Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q08601 (MCA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Metacaspase-1

EC=3.4.22.-
Gene names
Name:MCA1
Synonyms:YCA1
Ordered Locus Names:YOR197W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20

Subcellular location

Cytoplasm. Nucleus Ref.6.

Domain

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain. It targets the protein to insoluble protein aggregates. Ref.20

Miscellaneous

Present with 1400 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the peptidase C14B family.

Caution

Ref.18 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.

Sequence caution

The sequence AAT92851.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA99410.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – ? PotentialPRO_0000268683
Chain? – 432Metacaspase-1PRO_0000268684

Regions

Region29 – 131103Prion domain (PrD)

Sites

Active site2201 By similarity
Active site2761

Experimental info

Mutagenesis2761C → A: Blocks the processing and reduces caspase activity. Ref.4

Secondary structure

.............................................. 432
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08601 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 547D186E3EB481B7

FASTA43247,982
        10         20         30         40         50         60 
MYPGSGRYTY NNAGGNNGYQ RPMAPPPNQQ YGQQYGQQYE QQYGQQYGQQ NDQQFSQQYA 

        70         80         90        100        110        120 
PPPGPPPMAY NRPVYPPPQF QQEQAKAQLS NGYNNPNVNA SNMYGPPQNM SLPPPQTQTI 

       130        140        150        160        170        180 
QGTDQPYQYS QCTGRRKALI IGINYIGSKN QLRGCINDAH NIFNFLTNGY GYSSDDIVIL 

       190        200        210        220        230        240 
TDDQNDLVRV PTRANMIRAM QWLVKDAQPN DSLFLHYSGH GGQTEDLDGD EEDGMDDVIY 

       250        260        270        280        290        300 
PVDFETQGPI IDDEMHDIMV KPLQQGVRLT ALFDSCHSGT VLDLPYTYST KGIIKEPNIW 

       310        320        330        340        350        360 
KDVGQDGLQA AISYATGNRA ALIGSLGSIF KTVKGGMGNN VDRERVRQIK FSAADVVMLS 

       370        380        390        400        410        420 
GSKDNQTSAD AVEDGQNTGA MSHAFIKVMT LQPQQSYLSL LQNMRKELAG KYSQKPQLSS 

       430 
SHPIDVNLQF IM 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
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. expand/collapse author list , 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.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"A caspase-related protease regulates apoptosis in yeast."
Madeo F., Herker E., Maldener C., Wissing S., Laechelt S., Herlan M., Fehr M., Lauber K., Sigrist S.J., Wesselborg S., Froehlich K.-U.
Mol. Cell 9:911-917(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-276, PROTEOLYTIC PROCESSING.
[5]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[6]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Finding functional features in Saccharomyces genomes by phylogenetic footprinting."
Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.
Science 301:71-76(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[9]"Involvement of the yeast metacaspase Yca1 in ubp10Delta-programmed cell death."
Bettiga M., Calzari L., Orlandi I., Alberghina L., Vai M.
FEMS Yeast Res. 5:141-147(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"An AIF orthologue regulates apoptosis in yeast."
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.
J. Cell Biol. 166:969-974(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Chronological aging leads to apoptosis in yeast."
Herker E., Jungwirth H., Lehmann K.A., Maldener C., Froehlich K.-U., Wissing S., Buettner S., Fehr M., Sigrist S.J., Madeo F.
J. Cell Biol. 164:501-507(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Yeast lacking the SRO7/SOP1-encoded tumor suppressor homologue show increased susceptibility to apoptosis-like cell death on exposure to NaCl stress."
Wadskog I., Maldener C., Proksch A., Madeo F., Adler L.
Mol. Biol. Cell 15:1436-1444(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Yeast caspase 1 links messenger RNA stability to apoptosis in yeast."
Mazzoni C., Herker E., Palermo V., Jungwirth H., Eisenberg T., Madeo F., Falcone C.
EMBO Rep. 6:1076-1081(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Viral killer toxins induce caspase-mediated apoptosis in yeast."
Reiter J., Herker E., Madeo F., Schmitt M.J.
J. Cell Biol. 168:353-358(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Physiological regulation of yeast cell death in multicellular colonies is triggered by ammonia."
Vachova L., Palkova Z.
J. Cell Biol. 169:711-717(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Apoptosis in budding yeast caused by defects in initiation of DNA replication."
Weinberger M., Ramachandran L., Feng L., Sharma K., Sun X., Marchetti M., Huberman J.A., Burhans W.C.
J. Cell Sci. 118:3543-3553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Knockout of caspase-like gene, YCA1, abrogates apoptosis and elevates oxidized proteins in Saccharomyces cerevisiae."
Khan M.A., Chock P.B., Stadtman E.R.
Proc. Natl. Acad. Sci. U.S.A. 102:17326-17331(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen."
Nemecek J., Nakayashiki T., Wickner R.B.
Proc. Natl. Acad. Sci. U.S.A. 106:1892-1896(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
[19]Erratum
Nemecek J., Nakayashiki T., Wickner R.B.
Proc. Natl. Acad. Sci. U.S.A. 108:10022-10022(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
[20]"Metacaspase Yca1 is required for clearance of insoluble protein aggregates."
Lee R.E., Brunette S., Puente L.G., Megeney L.A.
Proc. Natl. Acad. Sci. U.S.A. 107:13348-13353(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN PRION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z75105 Genomic DNA. Translation: CAA99410.1. Different initiation.
AY692832 Genomic DNA. Translation: AAT92851.1. Different initiation.
BK006948 Genomic DNA. Translation: DAA10972.1.
PIRS67089.
RefSeqNP_014840.4. NM_001183616.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4F6OX-ray1.68A83-432[»]
4F6PX-ray1.62A83-432[»]
ProteinModelPortalQ08601.
SMRQ08601. Positions 90-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34595. 56 interactions.
DIPDIP-2802N.
IntActQ08601. 7 interactions.
MINTMINT-533648.
STRING4932.YOR197W.

Protein family/group databases

MEROPSC14.035.

Proteomic databases

MaxQBQ08601.
PaxDbQ08601.
PeptideAtlasQ08601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR197W; YOR197W; YOR197W.
GeneID854372.
KEGGsce:YOR197W.

Organism-specific databases

CYGDYOR197w.
SGDS000005723. MCA1.

Phylogenomic databases

eggNOGNOG68179.
HOGENOMHOG000240109.
OMAYERTKRT.
OrthoDBEOG78PVMS.

Enzyme and pathway databases

BioCycYEAST:G3O-33705-MONOMER.

Gene expression databases

GenevestigatorQ08601.

Family and domain databases

Gene3D3.40.50.1460. 1 hit.
InterProIPR029030. Caspase-like_dom.
IPR011600. Pept_C14_caspase.
[Graphical view]
PfamPF00656. Peptidase_C14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio976502.

Entry information

Entry nameMCA1_YEAST
AccessionPrimary (citable) accession number: Q08601
Secondary accession number(s): D6W2Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references