Detail Information for IndEnz0002015294
IED ID IndEnz0002015294
Enzyme Type ID protease015294
Protein Name Calpastatin
Calpain inhibitor
Gene Name CAST
Organism Sus scrofa (Pig)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig)
Enzyme Sequence MNPTETKAIPVSKQLEGPHSPNKKRHKKQAVKTEPEKKSQSTKPSVVHEKKTQEVKPKEHPEPKSLPTHSADAGSKRAHKEKAVSRSNEQPTSEKSTKPKAKPQDPTPSDGKLSVTGVSAASGKPAETKKDDKSLTSSVPAESKSSKPSGKSDMDAALDDLIDTLGGPEETEEDNTTYTGPEVLDPMSSTYIEELGKREVTLPPKYRELLDKKEGIPVPPPDTSKPLGPDDAIDALSLDLTCSSPTADGKKTEKEKSTGEVLKAQSVGVIKSAAAPPHEKKRRVEEDTMSDQALEALSASLGSRKSEPELDLSSIKEIDEAKAKEEKLKKCGEDDETVPPEYRLKPAMDKDGKPLLPEAEEKPKPLSESELIDELSEDFDQSKRKEKQSKPTEKTKESQATAPTPVGEAVSRTSLCCVQSAPPKPATGMVPDDAVEALAGSLGKKEADPEDGKPVEDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKTLPHKDPKEPVLPLSEDFVLDALSQDFAGPPAASSLFEDAKLSAAVSEVVSQTSAPTTHSAGPPPDTVSDDKKLDDALDQLSDSLGQRQPDPDENKPIEDKVKEKAEAEHRDKLGERDDTIPPEYRHLLDKDEEGKSTKPPTKKPEAPKKPEAAQDPIDALSGDFDRCPSTTETSENTTKDKDKKTASKSKAPKNGGKAKDSTKAKEETSKQKSDGKSTS
Enzyme Length 713
Uniprot Accession Number P12675
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme 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.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (9); Cross-link (1); Helix (1); Modified residue (13); Region (3); Repeat (4); Sequence conflict (1)
Keywords 3D-structure;Acetylation;Isopeptide bond;Phosphoprotein;Protease inhibitor;Reference proteome;Repeat;Thiol protease inhibitor;Ubl conjugation
Interact With
Induction
Subcellular Location
Modified Residue MOD_RES 50; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P51125; MOD_RES 87; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P51125; MOD_RES 134; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 136; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P27321; MOD_RES 244; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 367; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 369; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 376; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 441; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 517; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 528; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 575; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810; MOD_RES 577; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P20810
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 1NX0; 1NX1;
Mapped Pubmed ID 12684003;
Motif
Gene Encoded By
Mass 77,124
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda