CYM1_YEAST
ID CYM1_YEAST Reviewed; 989 AA.
AC P32898; D6VT59; Q04068;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mitochondrial presequence protease;
DE EC=3.4.24.-;
DE AltName: Full=Cytosolic metalloprotease 1;
DE AltName: Full=Metalloprotease of 112 kDa;
GN Name=CYM1; Synonyms=MOP112; OrderedLocusNames=YDR430C; ORFNames=D9461.18;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-166.
RX PubMed=8224861; DOI=10.1016/0378-1119(93)90193-7;
RA Ellis E.M., Reid G.A.;
RT "The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding
RT protein involved in mitochondrial protein targeting.";
RL Gene 132:175-183(1993).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15606766; DOI=10.1111/j.1432-1033.2004.04443.x;
RA Joenson L., Rehfeld J.F., Johnsen A.H.;
RT "Enhanced peptide secretion by gene disruption of CYM1, a novel protease in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 271:4788-4797(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-84; GLU-87 AND
RP HIS-88.
RX PubMed=15772085; DOI=10.1074/jbc.m500398200;
RA Kambacheld M., Augustin S., Tatsuta T., Muller S., Langer T.;
RT "Role of the novel metallopeptidase Mop112 and saccharolysin for the
RT complete degradation of proteins residing in different subcompartments of
RT mitochondria.";
RL J. Biol. Chem. 280:20132-20139(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: ATP-independent protease that degrades mitochondrial transit
CC peptides after their cleavage both in intermembrane space and in
CC matrix. Also degrades other unstructured peptides (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15772085}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15606766,
CC ECO:0000269|PubMed:15772085}. Note=May also be present in the
CC mitochondrial matrix.
CC -!- MISCELLANEOUS: Present with 6140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64877.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X70951; CAA50290.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64877.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006938; DAA12269.1; -; Genomic_DNA.
DR PIR; S69711; S69711.
DR RefSeq; NP_010718.1; NM_001180738.1.
DR AlphaFoldDB; P32898; -.
DR SMR; P32898; -.
DR BioGRID; 32488; 89.
DR DIP; DIP-6735N; -.
DR IntAct; P32898; 7.
DR STRING; 4932.YDR430C; -.
DR MEROPS; M16.013; -.
DR iPTMnet; P32898; -.
DR MaxQB; P32898; -.
DR PaxDb; P32898; -.
DR PRIDE; P32898; -.
DR EnsemblFungi; YDR430C_mRNA; YDR430C; YDR430C.
DR GeneID; 852041; -.
DR KEGG; sce:YDR430C; -.
DR SGD; S000002838; CYM1.
DR VEuPathDB; FungiDB:YDR430C; -.
DR eggNOG; KOG2019; Eukaryota.
DR GeneTree; ENSGT00390000018381; -.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; P32898; -.
DR OMA; MTYPDKT; -.
DR BioCyc; YEAST:G3O-29969-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR PRO; PR:P32898; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32898; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:SGD.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:SGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:SGD.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Phosphoprotein;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..989
FT /note="Mitochondrial presequence protease"
FT /id="PRO_0000178012"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 84
FT /note="H->Y: Loss of function."
FT /evidence="ECO:0000269|PubMed:15772085"
FT MUTAGEN 87
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:15772085"
FT MUTAGEN 88
FT /note="H->Y: Loss of function."
FT /evidence="ECO:0000269|PubMed:15772085"
SQ SEQUENCE 989 AA; 112180 MW; 6CAD2EE5A6080D9C CRC64;
MLRFQRFASS YAQAQAVRKY PVGGIFHGYE VRRILPVPEL RLTAVDLVHS QTGAEHLHID
RDDKNNVFSI AFKTNPPDST GVPHILEHTT LCGSVKYPVR DPFFKMLNKS LANFMNAMTG
PDYTFFPFST TNPQDFANLR GVYLDSTLNP LLKQEDFDQE GWRLEHKNIT DPESNIVFKG
VVYNEMKGQI SNANYYFWSK FQQSIYPSLN NSGGDPMKIT DLRYGDLLDF HHKNYHPSNA
KTFTYGNLPL VDTLKQLNEQ FSGYGKRARK DKLLMPIDLK KDIDVKLLGQ IDTMLPPEKQ
TKASMTWICG APQDTYDTFL LKVLGNLLMD GHSSVMYQKL IESGIGLEFS VNSGVEPTTA
VNLLTVGIQG VSDIEIFKDT VNNIFQNLLE TEHPFDRKRI DAIIEQLELS KKDQKADFGL
QLLYSILPGW TNKIDPFESL LFEDVLQRFR GDLETKGDTL FQDLIRKYIV HKPCFTFSIQ
GSEEFSKSLD DEEQTRLREK ITALDEQDKK NIFKRGILLQ EKQNEKEDLS CLPTLQIKDI
PRAGDKYSIE QKNNTMSRIT DTNGITYVRG KRLLNDIIPF ELFPYLPLFA ESLTNLGTTT
ESFSEIEDQI KLHTGGISTH VEVTSDPNTT EPRLIFGFDG WSLNSKTDHI FEFWSKILLE
TDFHKNSDKL KVLIRLLASS NTSSVADAGH AFARGYSAAH YRSSGAINET LNGIEQLQFI
NRLHSLLDNE ETFQREVVDK LTELQKYIVD TNNMNFFITS DSDVQAKTVE SQISKFMERL
PHGSCLPNGP KTSDYPLIGS KCKHTLIKFP FQVHYTSQAL LGVPYTHKDG SALQVMSNML
TFKHLHREVR EKGGAYGGGA SYSALAGIFS FYSYRDPQPL KSLETFKNSG RYILNDAKWG
VTDLDEAKLT IFQQVDAPKS PKGEGVTYFM SGVTDDMKQA RREQLLDVSL LDVHRVAEKY
LLNKEGVSTV IGPGIEGKTV SPNWEVKEL
