RRT12_YEAST
ID RRT12_YEAST Reviewed; 491 AA.
AC P25381; D6VR54;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Subtilase-type proteinase RRT12;
DE EC=3.4.21.-;
DE AltName: Full=Outer spore wall protein 3;
DE AltName: Full=Regulator of rDNA transcription protein 12;
DE Flags: Precursor;
GN Name=RRT12; Synonyms=OSW3; OrderedLocusNames=YCR045C; ORFNames=YCR45C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 GENE NAME, AND FUNCTION.
RX PubMed=19270272; DOI=10.1534/genetics.108.100313;
RA Hontz R.D., Niederer R.O., Johnson J.M., Smith J.S.;
RT "Genetic identification of factors that modulate ribosomal DNA
RT transcription in Saccharomyces cerevisiae.";
RL Genetics 182:105-119(2009).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-365.
RX PubMed=19779569; DOI=10.1371/journal.pone.0007184;
RA Suda Y., Rodriguez R.K., Coluccio A.E., Neiman A.M.;
RT "A screen for spore wall permeability mutants identifies a secreted
RT protease required for proper spore wall assembly.";
RL PLoS ONE 4:E7184-E7184(2009).
CC -!- FUNCTION: Subtilisin-related protease involved in the formation of a
CC protective dityrosine layer required for spore wall assembly.
CC Identified in a screen for mutants with increased levels of rDNA
CC transcription. {ECO:0000269|PubMed:19270272,
CC ECO:0000269|PubMed:19779569}.
CC -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:19779569}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42293.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07523.1; -; Genomic_DNA.
DR PIR; S19458; S19458.
DR RefSeq; NP_009974.1; NM_001178759.1.
DR AlphaFoldDB; P25381; -.
DR SMR; P25381; -.
DR BioGRID; 31027; 51.
DR DIP; DIP-1543N; -.
DR IntAct; P25381; 1.
DR MINT; P25381; -.
DR STRING; 4932.YCR045C; -.
DR MEROPS; S08.A50; -.
DR PaxDb; P25381; -.
DR PRIDE; P25381; -.
DR EnsemblFungi; YCR045C_mRNA; YCR045C; YCR045C.
DR GeneID; 850412; -.
DR KEGG; sce:YCR045C; -.
DR SGD; S000000641; RRT12.
DR VEuPathDB; FungiDB:YCR045C; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_0_1; -.
DR InParanoid; P25381; -.
DR OMA; YWASPAS; -.
DR BioCyc; YEAST:G3O-29356-MON; -.
DR PRO; PR:P25381; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25381; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease;
KW Signal; Sporulation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..491
FT /note="Subtilase-type proteinase RRT12"
FT /id="PRO_0000027205"
FT DOMAIN 142..442
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 365
FT /note="S->A: Abolishes protease activity."
FT /evidence="ECO:0000269|PubMed:19779569"
SQ SEQUENCE 491 AA; 55068 MW; 7C8000FF84CDDF5D CRC64;
MKPQCILISL LVNLAYAEEY LVRFKNPTAF QQFTSNSNRS WRQFIDNKIE KKFSIGSFRG
VTMNLSKNLV NKLKKSPLVA DIVPNFRFEA FEGDSVNSAE SSYTFNATAK YSYEDVEEEQ
NITYQPDAPR HLARISRHYQ LPFDVGDKDR YKSWFNYYYE HDYQGQDVNA YIMDTGIFAD
HPEFEDRVIQ GIDLTKEGFG DQNGHGTHVA GLVGSKTYGA AKRVNLVEVK VLGKDGSGEA
SNVLSGLEFI VEHCTKVSRP QGKKCVANLS LGSFRSPIIN MAVEGAIEEG IVFVAAAGNF
NLDAYWASPA SAENVITVGA FDDHIDTIAK FSNWGPCVNI FAPGVEIESL SHLNYNDTLI
LSGTSMSTPI VTGVAAILLS KGIEPEMIAQ EIEYLSTRNV FHRRTLFFKP STPNQILYNG
VDKLDDPYDD ETFPRLNIEA IAKELEEYNA TLQTPMSENL QSGSKLWGWN NDVTLPLGEI
RLKRRDFMKN L
