKS NFYIMYGKLE VILKAANGTG
IVSSFYLQSD DLDEIDIEWV GGDNTQFQSN FFSKGDTTTY DRGEFHGVDT PTDKFHNYTL
DWAMDKTTWY LDGESVRVLS NTSSEGYPQS PMYLMMGIWA GGDPDNAAGT IEWAGGETNY
NDAPFTMYIE KVIVTDYSTG KKYTYGDQSG SWESIEADGG SIYGRYDQAQ EDFAVLANGG
SISSSSTSSS TVSSSASSTV SSSVSSTVSS SASSTVSSSV SSTVSSSSSV SSSSSTSPSS
STATSSKTLA SSSVTTSSSI SSFEKQSSSS SKKTVASSST SESIISSTKT PATVSSTTRS
TVAPTTQQSS VSSDSPVQDK GGVATSSNDV TSSTTQISSK YTSTIQSSSS EASSTNSVQI
SNGADLAQSL PREGKLFSVL VALLALL
