CRR1_YEAST
ID CRR1_YEAST Reviewed; 422 AA.
AC Q05790; D6VYL4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Probable glycosidase CRR1;
DE EC=3.2.-.-;
DE AltName: Full=CRH-related protein 1;
DE Flags: Precursor;
GN Name=CRR1; OrderedLocusNames=YLR213C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INDUCTION.
RX PubMed=10922376; DOI=10.1074/jbc.m005946200;
RA Gross C., Kelleher M., Iyer V.R., Brown P.O., Winge D.R.;
RT "Identification of the copper regulon in Saccharomyces cerevisiae by DNA
RT microarrays.";
RL J. Biol. Chem. 275:32310-32316(2000).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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 [5]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15470107; DOI=10.1099/mic.0.27314-0;
RA Gomez-Esquer F., Rodriguez-Pena J.M., Diaz G., Rodriguez E., Briza P.,
RA Nombela C., Arroyo J.;
RT "CRR1, a gene encoding a putative transglycosidase, is required for proper
RT spore wall assembly in Saccharomyces cerevisiae.";
RL Microbiology 150:3269-3280(2004).
RN [6]
RP FUNCTION.
RX PubMed=15886332; DOI=10.1152/physiolgenomics.00055.2005;
RA van Bakel H., Strengman E., Wijmenga C., Holstege F.C.P.;
RT "Gene expression profiling and phenotype analyses of S. cerevisiae in
RT response to changing copper reveals six genes with new roles in copper and
RT iron metabolism.";
RL Physiol. Genomics 22:356-367(2005).
CC -!- FUNCTION: Spore specific glycosidase involved in spore wall assembly
CC during sporulation. May be involved in copper import.
CC {ECO:0000269|PubMed:10757808, ECO:0000269|PubMed:15470107,
CC ECO:0000269|PubMed:15886332}.
CC -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:15470107}.
CC Note=Spore wall envelope.
CC -!- DEVELOPMENTAL STAGE: Expressed in spores. {ECO:0000269|PubMed:10757808,
CC ECO:0000269|PubMed:15470107}.
CC -!- INDUCTION: Expression is increased in low copper conditions, probably
CC through the transcription regulation by the copper regulon
CC transcription factor MAC1. {ECO:0000269|PubMed:10922376}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. CRR1
CC subfamily. {ECO:0000305}.
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DR EMBL; U14913; AAB67443.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09530.1; -; Genomic_DNA.
DR PIR; S48564; S48564.
DR RefSeq; NP_013314.1; NM_001182100.1.
DR AlphaFoldDB; Q05790; -.
DR SMR; Q05790; -.
DR BioGRID; 31481; 29.
DR DIP; DIP-822N; -.
DR IntAct; Q05790; 1.
DR MINT; Q05790; -.
DR STRING; 4932.YLR213C; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q05790; -.
DR PRIDE; Q05790; -.
DR EnsemblFungi; YLR213C_mRNA; YLR213C; YLR213C.
DR GeneID; 850910; -.
DR KEGG; sce:YLR213C; -.
DR SGD; S000004203; CRR1.
DR VEuPathDB; FungiDB:YLR213C; -.
DR eggNOG; ENOG502QVQI; Eukaryota.
DR GeneTree; ENSGT00940000176705; -.
DR HOGENOM; CLU_039093_0_0_1; -.
DR InParanoid; Q05790; -.
DR OMA; WPCCSPY; -.
DR BioCyc; YEAST:G3O-32330-MON; -.
DR PRO; PR:Q05790; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05790; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; ISS:SGD.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006037; P:cell wall chitin metabolic process; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR InterPro; IPR008264; Beta_glucanase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR00737; GLHYDRLASE16.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Glycosidase; Hydrolase; Reference proteome; Signal; Sporulation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..422
FT /note="Probable glycosidase CRR1"
FT /id="PRO_0000228141"
FT DOMAIN 67..339
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 221
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47356 MW; 0158DB41F7E97B83 CRC64;
MRISILQLVP VVGYIGFALG ELYKPKNSIS CSPNNPCPAE WPCCSPYNEC GAGPICVGGC
NVRSSFDEES CAPIPALVAS QKLEFVSTPK VPKFIVNYQP KPPIREGNGP NKANTKVGVV
EGELNSKRII HYAKFLVTPD SKEAEKMLED FDFTHSGYTS IEASSGNIVL AMPKKTTGSL
ITSTRSFLYG KASVRMKTAR SRGVVTAFDL TSAIGDEIDF EWLGGDLMTA QSNYYSQGHL
DYTRMQRFPV GADTWATYHT YEIDWDPDRI IWYVDGKIAR TVLKKDTWDP ISKEYRYPQT
PMRLEIAVWP GGSETNGPGT INWAGGLIDW ENSPDIIEKG QFTAHVEQIT VTPYQNKFTE
QVQFCIKAKK KAPTFSQKDL SRVVVSYNRQ DRLNHHDEGS LKWDCFVTPK INDWLSSWKR
SK
