NM111_YEAST
ID NM111_YEAST Reviewed; 997 AA.
AC P53920; B0KZR3; B0KZU0; B0KZX6; B0L003; B0L021; D6W160;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Pro-apoptotic serine protease NMA111;
DE EC=3.4.21.-;
DE AltName: Full=111 kDa nuclear mediator of apoptosis;
GN Name=NMA111; Synonyms=YNM3; OrderedLocusNames=YNL123W; ORFNames=N1897;
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], AND VARIANTS SER-162; LEU-241; GLY-331;
RP SER-343; ILE-386; GLY-457; PRO-530; ASN-580; THR-621 AND PHE-942.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270,
RC YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
RA Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
RA Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
RT "Linking genome and proteome by mass spectrometry: large-scale
RT identification of yeast proteins from two dimensional gels.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
RN [6]
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 [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).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF SER-235.
RX PubMed=14657274; DOI=10.1242/jcs.00848;
RA Fahrenkrog B., Sauder U., Aebi U.;
RT "The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease
RT that mediates yeast apoptosis.";
RL J. Cell Sci. 117:115-126(2004).
RN [9]
RP FUNCTION.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [10]
RP FUNCTION, MUTAGENESIS OF SER-235, AND INTERACTION WITH BIR1.
RX PubMed=16608876; DOI=10.1242/jcs.02902;
RA Walter D., Wissing S., Madeo F., Fahrenkrog B.;
RT "The inhibitor-of-apoptosis protein Bir1p protects against apoptosis in S.
RT cerevisiae and is a substrate for the yeast homologue of Omi/HtrA2.";
RL J. Cell Sci. 119:1843-1851(2006).
RN [11]
RP IDENTIFICATION BY 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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Nuclear serine protease which mediates apoptosis through
CC proteolysis of the apoptotic inhibitor BIR1.
CC {ECO:0000269|PubMed:14645503, ECO:0000269|PubMed:14657274,
CC ECO:0000269|PubMed:16608876}.
CC -!- SUBUNIT: Interacts with BIR1. {ECO:0000269|PubMed:16608876}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14657274}.
CC -!- MISCELLANEOUS: Present with 3150 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; EF125216; ABN58534.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58544.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58553.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58562.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58571.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58580.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58589.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58598.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58607.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58616.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58625.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58643.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93384.1; -; Genomic_DNA.
DR EMBL; Z71399; CAA96004.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10426.1; -; Genomic_DNA.
DR PIR; S63064; S63064.
DR RefSeq; NP_014276.1; NM_001182961.1.
DR AlphaFoldDB; P53920; -.
DR SMR; P53920; -.
DR BioGRID; 35704; 86.
DR STRING; 4932.YNL123W; -.
DR MEROPS; S01.434; -.
DR iPTMnet; P53920; -.
DR MaxQB; P53920; -.
DR PaxDb; P53920; -.
DR PRIDE; P53920; -.
DR EnsemblFungi; YNL123W_mRNA; YNL123W; YNL123W.
DR GeneID; 855600; -.
DR KEGG; sce:YNL123W; -.
DR SGD; S000005067; NMA111.
DR VEuPathDB; FungiDB:YNL123W; -.
DR eggNOG; KOG1421; Eukaryota.
DR HOGENOM; CLU_003212_0_0_1; -.
DR InParanoid; P53920; -.
DR OMA; CVFDNHE; -.
DR BioCyc; YEAST:G3O-33144-MON; -.
DR PRO; PR:P53920; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53920; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:SGD.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:SGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IMP:SGD.
DR GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IMP:SGD.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR025926; PDZ-like_dom.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF12812; PDZ_1; 2.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF50494; SSF50494; 2.
PE 1: Evidence at protein level;
KW Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW Serine protease.
FT CHAIN 1..997
FT /note="Pro-apoptotic serine protease NMA111"
FT /id="PRO_0000203429"
FT DOMAIN 300..378
FT /note="PDZ 1"
FT DOMAIN 779..854
FT /note="PDZ 2"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..273
FT /note="Serine protease"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT VARIANT 162
FT /note="N -> S (in strain: YJM269, YJM270 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 241
FT /note="V -> L (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 331
FT /note="E -> G (in strain: YJM326)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 343
FT /note="T -> S (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 386
FT /note="T -> I (in strain: YJM269, YJM270 and YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 457
FT /note="D -> G (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 530
FT /note="S -> P (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 580
FT /note="K -> N (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 621
FT /note="A -> T (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 942
FT /note="P -> F (in strain: YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT MUTAGEN 235
FT /note="S->C: Impairs BIR1 degradation and death-promoting
FT activity."
FT /evidence="ECO:0000269|PubMed:14657274,
FT ECO:0000269|PubMed:16608876"
SQ SEQUENCE 997 AA; 110881 MW; A26005C1DDDB932C CRC64;
MTISLSNIKK RDHSKISDGT SGESSLVKRK QLESATGDQE EEYTDHEIII EPLHFANNNN
TVLTDSENYL RWQNTISNVV KSVVSIHFSQ VAPFDCDSAL VSEATGFVVD AKLGIILTNR
HVVGPGPFVG YVVFDNHEEC DVIPIYRDPV HDFGFLKFDP KNIKYSKIKA LTLKPSLAKV
GSEIRVVGND AGEKLSILAG FISRIDRNAP EYGELTYNDF NTEYIQAAAS ASGGSSGSPV
VNIDGYAVAL QAGGSTEAST DFFLPLDRIL RALICIQTNK PITRGTIQVQ WLLKPYDECR
RLGLTSERES EARAKFPENI GLLVAETVLR EGPGYDKIKE GDTLISINGE TISSFMQVDK
IQDENVGKEI QLVIQRGGVE CTVTCTVGDL HAITPHRYVE VCGATFHELS YQMARFYALP
VRGVFLSSAS GSFNFDSKER VGWIVDSIDN KETPDLDTFI EIMKTIPDRK RVTVRYHHLT
DQHSPLVTSI YIDRHWCNEF RVYTRNDTTG IWDYKNVADP LPADALKPRS AKIIPIPVNN
EKVAKLSSSL CTVATMAAVP LDSLSADILK TSGLIIDAEK GYVLVSRRVV PHDCLDTFVT
IADSLVVPAT VEFLHPTHNF AIVKYDPELV KAPLITPKLS TTRMKRGDKL QFIGFTQNDR
IVTSETTVTD ISSVSIPSNL IPRYRATNLE AISIDCNVST RCNSGILTDN DGTVRGLWLP
FLGERLENKE KVYLMGLDIM DCREVIDILK NGGKPRVSIV DAGFGSISVL QARIRGVPEE
WIMRMEHESN NRLQFITVSR VSYTEDKIHL ETGDVILSVN GKLVTEMNDL NGVVSSADGI
LPSAMLDFKV VRDGNIVDLK IKTVEVQETD RFVIFAGSIL QKPHHAVLQA MVDVPKGVYC
TFRGESSPAL QYGISATNFI THVNEIETPD LDTFLKVVKT IPDNSYCKMR LMTFDNVPFA
ISLKTNYHYF PTAELKRDNI THKWIEKEFT GNSQSEK
