| IED ID |
IndEnz0002005917 |
| Enzyme Type ID |
protease005917 |
| Protein Name |
Calreticulin
|
| Gene Name |
crt-1 Y38A10A.5 |
| Organism |
Caenorhabditis elegans |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Protostomia
Ecdysozoa
Nematoda (roundworms)
Chromadorea
Rhabditida
Rhabditina
Rhabditomorpha
Rhabditoidea
Rhabditidae
Peloderinae
Caenorhabditis
Caenorhabditis elegans
|
| Enzyme Sequence |
MKSLCLLAIVAVVSAEVYFKEEFNDASWEKRWVQSKHKDDFGAFKLSAGKFFDVESRDQGIQTSQDAKFYSRAAKFDKDFSNKGKTLVIQYTVKHEQGIDCGGGYVKVMRADADLGDFHGETPYNVMFGPDICGPTRRVHVILNYKGENKLIKKEITCKSDELTHLYTLILNSDNTYEVKIDGESAQTGSLEEDWDLLPAKKIKDPDAKKPEDWDEREYIDDAEDAKPEDWEKPEHIPDPDAKKPEDWDDEMDGEWEPPMIDNPEYKGEWKPKQIKNPAYKGKWIHPEIENPEYTPDDELYSYESWGAIGFDLWQVKSGTIFDNIIITDSVEEAEAHAAETFDKLKTVEKEKKEKADEETRKAEEEARKKAEEEKEAKKDDDEEEKEEEEGHDEL |
| Enzyme Length |
395 |
| Uniprot Accession Number |
P27798 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
BINDING 105; /note=An alpha-D-glucoside; /evidence=ECO:0000250|UniProtKB:P14211; BINDING 107; /note=An alpha-D-glucoside; /evidence=ECO:0000250|UniProtKB:P14211; BINDING 124; /note=An alpha-D-glucoside; /evidence=ECO:0000250|UniProtKB:P14211; BINDING 131; /note=An alpha-D-glucoside; /evidence=ECO:0000250|UniProtKB:P14211; BINDING 312; /note=An alpha-D-glucoside; /evidence=ECO:0000250|UniProtKB:P14211 |
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis (PubMed:20153198). Protects dopaminergic neurons against oxidative stress-induced neurodegeneration (PubMed:29346364). May play a role in protection against ER stress. {ECO:0000250|UniProtKB:P14211, ECO:0000269|PubMed:20153198, ECO:0000269|PubMed:24933177, ECO:0000269|PubMed:29346364}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Binding site (5); Chain (1); Compositional bias (4); Disulfide bond (1); Motif (1); Mutagenesis (3); Region (7); Repeat (7); Signal peptide (1) |
| Keywords |
Calcium;Chaperone;Disulfide bond;Endoplasmic reticulum;Lectin;Metal-binding;Reference proteome;Repeat;Signal;Zinc |
| Interact With |
|
| Induction |
INDUCTION: By ER stress in an xbp-1-dependent manner. {ECO:0000269|PubMed:24933177}. |
| Subcellular Location |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. |
| Modified Residue |
|
| Post Translational Modification |
PTM: Cleaved by caspase ced-3 in vitro. {ECO:0000269|PubMed:17371877}. |
| Signal Peptide |
SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
11381264;
11553721;
11580896;
11778048;
12529635;
12679813;
14704431;
15166316;
15782151;
15907843;
16005300;
16256074;
17651753;
18050435;
21177967;
22560298;
22562797;
22569626;
23800452;
25487147;
25491313;
26009280;
26351692;
27129311;
27493871;
27506200;
27994012;
31216475;
|
| Motif |
MOTIF 392..395; /note=Prevents secretion from ER; /evidence=ECO:0000255|PROSITE-ProRule:PRU10138 |
| Gene Encoded By |
|
| Mass |
45,616 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|