RIM13_YEAST
ID RIM13_YEAST Reviewed; 727 AA.
AC Q03792; D6VZX5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Calpain-like protease 1;
DE EC=3.4.22.-;
DE AltName: Full=Calpain-7;
DE AltName: Full=Cysteine protease RIM13;
DE AltName: Full=Regulator of IME2 protein 13;
GN Name=RIM13; Synonyms=CPL1; OrderedLocusNames=YMR154C; ORFNames=YM8520.03C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 FUNCTION.
RX PubMed=9017390; DOI=10.1093/genetics/145.1.63;
RA Li W., Mitchell A.P.;
RT "Proteolytic activation of Rim1p, a positive regulator of yeast sporulation
RT and invasive growth.";
RL Genetics 145:63-73(1997).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF CYS-128.
RX PubMed=9928935; DOI=10.1007/s004380050929;
RA Futai E., Maeda T., Sorimachi H., Kitamoto K., Ishiura S., Suzuki K.;
RT "The protease activity of a calpain-like cysteine protease in Saccharomyces
RT cerevisiae is required for alkaline adaptation and sporulation.";
RL Mol. Gen. Genet. 260:559-568(1999).
RN [5]
RP FUNCTION.
RX PubMed=11050096; DOI=10.1074/jbc.m008381200;
RA Lamb T.M., Xu W., Diamond A., Mitchell A.P.;
RT "Alkaline response genes of Saccharomyces cerevisiae and their relationship
RT to the RIM101 pathway.";
RL J. Biol. Chem. 276:1850-1856(2001).
RN [6]
RP INTERACTION WITH SNF7.
RX PubMed=11283351; DOI=10.1073/pnas.061034498;
RA Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT "A comprehensive two-hybrid analysis to explore the yeast protein
RT interactome.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Required for the proteolytic cleavage of the transcriptional
CC repressor RIM101 in response to alkaline ambient pH, which is necessary
CC for sporulation and invasive growth. Probably the protease that cleaves
CC RIM101. {ECO:0000269|PubMed:11050096, ECO:0000269|PubMed:9017390,
CC ECO:0000269|PubMed:9928935}.
CC -!- SUBUNIT: Interacts with SNF7, which may act together with RIM20 as a
CC scaffold to recruit RIM13 to its substrate RIM101.
CC {ECO:0000269|PubMed:11283351}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. PalB/RIM13 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z49705; CAA89790.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10049.1; -; Genomic_DNA.
DR PIR; S54512; S54512.
DR RefSeq; NP_013875.1; NM_001182657.1.
DR AlphaFoldDB; Q03792; -.
DR BioGRID; 35329; 394.
DR DIP; DIP-2809N; -.
DR IntAct; Q03792; 2.
DR MINT; Q03792; -.
DR STRING; 4932.YMR154C; -.
DR MEROPS; C02.030; -.
DR iPTMnet; Q03792; -.
DR MaxQB; Q03792; -.
DR PaxDb; Q03792; -.
DR PRIDE; Q03792; -.
DR EnsemblFungi; YMR154C_mRNA; YMR154C; YMR154C.
DR GeneID; 855186; -.
DR KEGG; sce:YMR154C; -.
DR SGD; S000004763; RIM13.
DR VEuPathDB; FungiDB:YMR154C; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_395483_0_0_1; -.
DR InParanoid; Q03792; -.
DR OMA; NISIDTY; -.
DR BioCyc; YEAST:G3O-32844-MON; -.
DR PRO; PR:Q03792; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03792; protein.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:SGD.
DR GO; GO:0016485; P:protein processing; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..727
FT /note="Calpain-like protease 1"
FT /id="PRO_0000207746"
FT DOMAIN 70..317
FT /note="Calpain catalytic"
FT ACT_SITE 128
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /evidence="ECO:0000250"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT MUTAGEN 128
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:9928935"
SQ SEQUENCE 727 AA; 83124 MW; 315F1A542FCC40F3 CRC64;
MNDWHEFNAA IKSIYCNAEG DSSSIINRLV GLAMKSEDST FIEAVLVLKE NVSKVDKQLR
FLWLTSTINS RFYPPIPISE ASPVSWNKTE YCAPGTEELQ RRYPGRAKLQ NEEDYSGGIE
QCRDVPDCSL VASLINLRSK NLNLPLIKQI SSTKYHVNLS FNGSNKRLVT VDISQIPTSV
DGKQLSLKSN DISDKIGELA LLLVSKGTYS TDGSNISIDT YRLSGFLPEI TQVNSYPFEK
LWKFHKSNLC LMGAGTGNRS NDMIKPLVEN HDYSIIDITY DSRLVKLRDP RNSALNVEIS
YEQYLKNFKQ LYLNWNQEKL FKRSQVLHFR YDTSRYNKFS IVADKPLFHL VNNSKVTETV
WLLLESHLQD EGSQENRSVS FLNEAPECII CPIEPPVECG GNHIGLQLVK LRLDAETERL
LYCYSTTNNN FSIHSFSVVK EICFQRLKDT KSLFAKVLFS FPYEIEGKAS FDTCNFFQNP
TFELEVHSEQ DYQVLMDAAC ISTSSHDLIN IQVYYFNDYE LIKPIMFDNH YQPGQGLKQD
VPILTNVKYM IVCSTYGPPA STEFELLASI RLSSSWRLIS GITLRSVNLI YGTYPYHCRN
RFHWKETSDK LKIQMTLPTK KYSTNKLFIR VVPVESSARL RMRCNIFEPE SALCVYECQE
YRTCPSGGIV IPDLEVSRTN IVVLMIERSV PISSCLPTEG QLDELELFVG SSQKIRIEKY
SDDVIPK
