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Pro-apoptotic serine protease NMA111 (EC 3.4.21.-) (111 kDa nuclear mediator of apoptosis)

 NM111_YEAST             Reviewed;         997 AA.
P53920; B0KZR3; B0KZU0; B0KZX6; B0L003; B0L021; D6W160;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 146.
RecName: Full=Pro-apoptotic serine protease NMA111;
EC=3.4.21.-;
AltName: Full=111 kDa nuclear mediator of apoptosis;
Name=NMA111; Synonyms=YNM3; OrderedLocusNames=YNL123W; ORFNames=N1897;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-162; LEU-241;
GLY-331; SER-343; ILE-386; GLY-457; PRO-530; ASN-580; THR-621 AND
PHE-942.
STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269,
YJM 270, YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
PubMed=18780730; DOI=10.1534/genetics.108.092932;
Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
Steinmetz L.M.;
"Sequential elimination of major-effect contributors identifies
additional quantitative trait loci conditioning high-temperature
growth in yeast.";
Genetics 180:1661-1670(2008).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9090055;
DOI=10.1002/(SICI)1097-0061(19970315)13:3<261::AID-YEA64>3.0.CO;2-L;
de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
Pallavicini A., Lanfranchi G., Valle G.;
"The DNA sequence of cosmid 14-13b from chromosome XIV of
Saccharomyces cerevisiae reveals an unusually high number of
overlapping open reading frames.";
Yeast 13:261-266(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=8962070; DOI=10.1073/pnas.93.25.14440;
Shevchenko A., Jensen O.N., Podtelejnikov A.V., Sagliocco F., Wilm M.,
Vorm O., Mortensen P., Shevchenko A., Boucherie H., Mann M.;
"Linking genome and proteome by mass spectrometry: large-scale
identification of yeast proteins from two dimensional gels.";
Proc. Natl. Acad. Sci. U.S.A. 93:14440-14445(1996).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF SER-235.
PubMed=14657274; DOI=10.1242/jcs.00848;
Fahrenkrog B., Sauder U., Aebi U.;
"The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine
protease that mediates yeast apoptosis.";
J. Cell Sci. 117:115-126(2004).
[9]
FUNCTION.
PubMed=14645503; DOI=10.1074/mcp.M300082-MCP200;
Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
"Synergistic computational and experimental proteomics approaches for
more accurate detection of active serine hydrolases in yeast.";
Mol. Cell. Proteomics 3:209-225(2004).
[10]
FUNCTION, MUTAGENESIS OF SER-235, AND INTERACTION WITH BIR1.
PubMed=16608876; DOI=10.1242/jcs.02902;
Walter D., Wissing S., Madeo F., Fahrenkrog B.;
"The inhibitor-of-apoptosis protein Bir1p protects against apoptosis
in S. cerevisiae and is a substrate for the yeast homologue of
Omi/HtrA2.";
J. Cell Sci. 119:1843-1851(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Nuclear serine protease which mediates apoptosis through
proteolysis of the apoptotic inhibitor BIR1.
{ECO:0000269|PubMed:14645503, ECO:0000269|PubMed:14657274,
ECO:0000269|PubMed:16608876}.
-!- SUBUNIT: Interacts with BIR1. {ECO:0000269|PubMed:16608876}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14657274}.
-!- MISCELLANEOUS: Present with 3150 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; EF125216; ABN58534.1; -; Genomic_DNA.
EMBL; EF125217; ABN58544.1; -; Genomic_DNA.
EMBL; EF125218; ABN58553.1; -; Genomic_DNA.
EMBL; EF125219; ABN58562.1; -; Genomic_DNA.
EMBL; EF125220; ABN58571.1; -; Genomic_DNA.
EMBL; EF125221; ABN58580.1; -; Genomic_DNA.
EMBL; EF125222; ABN58589.1; -; Genomic_DNA.
EMBL; EF125223; ABN58598.1; -; Genomic_DNA.
EMBL; EF125224; ABN58607.1; -; Genomic_DNA.
EMBL; EF125225; ABN58616.1; -; Genomic_DNA.
EMBL; EF125226; ABN58625.1; -; Genomic_DNA.
EMBL; EF125228; ABN58643.1; -; Genomic_DNA.
EMBL; Z69382; CAA93384.1; -; Genomic_DNA.
EMBL; Z71399; CAA96004.1; -; Genomic_DNA.
EMBL; BK006947; DAA10426.1; -; Genomic_DNA.
PIR; S63064; S63064.
RefSeq; NP_014276.1; NM_001182961.1.
ProteinModelPortal; P53920; -.
SMR; P53920; -.
BioGrid; 35704; 57.
IntAct; P53920; 7.
MINT; MINT-4499860; -.
STRING; 4932.YNL123W; -.
MEROPS; S01.434; -.
iPTMnet; P53920; -.
MaxQB; P53920; -.
PRIDE; P53920; -.
EnsemblFungi; YNL123W; YNL123W; YNL123W.
GeneID; 855600; -.
KEGG; sce:YNL123W; -.
EuPathDB; FungiDB:YNL123W; -.
SGD; S000005067; NMA111.
InParanoid; P53920; -.
OMA; PYDLCDI; -.
OrthoDB; EOG092C0BB0; -.
BioCyc; YEAST:G3O-33144-MONOMER; -.
PRO; PR:P53920; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:SGD.
GO; GO:0006915; P:apoptotic process; IMP:SGD.
GO; GO:0044255; P:cellular lipid metabolic process; IMP:SGD.
GO; GO:0034605; P:cellular response to heat; IMP:SGD.
GO; GO:0030163; P:protein catabolic process; IMP:SGD.
InterPro; IPR001478; PDZ.
InterPro; IPR025926; PDZ-like_dom.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001940; Peptidase_S1C.
Pfam; PF00595; PDZ; 1.
Pfam; PF12812; PDZ_1; 2.
PRINTS; PR00834; PROTEASES2C.
SMART; SM00228; PDZ; 2.
SUPFAM; SSF50156; SSF50156; 3.
SUPFAM; SSF50494; SSF50494; 2.
1: Evidence at protein level;
Apoptosis; Complete proteome; Hydrolase; Nucleus; Protease;
Reference proteome; Repeat; Serine protease.
CHAIN 1 997 Pro-apoptotic serine protease NMA111.
/FTId=PRO_0000203429.
DOMAIN 300 378 PDZ 1.
DOMAIN 779 854 PDZ 2.
REGION 83 273 Serine protease.
ACT_SITE 121 121 Charge relay system. {ECO:0000255}.
ACT_SITE 152 152 Charge relay system. {ECO:0000255}.
ACT_SITE 235 235 Charge relay system. {ECO:0000255}.
VARIANT 162 162 N -> S (in strain: YJM269, YJM270 and
YJM1129). {ECO:0000269|PubMed:18780730}.
VARIANT 241 241 V -> L (in strain: YJM269 and YJM270).
{ECO:0000269|PubMed:18780730}.
VARIANT 331 331 E -> G (in strain: YJM326).
{ECO:0000269|PubMed:18780730}.
VARIANT 343 343 T -> S (in strain: YJM269 and YJM270).
{ECO:0000269|PubMed:18780730}.
VARIANT 386 386 T -> I (in strain: YJM269, YJM270 and
YJM1129). {ECO:0000269|PubMed:18780730}.
VARIANT 457 457 D -> G (in strain: YJM269 and YJM270).
{ECO:0000269|PubMed:18780730}.
VARIANT 530 530 S -> P (in strain: YJM627).
{ECO:0000269|PubMed:18780730}.
VARIANT 580 580 K -> N (in strain: YJM627).
{ECO:0000269|PubMed:18780730}.
VARIANT 621 621 A -> T (in strain: YJM269 and YJM270).
{ECO:0000269|PubMed:18780730}.
VARIANT 942 942 P -> F (in strain: YJM627).
{ECO:0000269|PubMed:18780730}.
MUTAGEN 235 235 S->C: Impairs BIR1 degradation and death-
promoting activity.
{ECO:0000269|PubMed:14657274,
ECO:0000269|PubMed:16608876}.
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


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