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Metacaspase-1 (EC 3.4.22.-)

 MCA1_YEAST              Reviewed;         432 AA.
Q08601; D6W2Q6;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
12-SEP-2018, entry version 136.
RecName: Full=Metacaspase-1;
EC=3.4.22.-;
Flags: Precursor;
Name=MCA1; Synonyms=YCA1; OrderedLocusNames=YOR197W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
FUNCTION, MUTAGENESIS OF CYS-276, AND PROTEOLYTIC PROCESSING.
PubMed=11983181; DOI=10.1016/S1097-2765(02)00501-4;
Madeo F., Herker E., Maldener C., Wissing S., Laechelt S., Herlan M.,
Fehr M., Lauber K., Sigrist S.J., Wesselborg S., Froehlich K.-U.;
"A caspase-related protease regulates apoptosis in yeast.";
Mol. Cell 9:911-917(2002).
[5]
IDENTIFICATION OF PROBABLE INITIATION SITE.
PubMed=12748633; DOI=10.1038/nature01644;
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and
regulatory elements.";
Nature 423:241-254(2003).
[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]
IDENTIFICATION OF PROBABLE INITIATION SITE.
PubMed=12775844; DOI=10.1126/science.1084337;
Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B.,
Majors J., Waterston R., Cohen B.A., Johnston M.;
"Finding functional features in Saccharomyces genomes by phylogenetic
footprinting.";
Science 301:71-76(2003).
[9]
FUNCTION.
PubMed=15489197; DOI=10.1016/j.femsyr.2004.07.005;
Bettiga M., Calzari L., Orlandi I., Alberghina L., Vai M.;
"Involvement of the yeast metacaspase Yca1 in ubp10Delta-programmed
cell death.";
FEMS Yeast Res. 5:141-147(2004).
[10]
FUNCTION.
PubMed=15381687; DOI=10.1083/jcb.200404138;
Wissing S., Ludovico P., Herker E., Buettner S., Engelhardt S.M.,
Decker T., Link A., Proksch A., Rodrigues F., Corte-Real M.,
Froehlich K.-U., Manns J., Cande C., Sigrist S.J., Kroemer G.,
Madeo F.;
"An AIF orthologue regulates apoptosis in yeast.";
J. Cell Biol. 166:969-974(2004).
[11]
FUNCTION.
PubMed=14970189; DOI=10.1083/jcb.200310014;
Herker E., Jungwirth H., Lehmann K.A., Maldener C., Froehlich K.-U.,
Wissing S., Buettner S., Fehr M., Sigrist S.J., Madeo F.;
"Chronological aging leads to apoptosis in yeast.";
J. Cell Biol. 164:501-507(2004).
[12]
FUNCTION.
PubMed=14718573; DOI=10.1091/mbc.E03-02-0114;
Wadskog I., Maldener C., Proksch A., Madeo F., Adler L.;
"Yeast lacking the SRO7/SOP1-encoded tumor suppressor homologue show
increased susceptibility to apoptosis-like cell death on exposure to
NaCl stress.";
Mol. Biol. Cell 15:1436-1444(2004).
[13]
FUNCTION.
PubMed=16170310; DOI=10.1038/sj.embor.7400514;
Mazzoni C., Herker E., Palermo V., Jungwirth H., Eisenberg T.,
Madeo F., Falcone C.;
"Yeast caspase 1 links messenger RNA stability to apoptosis in
yeast.";
EMBO Rep. 6:1076-1081(2005).
[14]
FUNCTION.
PubMed=15668299; DOI=10.1083/jcb.200408071;
Reiter J., Herker E., Madeo F., Schmitt M.J.;
"Viral killer toxins induce caspase-mediated apoptosis in yeast.";
J. Cell Biol. 168:353-358(2005).
[15]
FUNCTION.
PubMed=15939758; DOI=10.1083/jcb.200410064;
Vachova L., Palkova Z.;
"Physiological regulation of yeast cell death in multicellular
colonies is triggered by ammonia.";
J. Cell Biol. 169:711-717(2005).
[16]
FUNCTION.
PubMed=16079294; DOI=10.1242/jcs.02477;
Weinberger M., Ramachandran L., Feng L., Sharma K., Sun X.,
Marchetti M., Huberman J.A., Burhans W.C.;
"Apoptosis in budding yeast caused by defects in initiation of DNA
replication.";
J. Cell Sci. 118:3543-3553(2005).
[17]
FUNCTION.
PubMed=16301538; DOI=10.1073/pnas.0508120102;
Khan M.A., Chock P.B., Stadtman E.R.;
"Knockout of caspase-like gene, YCA1, abrogates apoptosis and elevates
oxidized proteins in Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 102:17326-17331(2005).
[18]
RETRACTED PAPER.
PubMed=19174511; DOI=10.1073/pnas.0812470106;
Nemecek J., Nakayashiki T., Wickner R.B.;
"A prion of yeast metacaspase homolog (Mca1p) detected by a genetic
screen.";
Proc. Natl. Acad. Sci. U.S.A. 106:1892-1896(2009).
[19]
RETRACTION NOTICE OF PUBMED:19174511.
PubMed=21628591; DOI=10.1073/pnas.1107490108;
Nemecek J., Nakayashiki T., Wickner R.B.;
Proc. Natl. Acad. Sci. U.S.A. 108:10022-10022(2011).
[20]
FUNCTION, AND DOMAIN PRION.
PubMed=20624963; DOI=10.1073/pnas.1006610107;
Lee R.E., Brunette S., Puente L.G., Megeney L.A.;
"Metacaspase Yca1 is required for clearance of insoluble protein
aggregates.";
Proc. Natl. Acad. Sci. U.S.A. 107:13348-13353(2010).
-!- FUNCTION: Mediates cell death (apoptosis) triggered by oxygen
stress, salt stress or chronological aging. Regulated cell death
can prevent a release of toxic cellular components, thus avoiding
necrotic collapse of the colony, and can also provide nutrients
for healthy cells. Therefore, regulated cell death in yeast
colonies can be as important for their development as are
apoptosis and related processes that occur within metazoa.
Promotes the removal of insoluble protein aggregates during normal
growth. {ECO:0000269|PubMed:11983181, ECO:0000269|PubMed:14718573,
ECO:0000269|PubMed:14970189, ECO:0000269|PubMed:15381687,
ECO:0000269|PubMed:15489197, ECO:0000269|PubMed:15668299,
ECO:0000269|PubMed:15939758, ECO:0000269|PubMed:16079294,
ECO:0000269|PubMed:16170310, ECO:0000269|PubMed:16301538,
ECO:0000269|PubMed:20624963}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain. It
targets the protein to insoluble protein aggregates.
{ECO:0000269|PubMed:20624963}.
-!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the peptidase C14B family. {ECO:0000305}.
-!- CAUTION: PubMed:19174511 reported that MCA1 may have a prion form,
dubbed [MCA]. However, the same authors have later not been able
to reproduce these results and retracted the paper. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAT92851.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA99410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z75105; CAA99410.1; ALT_INIT; Genomic_DNA.
EMBL; AY692832; AAT92851.1; ALT_INIT; Genomic_DNA.
EMBL; BK006948; DAA10972.1; -; Genomic_DNA.
PIR; S67089; S67089.
RefSeq; NP_014840.4; NM_001183616.3.
PDB; 4F6O; X-ray; 1.68 A; A=83-432.
PDB; 4F6P; X-ray; 1.62 A; A=83-432.
PDBsum; 4F6O; -.
PDBsum; 4F6P; -.
ProteinModelPortal; Q08601; -.
SMR; Q08601; -.
BioGrid; 34595; 131.
DIP; DIP-2802N; -.
IntAct; Q08601; 27.
MINT; Q08601; -.
STRING; 4932.YOR197W; -.
MEROPS; C14.035; -.
MaxQB; Q08601; -.
PaxDb; Q08601; -.
PRIDE; Q08601; -.
EnsemblFungi; YOR197W; YOR197W; YOR197W.
GeneID; 854372; -.
KEGG; sce:YOR197W; -.
EuPathDB; FungiDB:YOR197W; -.
SGD; S000005723; MCA1.
HOGENOM; HOG000240109; -.
InParanoid; Q08601; -.
KO; K22684; -.
OMA; FFQYSQC; -.
OrthoDB; EOG092C4ES8; -.
BioCyc; YEAST:G3O-33705-MONOMER; -.
PRO; PR:Q08601; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:SGD.
GO; GO:0006915; P:apoptotic process; IDA:SGD.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:SGD.
InterPro; IPR029030; Caspase-like_dom_sf.
SUPFAM; SSF52129; SSF52129; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Nucleus; Protease; Reference proteome; Thiol protease; Zymogen.
PROPEP 1 ? {ECO:0000255}.
/FTId=PRO_0000268683.
CHAIN ? 432 Metacaspase-1.
/FTId=PRO_0000268684.
REGION 29 131 Prion domain (PrD).
ACT_SITE 220 220 {ECO:0000250}.
ACT_SITE 276 276
MUTAGEN 276 276 C->A: Blocks the processing and reduces
caspase activity.
{ECO:0000269|PubMed:11983181}.
TURN 92 94 {ECO:0000244|PDB:4F6O}.
STRAND 102 104 {ECO:0000244|PDB:4F6O}.
STRAND 136 142 {ECO:0000244|PDB:4F6P}.
HELIX 155 167 {ECO:0000244|PDB:4F6P}.
HELIX 174 176 {ECO:0000244|PDB:4F6P}.
STRAND 177 181 {ECO:0000244|PDB:4F6P}.
HELIX 187 189 {ECO:0000244|PDB:4F6P}.
HELIX 193 204 {ECO:0000244|PDB:4F6P}.
STRAND 212 219 {ECO:0000244|PDB:4F6P}.
STRAND 221 223 {ECO:0000244|PDB:4F6P}.
STRAND 237 239 {ECO:0000244|PDB:4F6P}.
HELIX 244 247 {ECO:0000244|PDB:4F6P}.
HELIX 252 259 {ECO:0000244|PDB:4F6P}.
TURN 260 262 {ECO:0000244|PDB:4F6P}.
STRAND 268 273 {ECO:0000244|PDB:4F6P}.
STRAND 275 277 {ECO:0000244|PDB:4F6P}.
TURN 279 282 {ECO:0000244|PDB:4F6P}.
STRAND 285 289 {ECO:0000244|PDB:4F6P}.
STRAND 292 295 {ECO:0000244|PDB:4F6P}.
STRAND 354 362 {ECO:0000244|PDB:4F6P}.
HELIX 380 391 {ECO:0000244|PDB:4F6P}.
HELIX 397 408 {ECO:0000244|PDB:4F6P}.
TURN 409 411 {ECO:0000244|PDB:4F6P}.
STRAND 415 422 {ECO:0000244|PDB:4F6P}.
SEQUENCE 432 AA; 47982 MW; 547D186E3EB481B7 CRC64;
MYPGSGRYTY NNAGGNNGYQ RPMAPPPNQQ YGQQYGQQYE QQYGQQYGQQ NDQQFSQQYA
PPPGPPPMAY NRPVYPPPQF QQEQAKAQLS NGYNNPNVNA SNMYGPPQNM SLPPPQTQTI
QGTDQPYQYS QCTGRRKALI IGINYIGSKN QLRGCINDAH NIFNFLTNGY GYSSDDIVIL
TDDQNDLVRV PTRANMIRAM QWLVKDAQPN DSLFLHYSGH GGQTEDLDGD EEDGMDDVIY
PVDFETQGPI IDDEMHDIMV KPLQQGVRLT ALFDSCHSGT VLDLPYTYST KGIIKEPNIW
KDVGQDGLQA AISYATGNRA ALIGSLGSIF KTVKGGMGNN VDRERVRQIK FSAADVVMLS
GSKDNQTSAD AVEDGQNTGA MSHAFIKVMT LQPQQSYLSL LQNMRKELAG KYSQKPQLSS
SHPIDVNLQF IM


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