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Q08601

- MCA1_YEAST

UniProt

Q08601 - MCA1_YEAST

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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

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
Complete GO annotation...

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
Complete GO annotation...

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. 77 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.
InParanoidiQ08601.
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

« Hide

        10         20         30         40         50
MYPGSGRYTY NNAGGNNGYQ RPMAPPPNQQ YGQQYGQQYE QQYGQQYGQQ
60 70 80 90 100
NDQQFSQQYA PPPGPPPMAY NRPVYPPPQF QQEQAKAQLS NGYNNPNVNA
110 120 130 140 150
SNMYGPPQNM SLPPPQTQTI QGTDQPYQYS QCTGRRKALI IGINYIGSKN
160 170 180 190 200
QLRGCINDAH NIFNFLTNGY GYSSDDIVIL TDDQNDLVRV PTRANMIRAM
210 220 230 240 250
QWLVKDAQPN DSLFLHYSGH GGQTEDLDGD EEDGMDDVIY PVDFETQGPI
260 270 280 290 300
IDDEMHDIMV KPLQQGVRLT ALFDSCHSGT VLDLPYTYST KGIIKEPNIW
310 320 330 340 350
KDVGQDGLQA AISYATGNRA ALIGSLGSIF KTVKGGMGNN VDRERVRQIK
360 370 380 390 400
FSAADVVMLS GSKDNQTSAD AVEDGQNTGA MSHAFIKVMT LQPQQSYLSL
410 420 430
LQNMRKELAG KYSQKPQLSS SHPIDVNLQF IM
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. 77 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.
InParanoidi Q08601.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 104 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