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Protein

Subtilase-type proteinase RRT12

Gene

RRT12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Subtilisin-related protease involved in the formation of a protective dityrosine layer required for spore wall assembly. Identified in a screen for mutants with increased levels of rDNA transcription.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei174 – 1741Charge relay systemBy similarity
Active sitei205 – 2051Charge relay systemBy similarity
Active sitei365 – 3651Charge relay systemBy similarity

GO - Molecular functioni

  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: SGD

GO - Biological processi

  • ascospore wall assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29356-MONOMER.

Protein family/group databases

MEROPSiS08.A50.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilase-type proteinase RRT12 (EC:3.4.21.-)
Alternative name(s):
Outer spore wall protein 3
Regulator of rDNA transcription protein 12
Gene namesi
Name:RRT12
Synonyms:OSW3
Ordered Locus Names:YCR045C
ORF Names:YCR45C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR045C.
SGDiS000000641. RRT12.

Subcellular locationi

GO - Cellular componenti

  • ascospore wall Source: SGD
  • nuclear envelope Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3651S → A: Abolishes protease activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 491474Subtilase-type proteinase RRT12PRO_0000027205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence analysis
Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence analysis
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

BioGridi31027. 4 interactions.
DIPiDIP-1543N.
IntActiP25381. 1 interaction.
MINTiMINT-405645.

Structurei

3D structure databases

ProteinModelPortaliP25381.
SMRiP25381. Positions 16-443.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 389234Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00490000043472.
InParanoidiP25381.
KOiK14644.
OMAiCVDVFAS.
OrthoDBiEOG7WT4B5.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 2 hits.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPQCILISL LVNLAYAEEY LVRFKNPTAF QQFTSNSNRS WRQFIDNKIE
60 70 80 90 100
KKFSIGSFRG VTMNLSKNLV NKLKKSPLVA DIVPNFRFEA FEGDSVNSAE
110 120 130 140 150
SSYTFNATAK YSYEDVEEEQ NITYQPDAPR HLARISRHYQ LPFDVGDKDR
160 170 180 190 200
YKSWFNYYYE HDYQGQDVNA YIMDTGIFAD HPEFEDRVIQ GIDLTKEGFG
210 220 230 240 250
DQNGHGTHVA GLVGSKTYGA AKRVNLVEVK VLGKDGSGEA SNVLSGLEFI
260 270 280 290 300
VEHCTKVSRP QGKKCVANLS LGSFRSPIIN MAVEGAIEEG IVFVAAAGNF
310 320 330 340 350
NLDAYWASPA SAENVITVGA FDDHIDTIAK FSNWGPCVNI FAPGVEIESL
360 370 380 390 400
SHLNYNDTLI LSGTSMSTPI VTGVAAILLS KGIEPEMIAQ EIEYLSTRNV
410 420 430 440 450
FHRRTLFFKP STPNQILYNG VDKLDDPYDD ETFPRLNIEA IAKELEEYNA
460 470 480 490
TLQTPMSENL QSGSKLWGWN NDVTLPLGEI RLKRRDFMKN L
Length:491
Mass (Da):55,068
Last modified:May 1, 1992 - v1
Checksum:i7C8000FF84CDDF5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42293.1.
BK006937 Genomic DNA. Translation: DAA07523.1.
PIRiS19458.
RefSeqiNP_009974.1. NM_001178759.1.

Genome annotation databases

EnsemblFungiiCAA42293; CAA42293; CAA42293.
YCR045C; YCR045C; YCR045C.
GeneIDi850412.
KEGGisce:YCR045C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42293.1.
BK006937 Genomic DNA. Translation: DAA07523.1.
PIRiS19458.
RefSeqiNP_009974.1. NM_001178759.1.

3D structure databases

ProteinModelPortaliP25381.
SMRiP25381. Positions 16-443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31027. 4 interactions.
DIPiDIP-1543N.
IntActiP25381. 1 interaction.
MINTiMINT-405645.

Protein family/group databases

MEROPSiS08.A50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42293; CAA42293; CAA42293.
YCR045C; YCR045C; YCR045C.
GeneIDi850412.
KEGGisce:YCR045C.

Organism-specific databases

EuPathDBiFungiDB:YCR045C.
SGDiS000000641. RRT12.

Phylogenomic databases

GeneTreeiENSGT00490000043472.
InParanoidiP25381.
KOiK14644.
OMAiCVDVFAS.
OrthoDBiEOG7WT4B5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29356-MONOMER.

Miscellaneous databases

PROiP25381.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 2 hits.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. S8pro/Inhibitor_I9.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Genetic identification of factors that modulate ribosomal DNA transcription in Saccharomyces cerevisiae."
    Hontz R.D., Niederer R.O., Johnson J.M., Smith J.S.
    Genetics 182:105-119(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME, FUNCTION.
  4. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].
  5. "A screen for spore wall permeability mutants identifies a secreted protease required for proper spore wall assembly."
    Suda Y., Rodriguez R.K., Coluccio A.E., Neiman A.M.
    PLoS ONE 4:E7184-E7184(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-365.

Entry informationi

Entry nameiRRT12_YEAST
AccessioniPrimary (citable) accession number: P25381
Secondary accession number(s): D6VR54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 8, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.