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Q08601

- MCA1_YEAST

UniProt

Q08601 - MCA1_YEAST

Protein

Metacaspase-1

Gene

MCA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    Functioni

    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.11 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei220 – 2201By similarity
    Active sitei276 – 2761

    GO - Molecular functioni

    1. calcium-dependent cysteine-type endopeptidase activity Source: SGD

    GO - Biological processi

    1. apoptotic process Source: SGD
    2. misfolded or incompletely synthesized protein catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33705-MONOMER.

    Protein family/group databases

    MEROPSiC14.035.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Metacaspase-1 (EC:3.4.22.-)
    Gene namesi
    Name:MCA1
    Synonyms:YCA1
    Ordered Locus Names:YOR197W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR197w.
    SGDiS000005723. MCA1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi276 – 2761C → A: Blocks the processing and reduces caspase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 432Metacaspase-1PRO_0000268684
    Propeptidei1 – ?Sequence AnalysisPRO_0000268683

    Keywords - PTMi

    Zymogen

    Proteomic databases

    MaxQBiQ08601.
    PaxDbiQ08601.
    PeptideAtlasiQ08601.

    Expressioni

    Gene expression databases

    GenevestigatoriQ08601.

    Interactioni

    Protein-protein interaction databases

    BioGridi34595. 56 interactions.
    DIPiDIP-2802N.
    IntActiQ08601. 7 interactions.
    MINTiMINT-533648.
    STRINGi4932.YOR197W.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni92 – 943
    Beta strandi102 – 1043
    Beta strandi136 – 1427
    Helixi155 – 16713
    Helixi174 – 1763
    Beta strandi177 – 1815
    Helixi187 – 1893
    Helixi193 – 20412
    Beta strandi212 – 2198
    Beta strandi221 – 2233
    Beta strandi237 – 2393
    Helixi244 – 2474
    Helixi252 – 2598
    Turni260 – 2623
    Beta strandi268 – 2736
    Beta strandi275 – 2773
    Turni279 – 2824
    Beta strandi285 – 2895
    Beta strandi292 – 2954
    Beta strandi354 – 3629
    Helixi380 – 39112
    Helixi397 – 40812
    Turni409 – 4113
    Beta strandi415 – 4228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F6OX-ray1.68A83-432[»]
    4F6PX-ray1.62A83-432[»]
    ProteinModelPortaliQ08601.
    SMRiQ08601. Positions 90-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni29 – 131103Prion domain (PrD)Add
    BLAST

    Domaini

    The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain. It targets the protein to insoluble protein aggregates.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C14B family.Curated

    Phylogenomic databases

    eggNOGiNOG68179.
    HOGENOMiHOG000240109.
    OMAiYERTKRT.
    OrthoDBiEOG78PVMS.

    Family and domain databases

    Gene3Di3.40.50.1460. 1 hit.
    InterProiIPR029030. Caspase-like_dom.
    IPR011600. Pept_C14_caspase.
    [Graphical view]
    PfamiPF00656. Peptidase_C14. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q08601-1 [UniParc]FASTAAdd to Basket

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    MYPGSGRYTY NNAGGNNGYQ RPMAPPPNQQ YGQQYGQQYE QQYGQQYGQQ    50
    NDQQFSQQYA PPPGPPPMAY NRPVYPPPQF QQEQAKAQLS NGYNNPNVNA 100
    SNMYGPPQNM SLPPPQTQTI QGTDQPYQYS QCTGRRKALI IGINYIGSKN 150
    QLRGCINDAH NIFNFLTNGY GYSSDDIVIL TDDQNDLVRV PTRANMIRAM 200
    QWLVKDAQPN DSLFLHYSGH GGQTEDLDGD EEDGMDDVIY PVDFETQGPI 250
    IDDEMHDIMV KPLQQGVRLT ALFDSCHSGT VLDLPYTYST KGIIKEPNIW 300
    KDVGQDGLQA AISYATGNRA ALIGSLGSIF KTVKGGMGNN VDRERVRQIK 350
    FSAADVVMLS GSKDNQTSAD AVEDGQNTGA MSHAFIKVMT LQPQQSYLSL 400
    LQNMRKELAG KYSQKPQLSS SHPIDVNLQF IM 432
    Length:432
    Mass (Da):47,982
    Last modified:May 20, 2008 - v2
    Checksum:i547D186E3EB481B7
    GO

    Sequence cautioni

    The sequence AAT92851.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA99410.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z75105 Genomic DNA. Translation: CAA99410.1. Different initiation.
    AY692832 Genomic DNA. Translation: AAT92851.1. Different initiation.
    BK006948 Genomic DNA. Translation: DAA10972.1.
    PIRiS67089.
    RefSeqiNP_014840.4. NM_001183616.3.

    Genome annotation databases

    EnsemblFungiiYOR197W; YOR197W; YOR197W.
    GeneIDi854372.
    KEGGisce:YOR197W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z75105 Genomic DNA. Translation: CAA99410.1 . Different initiation.
    AY692832 Genomic DNA. Translation: AAT92851.1 . Different initiation.
    BK006948 Genomic DNA. Translation: DAA10972.1 .
    PIRi S67089.
    RefSeqi NP_014840.4. NM_001183616.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F6O X-ray 1.68 A 83-432 [» ]
    4F6P X-ray 1.62 A 83-432 [» ]
    ProteinModelPortali Q08601.
    SMRi Q08601. Positions 90-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34595. 56 interactions.
    DIPi DIP-2802N.
    IntActi Q08601. 7 interactions.
    MINTi MINT-533648.
    STRINGi 4932.YOR197W.

    Protein family/group databases

    MEROPSi C14.035.

    Proteomic databases

    MaxQBi Q08601.
    PaxDbi Q08601.
    PeptideAtlasi Q08601.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR197W ; YOR197W ; YOR197W .
    GeneIDi 854372.
    KEGGi sce:YOR197W.

    Organism-specific databases

    CYGDi YOR197w.
    SGDi S000005723. MCA1.

    Phylogenomic databases

    eggNOGi NOG68179.
    HOGENOMi HOG000240109.
    OMAi YERTKRT.
    OrthoDBi EOG78PVMS.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33705-MONOMER.

    Miscellaneous databases

    NextBioi 976502.

    Gene expression databases

    Genevestigatori Q08601.

    Family and domain databases

    Gene3Di 3.40.50.1460. 1 hit.
    InterProi IPR029030. Caspase-like_dom.
    IPR011600. Pept_C14_caspase.
    [Graphical view ]
    Pfami PF00656. Peptidase_C14. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. 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. Cited for: FUNCTION.
    11. 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. 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.

    Entry informationi

    Entry nameiMCA1_YEAST
    AccessioniPrimary (citable) accession number: Q08601
    Secondary accession number(s): D6W2Q6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1400 molecules/cell in log phase SD medium.1 Publication

    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.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3