| IED ID | IndEnz0001000319 |
| Enzyme Type ID | amylase000319 |
| Protein Name |
Crustacean hyperglycemic hormones isoform A Cleaved into: CHH precursor-related peptide A CPRP-A ; Crustacean hyperglycemic hormone A CHH-A Molt-inhibiting hormone MIH |
| Gene Name | |
| Organism | Homarus americanus (American lobster) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Crustacea Multicrustacea Malacostraca Eumalacostraca Eucarida Decapoda Pleocyemata Astacidea (true lobsters and crayfishes) Nephropoidea Nephropidae (clawed lobsters) Homarus Homarus americanus (American lobster) |
| Enzyme Sequence | MMACRTLCLVVVMVASLGTSGVGGRSVEGASRMEKLLSSSNSPSSTPLGFLSQDHSVNKRQVFDQACKGVYDRNLFKKLDRVCEDCYNLYRKPFVATTCRENCYSNWVFRQCLDDLLLSDVIDEYVSNVQMVGK |
| Enzyme Length | 134 |
| Uniprot Accession Number | P19806 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: CHH is the most abundant hormone in the sinus gland of isopods and decapods which controls the blood sugar level. Has a secretagogue action over the amylase released from the midgut gland. May act as a stress hormone.; FUNCTION: MIH may inhibit Y-organs where molting hormone (ecdysteroid) is secreted and a molting cycle is initiated when MIH secretion diminishes or stops. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Disulfide bond (3); Modified residue (3); Peptide (2); Sequence conflict (4); Signal peptide (1) |
| Keywords | Amidation;Carbohydrate metabolism;Cleavage on pair of basic residues;D-amino acid;Direct protein sequencing;Disulfide bond;Glucose metabolism;Hormone;Neuropeptide;Pyrrolidone carboxylic acid;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 61; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:8034574; MOD_RES 63; /note=D-phenylalanine; in form CHH-A-II; /evidence=ECO:0000269|PubMed:8034574; MOD_RES 132; /note=Valine amide; /evidence=ECO:0000269|PubMed:1879416 |
| Post Translational Modification | PTM: Stereoinversion of L-Phe (form CHH-A-I) to D-Phe (form CHH-A-II). {ECO:0000269|PubMed:8034574}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 14,996 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |