Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Metacaspase-1

Gene

MCA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei220By similarity1
Active sitei2761

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: SGD

GO - Biological processi

  • apoptotic process Source: SGD
  • 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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR197W.
SGDiS000005723. MCA1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi276C → A: Blocks the processing and reduces caspase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000268684? – 432Metacaspase-1
PropeptideiPRO_00002686831 – ?Sequence analysis

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiQ08601.
PRIDEiQ08601.

Interactioni

Protein-protein interaction databases

BioGridi34595. 80 interactors.
DIPiDIP-2802N.
IntActiQ08601. 7 interactors.
MINTiMINT-533648.

Structurei

Secondary structure

1432
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni92 – 94Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi136 – 142Combined sources7
Helixi155 – 167Combined sources13
Helixi174 – 176Combined sources3
Beta strandi177 – 181Combined sources5
Helixi187 – 189Combined sources3
Helixi193 – 204Combined sources12
Beta strandi212 – 219Combined sources8
Beta strandi221 – 223Combined sources3
Beta strandi237 – 239Combined sources3
Helixi244 – 247Combined sources4
Helixi252 – 259Combined sources8
Turni260 – 262Combined sources3
Beta strandi268 – 273Combined sources6
Beta strandi275 – 277Combined sources3
Turni279 – 282Combined sources4
Beta strandi285 – 289Combined sources5
Beta strandi292 – 295Combined sources4
Beta strandi354 – 362Combined sources9
Helixi380 – 391Combined sources12
Helixi397 – 408Combined sources12
Turni409 – 411Combined sources3
Beta strandi415 – 422Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F6OX-ray1.68A83-432[»]
4F6PX-ray1.62A83-432[»]
ProteinModelPortaliQ08601.
SMRiQ08601.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni29 – 131Prion domain (PrD)Add BLAST103

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

HOGENOMiHOG000240109.
InParanoidiQ08601.
OMAiYERTKRT.
OrthoDBiEOG092C4ES8.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F6OX-ray1.68A83-432[»]
4F6PX-ray1.62A83-432[»]
ProteinModelPortaliQ08601.
SMRiQ08601.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34595. 80 interactors.
DIPiDIP-2802N.
IntActiQ08601. 7 interactors.
MINTiMINT-533648.

Protein family/group databases

MEROPSiC14.035.

Proteomic databases

MaxQBiQ08601.
PRIDEiQ08601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOR197W.
SGDiS000005723. MCA1.

Phylogenomic databases

HOGENOMiHOG000240109.
InParanoidiQ08601.
OMAiYERTKRT.
OrthoDBiEOG092C4ES8.

Enzyme and pathway databases

BioCyciYEAST:G3O-33705-MONOMER.

Miscellaneous databases

PROiQ08601.

Family and domain databases

Gene3Di3.40.50.1460. 1 hit.
InterProiIPR029030. Caspase-like_dom.
[Graphical view]
SUPFAMiSSF52129. SSF52129. 1 hit.
ProtoNetiSearch...

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: November 2, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.