SPR1_YEAST
ID SPR1_YEAST Reviewed; 445 AA.
AC P32603; D6W2P6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Sporulation-specific glucan 1,3-beta-glucosidase;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase;
DE Flags: Precursor;
GN Name=SPR1; Synonyms=SSG1; OrderedLocusNames=YOR190W;
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].
RX PubMed=8419289; DOI=10.1128/jb.175.2.386-394.1993;
RA Muthukumar G., Suhng S.-H., Magee P.T., Jewell R.D., Primerano D.A.;
RT "The Saccharomyces cerevisiae SPR1 gene encodes a sporulation-specific exo-
RT 1,3-beta-glucanase which contributes to ascospore thermoresistance.";
RL J. Bacteriol. 175:386-394(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8509335; DOI=10.1128/jb.175.12.3823-3837.1993;
RA San Segundo P., Correa J., Vazquez de Aldana C.R., del Rey F.;
RT "SSG1, a gene encoding a sporulation-specific 1,3-beta-glucanase in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 175:3823-3837(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Probably involved in the processes of spore formation and
CC contributes to ascospore thermoresistance by participating in the
CC morphogenesis of ascospore walls. The enzyme may do this by modifying
CC glucan linkages in the developing ascospore wall, thus strengthening it
CC or lending it plasticity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Late stages of sporulation, during ascospore wall
CC formation. Probably functions before partitioning of nuclei or is
CC distributed to developing ascospores prior to the completion of pro-
CC spore walls.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; S52935; AAB24895.1; -; Genomic_DNA.
DR EMBL; X59259; CAA41952.1; -; Genomic_DNA.
DR EMBL; Z75098; CAA99399.1; -; Genomic_DNA.
DR EMBL; AY723868; AAU09785.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10962.1; -; Genomic_DNA.
DR PIR; A40639; A40639.
DR RefSeq; NP_014833.3; NM_001183609.3.
DR AlphaFoldDB; P32603; -.
DR SMR; P32603; -.
DR BioGRID; 34585; 41.
DR DIP; DIP-3910N; -.
DR STRING; 4932.YOR190W; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR CLAE; EXG5C_YEAST; -.
DR PaxDb; P32603; -.
DR PRIDE; P32603; -.
DR EnsemblFungi; YOR190W_mRNA; YOR190W; YOR190W.
DR GeneID; 854362; -.
DR KEGG; sce:YOR190W; -.
DR SGD; S000005716; SPR1.
DR VEuPathDB; FungiDB:YOR190W; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR GeneTree; ENSGT00940000176313; -.
DR HOGENOM; CLU_004624_0_1_1; -.
DR InParanoid; P32603; -.
DR OMA; DTHHYQV; -.
DR BioCyc; YEAST:YOR190W-MON; -.
DR PRO; PR:P32603; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32603; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IMP:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006073; P:cellular glucan metabolic process; IBA:GO_Central.
DR GO; GO:0009251; P:glucan catabolic process; IBA:GO_Central.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Reference proteome; Secreted; Signal; Sporulation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..445
FT /note="Sporulation-specific glucan 1,3-beta-glucosidase"
FT /id="PRO_0000007898"
FT ACT_SITE 233
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 51809 MW; 0948A6E4703D41D4 CRC64;
MVSFRGLTTL TLLFTKLVNC NPVSTKNRDS IQFIYKEKDS IYSAINNQAI NEKIHGVNLG
GWLVLEPYIT PSLFETFRTN PYNDDGIPVD EYHFCEKLGY EKAKERLYSH WSTFYKEEDF
AKIASQGFNL VRIPIGYWAF TTLSHDPYVT AEQEYFLDRA IDWARKYGLK VWIDLHGAAG
SQNGFDNSGL RDSYKFLEDE NLSATMKALT YILSKYSTDV YLDTVIGIEL LNEPLGPVID
MERLKNLLLK PAYDYLRNKI NSNQIIVIHD AFQPYHYWDG FLNDEKNEYG VIIDHHHYQV
FSQVELTRKM NERIKIACQW GKDAVSEKHW SVAGEFSAAL TDCTKWLNGV GLGARYDGSW
TKDNEKSHYI NTCANNENIA LWPEERKQNT RKFIEAQLDA FEMTGGWIMW CYKTENSIEW
DVEKLIQLNI FPQPINDRKY PNQCH
