Detail Information for IndEnz0002006536
IED ID IndEnz0002006536
Enzyme Type ID protease006536
Protein Name Matrix metalloproteinase-27
MMP-27
EC 3.4.24.-
Gene Name MMP27
Organism Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri)
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 Scandentia (tree shrews) Tupaiidae (tree shrews) Tupaia Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri)
Enzyme Sequence MKSFLLLFLLFVTFSSALPADQKMENEENMQLAQAYLNQFYSLEIEGSHLVQSKNGSLLDGKIREMQAFFGLTVTGTLDSNTLEIMKTPRCGVPDVGQYGYTLPGWRKYNLTYRIMNYTPDMARADVDEAIQKALEVWSKVTPLTFTKIFKGIADIMIAFRTRVHGRCPRYFDGPLGVLGHAFPPGLGLGGDTHFDEDENWTKDTAGFSLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPSKYPLSQDDIDGIQSIYGGLPTTPSKPKGPKIPHACDPDLTFDAITNIRREVMFFKGRHLWRIYHDITDVEFELIASFWPSLPADLQAAYENPRDKILVFKDENFWMIGAYNVLPRYPRSIHILGFPRYVKKIDAAVCDQDTRKTYFFVGIWCWRYDEMTRTMDRGYPQRIVRHFPGIGLRVDAAFQHKGFFYFFRGSKQFEYDIKAKSITRIMRTNTWFQCKEPLNSSLDFHFNQEKAYSGEVETLHHQSLSLLIFGIVHLLNKICSY
Enzyme Length 512
Uniprot Accession Number Q9GKE1
Absorption
Active Site ACT_SITE 217; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (20); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1)
Keywords Calcium;Collagen degradation;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Repeat;Signal;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H306}. Note=Retained in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9H306}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9H306}.
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250
Gene Encoded By
Mass 58,816
Kinetics
Metal Binding METAL 91; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 121; /note=Calcium 1; /evidence=ECO:0000250; METAL 155; /note=Calcium 2; /evidence=ECO:0000250; METAL 165; /note=Zinc 1; /evidence=ECO:0000250; METAL 173; /note=Calcium 3; /evidence=ECO:0000250; METAL 174; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 181; /note=Zinc 1; /evidence=ECO:0000250; METAL 188; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 192; /note=Calcium 2; /evidence=ECO:0000250; METAL 194; /note=Zinc 1; /evidence=ECO:0000250; METAL 196; /note=Calcium 3; /evidence=ECO:0000250; METAL 199; /note=Calcium 1; /evidence=ECO:0000250; METAL 199; /note=Calcium 3; /evidence=ECO:0000250; METAL 216; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 220; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 226; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 286; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 377; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 426; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda