IED ID | IndEnz0002001036 |
Enzyme Type ID | protease001036 |
Protein Name |
Serine protease inhibitor A3L Serpin A3L CPI-23 Contrapsin-like protease inhibitor 3 Serine protease inhibitor 1 SPI-1 |
Gene Name | Serpina3l Spin2a |
Organism | Rattus norvegicus (Rat) |
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MAFIAALGLLMAGICPAVLCDGTLGRDTLSHEDHGKGRQLHSLTLASSNTDFALSLYKKLALRNPDKNVVFSPLSISAALTILSLGAKDSTMEEILEGLKFNLTEITEEEIHQGFGHLLQRLSQPEDQVEINTGSALFIDKEQPILSEFQEKTRALYQAEAFIADFKQPNEAKKLINDYVSNQTQGKIAELFSDLEERTSMVLVNYLLFKGKWKVPFNPNDTFESEFYLDEKRSVKVPMMKIKEVTTPYVRDEELSCSVLELKYTGNASALFILPDQGKMQQVESSLQPETLKKWKDSLIPRIINDLRMPKFSISTDYSLKEVLPELGIKKVFSQQADLSRITGTKDLYVSQVVHKAVLDVDETGTEATAATGVATVIRRQPRTLNFNRPFMVVITDMDSQSILFVAKITNPK |
Enzyme Length | 413 |
Uniprot Accession Number | P05544 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Glycosylation (4); Modified residue (1); Region (1); Sequence conflict (1); Signal peptide (1); Site (1) |
Keywords | Direct protein sequencing;Glycoprotein;Phosphoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
Interact With | |
Induction | INDUCTION: By growth hormone. Reduced during acute inflammation. {ECO:0000269|PubMed:1694763, ECO:0000269|PubMed:3494016}. |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | MOD_RES 30; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:1694763}. |
Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 46,277 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |