Detail Information for IndEnz0002010824
IED ID IndEnz0002010824
Enzyme Type ID protease010824
Protein Name Suppressor of tumorigenicity 14 protein homolog
EC 3.4.21.109
Epithin
Serine protease 14
Gene Name St14 Prss14
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MGSNRGRKAGGGSQDFGAGLKYNSRLENMNGFEEGVEFLPANNAKKVEKRGPRRWVVLVAVLFSFLLLSLMAGLLVWHFHYRNVRVQKVFNGHLRITNEIFLDAYENSTSTEFISLASQVKEALKLLYNEVPVLGPYHKKSAVTAFSEGSVIAYYWSEFSIPPHLAEEVDRAMAVERVVTLPPRARALKSFVLTSVVAFPIDPRMLQRTQDNSCSFALHAHGAAVTRFTTPGFPNSPYPAHARCQWVLRGDADSVLSLTFRSFDVAPCDEHGSDLVTVYDSLSPMEPHAVVRLCGTFSPSYNLTFLSSQNVFLVTLITNTDRRHPGFEATFFQLPKMSSCGGFLSDTQGTFSSPYYPGHYPPNINCTWNIKVPNNRNVKVRFKLFYLVDPNVPVGSCTKDYVEINGEKYCGERSQFVVSSNSSKITVHFHSDHSYTDTGFLAEYLSYDSNDPCPGMFMCKTGRCIRKELRCDGWADCPDYSDERYCRCNATHQFTCKNQFCKPLFWVCDSVNDCGDGSDEEGCSCPAGSFKCSNGKCLPQSQKCNGKDNCGDGSDEASCDSVNVVSCTKYTYRCQNGLCLSKGNPECDGKTDCSDGSDEKNCDCGLRSFTKQARVVGGTNADEGEWPWQVSLHALGQGHLCGASLISPDWLVSAAHCFQDDKNFKYSDYTMWTAFLGLLDQSKRSASGVQELKLKRIITHPSFNDFTFDYDIALLELEKSVEYSTVVRPICLPDATHVFPAGKAIWVTGWGHTKEGGTGALILQKGEIRVINQTTCEDLMPQQITPRMMCVGFLSGGVDSCQGDSGGPLSSAEKDGRMFQAGVVSWGEGCAQRNKPGVYTRLPVVRDWIKEHTGV
Enzyme Length 855
Uniprot Accession Number P56677
Absorption
Active Site ACT_SITE 656; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 711; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 805; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position.; EC=3.4.21.109;
DNA Binding
EC Number 3.4.21.109
Enzyme Function FUNCTION: Degrades extracellular matrix. Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site (By similarity). Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (18); Domain (8); Glycosylation (6); Modified residue (1); Topological domain (2); Transmembrane (1)
Keywords Disulfide bond;Glycoprotein;Hydrolase;Membrane;Phosphoprotein;Protease;Reference proteome;Repeat;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Modified Residue MOD_RES 13; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11567025; 12032844; 12466851; 12520002; 14610273; 14638864; 14747469; 15629466; 15848395; 16103220; 16141072; 16170303; 16428450; 16524950; 16651618; 16980306; 16983341; 17174946; 17228523; 17328885; 17471493; 17940283; 17967808; 18402552; 18554416; 18713750; 18799693; 18832587; 19156209; 19387477; 19389929; 19592578; 19717635; 19853659; 20142489; 20152175; 20398629; 20652801; 20657595; 21149451; 21217780; 21267068; 22081509; 22139080; 22514623; 22952456; 24194600; 24469043; 24551030; 24685580; 24962579; 25078604; 25245289; 25486433; 25873032; 26599507; 27385010; 28094766; 28490634; 30559294; 31628112; 32907879;
Motif
Gene Encoded By
Mass 94,655
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda