Detail Information for IndEnz0002019206
IED ID IndEnz0002019206
Enzyme Type ID protease019206
Protein Name Calpain-8
EC 3.4.22.53
New calpain 2
nCL-2
Stomach-specific M-type calpain
Gene Name CAPN8 NCL2
Organism Homo sapiens (Human)
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 Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAAQAAGVSRQRAATQGLGSNQNALKYLGQDFKTLRQQCLDSGVLFKDPEFPACPSALGYKDLGPGSPQTQGIIWKRPTELCPSPQFIVGGATRTDICQGGLGDCWLLAAIASLTLNEELLYRVVPRDQDFQENYAGIFHFQFWQYGEWVEVVIDDRLPTKNGQLLFLHSEQGNEFWSALLEKAYAKLNGCYEALAGGSTVEGFEDFTGGISEFYDLKKPPANLYQIIRKALCAGSLLGCSIDVSSAAEAEAITSQKLVKSHAYSVTGVEEVNFQGHPEKLIRLRNPWGEVEWSGAWSDDAPEWNHIDPRRKEELDKKVEDGEFWMSLSDFVRQFSRLEICNLSPDSLSSEEVHKWNLVLFNGHWTRGSTAGGCQNYPATYWTNPQFKIRLDEVDEDQEESIGEPCCTVLLGLMQKNRRWRKRIGQGMLSIGYAVYQVPKELESHTDAHLGRDFFLAYQPSARTSTYVNLREVSGRARLPPGEYLVVPSTFEPFKDGEFCLRVFSEKKAQALEIGDVVAGNPYEPHPSEVDQEDDQFRRLFEKLAGKDSEITANALKILLNEAFSKRTDIKFDGFNINTCREMISLLDSNGTGTLGAVEFKTLWLKIQKYLEIYWETDYNHSGTIDAHEMRTALRKAGFTLNSQVQQTIALRYACSKLGINFDSFVACMIRLETLFKLFSLLDEDKDGMVQLSLAEWLCCVLV
Enzyme Length 703
Uniprot Accession Number A6NHC0
Absorption
Active Site ACT_SITE 105; /evidence=ECO:0000250; ACT_SITE 262; /evidence=ECO:0000250; ACT_SITE 286; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
DNA Binding
EC Number 3.4.22.53
Enzyme Function FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Beta strand (13); Chain (1); Domain (4); Helix (15); Metal binding (10); Region (1); Sequence conflict (2); Turn (1)
Keywords 3D-structure;Autocatalytic cleavage;Calcium;Cytoplasm;Golgi apparatus;Hydrolase;Metal-binding;Protease;Reference proteome;Repeat;Thiol protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Modified Residue
Post Translational Modification PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which gives rise to fragments extending from Ala-6 to the C-terminus, Ala-6 to the EF-hand 2 domain and from Ala-6 to the beginning of domain III. {ECO:0000250}.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2NQA;
Mapped Pubmed ID 12843408; 17608959; 17646163; 21030783; 21670566; 21864727; 23035980; 28002826;
Motif
Gene Encoded By
Mass 79,144
Kinetics
Metal Binding METAL 588; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 590; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 592; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 594; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 599; /note=Calcium 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 618; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 620; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 622; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 624; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; METAL 629; /note=Calcium 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448
Rhea ID
Cross Reference Brenda 3.4.22.B28;