CRH2_YEAST
ID CRH2_YEAST Reviewed; 467 AA.
AC P32623; D3DLK9; Q6B1R6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Probable glycosidase CRH2;
DE EC=3.2.-.-;
DE AltName: Full=Congo red hypersensitive protein 2;
DE AltName: Full=Unknown transcript 2 protein;
DE Flags: Precursor;
GN Name=UTR2; Synonyms=CRH2; OrderedLocusNames=YEL040W; ORFNames=SYGP-ORF18;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 76-467.
RC STRAIN=B-6441;
RX PubMed=8411151; DOI=10.1006/jmbi.1993.1518;
RA Melnick L., Sherman F.;
RT "The gene clusters ARC and COR on chromosomes 5 and 10, respectively, of
RT Saccharomyces cerevisiae share a common ancestry.";
RL J. Mol. Biol. 233:372-388(1993).
RN [5]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=12045225; DOI=10.1242/jcs.115.12.2549;
RA Rodriguez-Pena J.M., Rodriguez C., Alvarez A., Nombela C., Arroyo J.;
RT "Mechanisms for targeting of the Saccharomyces cerevisiae GPI-anchored cell
RT wall protein Crh2p to polarised growth sites.";
RL J. Cell Sci. 115:2549-2558(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 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. Localizes to sites
CC of polarized growth. Found at the incipient bud site, as a ring at the
CC bud neck as the bud grows, and in the septum at the time of
CC cytokinesis. Redistributes uniformly over the cell cortex upon heat
CC stress.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB28444.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18779; AAB65002.1; -; Genomic_DNA.
DR EMBL; AY693014; AAT93033.1; -; Genomic_DNA.
DR EMBL; L22173; AAA34941.1; ALT_FRAME; Genomic_DNA.
DR EMBL; S65964; AAD13975.1; ALT_FRAME; Genomic_DNA.
DR EMBL; S66130; AAB28444.1; ALT_FRAME; mRNA.
DR EMBL; BK006939; DAA07613.1; -; Genomic_DNA.
DR PIR; S30839; S30839.
DR RefSeq; NP_010874.3; NM_001178855.3.
DR AlphaFoldDB; P32623; -.
DR SMR; P32623; -.
DR BioGRID; 36689; 93.
DR DIP; DIP-7767N; -.
DR MINT; P32623; -.
DR STRING; 4932.YEL040W; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; P32623; -.
DR MaxQB; P32623; -.
DR PaxDb; P32623; -.
DR PRIDE; P32623; -.
DR EnsemblFungi; YEL040W_mRNA; YEL040W; YEL040W.
DR GeneID; 856671; -.
DR KEGG; sce:YEL040W; -.
DR SGD; S000000766; UTR2.
DR VEuPathDB; FungiDB:YEL040W; -.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR GeneTree; ENSGT00940000176705; -.
DR HOGENOM; CLU_040459_0_0_1; -.
DR InParanoid; P32623; -.
DR OMA; CYDPPSG; -.
DR BioCyc; YEAST:G3O-30161-MON; -.
DR PRO; PR:P32623; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32623; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000144; C:cellular bud neck septin ring; 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: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; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..445
FT /note="Probable glycosidase CRH2"
FT /id="PRO_0000065745"
FT PROPEP 446..467
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000232722"
FT DOMAIN 63..280
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 337..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 445
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 130
FT /note="L -> V (in Ref. 4; AAA34941/AAD13975/AAB28444)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="A -> R (in Ref. 4; AAA34941/AAD13975/AAB28444)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> C (in Ref. 4; AAA34941/AAD13975/AAB28444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 49906 MW; B6AE762B5489AA3A CRC64;
MAIVNSWLIC LVSIFSFVVR VEAATFCNAT QACPEDKPCC SQYGECGTGQ YCLNNCDVRY
SFSHDSCMPV PICKSSSTKF KDYSSKLGNA NTFLGNVSEA DWLYTGDVLD YDDEESLILA
MPKNSGGTVL SSTRAVWYGK VSARIKTSHL AGVVTGFILY SGAGDELDYE FVGADLETAQ
TNFYWESVLN YTNSANISTT DTFENYHTYE LDWHEDYVTW SIDGVVGRTL YKNETYNATT
QKYQYPQTPS KVDISIWPGG NSTNAPGTIA WSGGEINWDA SDISNPGYYY AIVNEVNITC
YDPPSDTKKN GTSAYVYTSS SEFLAKDIAI TDDEVMMDSD EGSGLDPHKG ATTSSTQKSS
SSTATSSSKT SSDHSSSTKK SSKTSSTASS SSSSSSSSSS SSSTATKNGD KVVSSVSSSV
TSQTQTTSSV SGSASSSTSS MSGNNAGANV AANWRLTVLC VILGYVL
