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   27-MAR-2024, entry version 180.
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;
GN   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; 109.
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   GlyCosmos; P32623; 9 sites, No reported glycans.
DR   GlyGen; P32623; 9 sites.
DR   iPTMnet; P32623; -.
DR   MaxQB; P32623; -.
DR   PaxDb; 4932-YEL040W; -.
DR   PeptideAtlas; P32623; -.
DR   EnsemblFungi; YEL040W_mRNA; YEL040W; YEL040W.
DR   GeneID; 856671; -.
DR   KEGG; sce:YEL040W; -.
DR   AGR; SGD:S000000766; -.
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; WNATANQ; -.
DR   OrthoDB; 337487at2759; -.
DR   BioCyc; YEAST:G3O-30161-MONOMER; -.
DR   BioGRID-ORCS; 856671; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P32623; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P32623; Protein.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   CDD; cd06923; ChtBD1_GH16; 1.
DR   CDD; cd02183; GH16_fungal_CRH1_transglycosylase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR017168; Glyco_hydro_16_CRH1_prd.
DR   PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   PIRSF; PIRSF037299; Glycosidase_CRH1_prd; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//