P51125 · ICAL_MOUSE
- ProteinCalpastatin
- GeneCast
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids788 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | membrane | |
Cellular Component | postsynaptic density | |
Molecular Function | calcium-dependent cysteine-type endopeptidase inhibitor activity | |
Molecular Function | protease binding | |
Biological Process | egg activation | |
Biological Process | negative regulation of type B pancreatic cell apoptotic process | |
Biological Process | protein catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCalpastatin
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP51125
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000147633 | 1-788 | Calpastatin | |||
Sequence: MSQPGPKPAASPRPSRGAAARHTQEHVNEKNIGSSSKPGEKKGSDEKKAASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIPVNKQLEGPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKNLPKHTSSTGSKHAHKEKALSRSNEQMVSEKPSESKTKFQDVPSAGGESVAGGGTVATALDKVVGKKKEQKPFTPASPVQSTPSKPSDKSGMDAALDDLIDTLGGHEDTNRDDPPYTGPVVLDPMYSTYLEALGIKEGTIPPEYRKLLEKNEGITQPLPDSPKPMGTDQAIDALSSDFTCSSPTGKQSEKEKSTGEIFKAQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLSESELIGELSADFDRSTYQDKPSTPAEKKSNDTSQTPPGETVPRASMCSIRSAPPKLASLKGVVPEDAVETLAGSLGTREADPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLPKESQEQLAPLSDDFLLDALSQDFSSPANISSLEFEDAKLSAAISEVVSQTPAPSTHAAAPLPGTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALSEDLDSCPSTTETSKNTAKGKSKKTSSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS | ||||||
Modified residue | 11 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 112 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 129 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 165 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 216 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 219 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 303 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 324 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 444 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 446 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 453 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 479 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 518 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 594 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 605 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 653 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 655 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 2 is the major form in all tissues examined. Isoform 1 accounts for 5-10% in tissues such as skeletal muscle, liver and brain, and 30% in myoblasts. Isoforms 4 and 5 are testis-specific. Isoform 6 is highly expressed in heart and skeletal muscle with lower levels in liver, brain and testis. Isoform 7 is expressed at high levels in liver.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-262 | Disordered | ||||
Sequence: MSQPGPKPAASPRPSRGAAARHTQEHVNEKNIGSSSKPGEKKGSDEKKAASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIPVNKQLEGPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKNLPKHTSSTGSKHAHKEKALSRSNEQMVSEKPSESKTKFQDVPSAGGESVAGGGTVATALDKVVGKKKEQKPFTPASPVQSTPSKPSDKSGMDAALDDLIDTLGGHEDTNRDDPPYTGPV | ||||||
Compositional bias | 49-93 | Polar residues | ||||
Sequence: AASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIP | ||||||
Compositional bias | 100-143 | Basic and acidic residues | ||||
Sequence: GPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKN | ||||||
Compositional bias | 152-179 | Basic and acidic residues | ||||
Sequence: GSKHAHKEKALSRSNEQMVSEKPSESKT | ||||||
Compositional bias | 216-230 | Polar residues | ||||
Sequence: TPASPVQSTPSKPSD | ||||||
Compositional bias | 233-255 | Basic and acidic residues | ||||
Sequence: GMDAALDDLIDTLGGHEDTNRDD | ||||||
Repeat | 251-303 | Inhibitory domain 1 | ||||
Sequence: TNRDDPPYTGPVVLDPMYSTYLEALGIKEGTIPPEYRKLLEKNEGITQPLPDS | ||||||
Region | 289-493 | Disordered | ||||
Sequence: LLEKNEGITQPLPDSPKPMGTDQAIDALSSDFTCSSPTGKQSEKEKSTGEIFKAQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLSESELIGELSADFDRSTYQDKPSTPAEKKSNDTSQTPPGETVPRASMCSI | ||||||
Compositional bias | 314-330 | Polar residues | ||||
Sequence: DALSSDFTCSSPTGKQS | ||||||
Compositional bias | 352-366 | Basic and acidic residues | ||||
Sequence: VPPKEKKRKVEEEVI | ||||||
Compositional bias | 370-389 | Polar residues | ||||
Sequence: ALQALSDSLGTRQPDPPSHV | ||||||
Repeat | 384-436 | Inhibitory domain 2 | ||||
Sequence: DPPSHVSQAEQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEP | ||||||
Compositional bias | 394-444 | Basic and acidic residues | ||||
Sequence: QVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLS | ||||||
Compositional bias | 471-485 | Polar residues | ||||
Sequence: KKSNDTSQTPPGETV | ||||||
Region | 514-580 | Disordered | ||||
Sequence: TLAGSLGTREADPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLPKESQEQ | ||||||
Compositional bias | 522-574 | Basic and acidic residues | ||||
Sequence: READPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLP | ||||||
Repeat | 524-577 | Inhibitory domain 3 | ||||
Sequence: ADPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLPKES | ||||||
Region | 620-788 | Disordered | ||||
Sequence: VVSQTPAPSTHAAAPLPGTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALSEDLDSCPSTTETSKNTAKGKSKKTSSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS | ||||||
Compositional bias | 637-730 | Basic and acidic residues | ||||
Sequence: GTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALS | ||||||
Repeat | 661-714 | Inhibitory domain 4 | ||||
Sequence: PDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTK | ||||||
Compositional bias | 733-753 | Polar residues | ||||
Sequence: LDSCPSTTETSKNTAKGKSKK | ||||||
Compositional bias | 755-788 | Basic and acidic residues | ||||
Sequence: SSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS |
Domain
Each of the four flexible inhibitory domains can inhibit one calcium-bound calpain molecule by occupying both sides of the active site.
Sequence similarities
Belongs to the protease inhibitor I27 (calpastatin) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 7 isoforms produced by Alternative splicing.
P51125-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsMCS-A
- Length788
- Mass (Da)84,922
- Last updated2002-08-13 v2
- Checksum28E4D3B4A68BFEB9
P51125-2
- Name2
- SynonymsMCS-B
- Differences from canonical
- 92-110: Missing
P51125-3
- Name3
- SynonymsMCS-C
P51125-4
- Name4
- SynonymsTCAST1
P51125-5
- Name5
- SynonymsTCAST2
P51125-6
- Name6
- Differences from canonical
- 1-25: MSQPGPKPAASPRPSRGAAARHTQE → MAFASWWYKT
P51125-7
- Name7
- Differences from canonical
- 1-83: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A338P6J9 | A0A338P6J9_MOUSE | Cast | 520 | ||
A0A1Y7VJN8 | A0A1Y7VJN8_MOUSE | Cast | 445 | ||
Q8C281 | Q8C281_MOUSE | Cast | 686 | ||
Q8CE80 | Q8CE80_MOUSE | Cast | 754 | ||
Q8CE04 | Q8CE04_MOUSE | Cast | 704 | ||
Q921U7 | Q921U7_MOUSE | Cast | 674 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_000745 | 1-25 | in isoform 6 | |||
Sequence: MSQPGPKPAASPRPSRGAAARHTQE → MAFASWWYKT | ||||||
Alternative sequence | VSP_000746 | 1-83 | in isoform 7 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000747 | 1-341 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_000749 | 1-357 | in isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 49-93 | Polar residues | ||||
Sequence: AASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIP | ||||||
Alternative sequence | VSP_000751 | 92-110 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 100-143 | Basic and acidic residues | ||||
Sequence: GPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKN | ||||||
Compositional bias | 152-179 | Basic and acidic residues | ||||
Sequence: GSKHAHKEKALSRSNEQMVSEKPSESKT | ||||||
Compositional bias | 216-230 | Polar residues | ||||
Sequence: TPASPVQSTPSKPSD | ||||||
Compositional bias | 233-255 | Basic and acidic residues | ||||
Sequence: GMDAALDDLIDTLGGHEDTNRDD | ||||||
Alternative sequence | VSP_000752 | 305-333 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 314-330 | Polar residues | ||||
Sequence: DALSSDFTCSSPTGKQS | ||||||
Alternative sequence | VSP_000748 | 342-396 | in isoform 4 | |||
Sequence: AQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVK → MGQFLSSTFWEGSPAAVWQEKLREGERKGAGETIPILQDHVICSEEREHGSKHH | ||||||
Compositional bias | 352-366 | Basic and acidic residues | ||||
Sequence: VPPKEKKRKVEEEVI | ||||||
Alternative sequence | VSP_000750 | 358-397 | in isoform 5 | |||
Sequence: KRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKE → MGQFLSSTFWEGSPAAVWQEKLREGERKGAGETIPILQDH | ||||||
Compositional bias | 370-389 | Polar residues | ||||
Sequence: ALQALSDSLGTRQPDPPSHV | ||||||
Compositional bias | 394-444 | Basic and acidic residues | ||||
Sequence: QVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLS | ||||||
Compositional bias | 471-485 | Polar residues | ||||
Sequence: KKSNDTSQTPPGETV | ||||||
Compositional bias | 522-574 | Basic and acidic residues | ||||
Sequence: READPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLP | ||||||
Compositional bias | 637-730 | Basic and acidic residues | ||||
Sequence: GTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALS | ||||||
Compositional bias | 733-753 | Polar residues | ||||
Sequence: LDSCPSTTETSKNTAKGKSKK | ||||||
Compositional bias | 755-788 | Basic and acidic residues | ||||
Sequence: SSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB026997 EMBL· GenBank· DDBJ | BAA84768.1 EMBL· GenBank· DDBJ | mRNA | ||
AF190152 EMBL· GenBank· DDBJ | AAF25194.1 EMBL· GenBank· DDBJ | mRNA | ||
AF190151 EMBL· GenBank· DDBJ | AAF25193.1 EMBL· GenBank· DDBJ | mRNA | ||
AB044334 EMBL· GenBank· DDBJ | BAB18888.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB044334 EMBL· GenBank· DDBJ | BAB18889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB044334 EMBL· GenBank· DDBJ | BAB18886.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB044334 EMBL· GenBank· DDBJ | BAB18887.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X62519 EMBL· GenBank· DDBJ | CAA44385.1 EMBL· GenBank· DDBJ | mRNA |