Detail Information for IndEnz0002000934
IED ID IndEnz0002000934
Enzyme Type ID protease000934
Protein Name Peptidase inhibitor 16
PI-16
Cysteine-rich secretory protein 9
CRISP-9
PSP94-binding protein
CD antigen CD364
Gene Name PI16 CRISP9 PSPBP PSEC0164 UNQ289/PRO328
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 MHGSCSFLMLLLPLLLLLVATTGPVGALTDEEKRLMVELHNLYRAQVSPTASDMLHMRWDEELAAFAKAYARQCVWGHNKERGRRGENLFAITDEGMDVPLAMEEWHHEREHYNLSAATCSPGQMCGHYTQVVWAKTERIGCGSHFCEKLQGVEETNIELLVCNYEPPGNVKGKRPYQEGTPCSQCPSGYHCKNSLCEPIGSPEDAQDLPYLVTEAPSFRATEASDSRKMGTPSSLATGIPAFLVTEVSGSLATKALPAVETQAPTSLATKDPPSMATEAPPCVTTEVPSILAAHSLPSLDEEPVTFPKSTHVPIPKSADKVTDKTKVPSRSPENSLDPKMSLTGARELLPHAQEEAEAEAELPPSSEVLASVFPAQDKPGELQATLDHTGHTSSKSLPNFPNTSATANATGGRALALQSSLPGAEGPDKPSVVSGLNSGPGHVWGPLLGLLLLPPLVLAGIF
Enzyme Length 463
Uniprot Accession Number Q6UXB8
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: May inhibit cardiomyocyte growth. {ECO:0000250|UniProtKB:Q9ET66}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Compositional bias (1); Domain (1); Frameshift (1); Glycosylation (3); Natural variant (2); Region (4); Sequence conflict (2); Signal peptide (1)
Keywords Alternative splicing;Direct protein sequencing;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Signal
Interact With P27449; P60201-2; P0DN84; P55061; Q9H2L4; Q8N2M4
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15344909, ECO:0000269|PubMed:17062675, ECO:0000269|PubMed:22171320}.
Modified Residue
Post Translational Modification PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:15344909, ECO:0000269|PubMed:22171320}.
Signal Peptide SIGNAL 1..27; /evidence=ECO:0000269|PubMed:15344909
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 20237162; 22533972; 27996045; 30365157; 31127857;
Motif
Gene Encoded By
Mass 49,471
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda