| IED ID | IndEnz0002016253 |
| Enzyme Type ID | protease016253 |
| Protein Name |
Calpain small subunit 1 CSS1 Calcium-activated neutral proteinase small subunit CANP small subunit Calcium-dependent protease small subunit CDPS Calcium-dependent protease small subunit 1 Calpain regulatory subunit |
| Gene Name | CAPNS1 CAPN4 CAPNS |
| 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 | MFLVNSFLKGGGGGGGGGGGLGGGLGNVLGGLISGAGGGGGGGGGGGGGGGGGGGGTAMRILGGVISAISEAAAQYNPEPPPPRTHYSNIEANESEEVRQFRRLFAQLAGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYKQFDTDRSGTICSSELPGAFEAAGFHLNEHLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQEWLQLTMYS |
| Enzyme Length | 268 |
| Uniprot Accession Number | P04632 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | CA_BIND 108..119; /note=1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 152..163; /note=2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448; CA_BIND 182..193; /note=3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00448 |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Essential for embryonic development (By similarity). {ECO:0000250|UniProtKB:O88456}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Calcium binding (3); Chain (1); Domain (5); Helix (9); Metal binding (16); Modified residue (3); Natural variant (1); Sequence conflict (5); Turn (2) |
| Keywords | 3D-structure;Acetylation;Calcium;Cell membrane;Cytoplasm;Direct protein sequencing;Membrane;Metal-binding;Phosphoprotein;Reference proteome;Repeat |
| Interact With | Q6RW13; Q96NL8; P17655; P20936 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon calcium binding. {ECO:0000250}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"; MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 179; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1KFU; 1KFX; 4PHJ; 4PHK; 4PHM; 4WQ2; 4WQ3; 5D69; 6QLB; |
| Mapped Pubmed ID | 10830966; 11076937; 11853546; 12121983; 12393869; 12843408; 15611136; 16169070; 17110338; 17515931; 17608959; 18234454; 18519038; 18544539; 18761085; 19486527; 19712109; 19913121; 19942621; 20107320; 20179351; 20419804; 20628086; 20711500; 21030783; 21268016; 21670566; 21864727; 21988832; 21997417; 22623428; 23035980; 23349941; 23629652; 24297866; 24514433; 24628706; 24703594; 24962955; 25086406; 25304384; 25416956; 25636510; 26496610; 26771715; 27878263; 28757975; 28857668; 29331389; 29331762; 29648579; 30444080; 30448882; 30452399; 31691433; 32777225; 33760208; 33887737; 7698360; 9228946; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,316 |
| Kinetics | |
| Metal Binding | METAL 109; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 112; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 114; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 119; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 137; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 152; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 154; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 156; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 158; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 163; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 182; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 184; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 186; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 188; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 193; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:Q64537; METAL 225; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:Q64537 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.53;3.4.22.B24; |