P33435
PR
Gene name |
Mmp13 |
Protein name |
Collagenase 3 |
Names |
Matrix metalloproteinase-13, MMP-13 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:17386 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for P33435
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1CXV | X-ray | 200 A | A/B | 105-268 | PDB |
| AF-P33435-F1 | Predicted | AlphaFoldDB |
15 variants for P33435
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389009825 | 12 | L>V | No | EVA | |
| rs3388991760 | 20 | L>Q | No | EVA | |
| rs3389023190 | 23 | P>H | No | EVA | |
| rs3389016750 | 36 | D>N | No | EVA | |
| rs3389020860 | 111 | T>R | No | EVA | |
| rs3400039842 | 141 | K>I | No | EVA | |
| rs232479590 | 171 | K>N | No | EVA | |
| rs3389016802 | 217 | L>F | No | EVA | |
| rs3389002489 | 239 | A>V | No | EVA | |
| rs3389028355 | 260 | V>A | No | EVA | |
| rs239017329 | 265 | F>S | No | EVA | |
| rs3389016733 | 314 | P>H | No | EVA | |
| rs3388991786 | 327 | F>Y | No | EVA | |
| rs48999703 | 348 | F>L | No | EVA | |
| rs3389009797 | 449 | I>M | No | EVA |
No associated diseases with P33435
11 regional properties for P33435
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Hemopexin-like domain | 282 - 472 | IPR000585 |
| domain | Peptidase M10, metallopeptidase | 113 - 268 | IPR001818 |
| domain | Peptidoglycan binding-like | 34 - 92 | IPR002477 |
| domain | Peptidase, metallopeptidase | 110 - 269 | IPR006026 |
| conserved_site | Hemopexin, conserved site | 324 - 339 | IPR018486 |
| repeat | Hemopexin-like repeats | 282 - 333 | IPR018487-1 |
| repeat | Hemopexin-like repeats | 332 - 378 | IPR018487-2 |
| repeat | Hemopexin-like repeats | 380 - 430 | IPR018487-3 |
| repeat | Hemopexin-like repeats | 429 - 472 | IPR018487-4 |
| binding_site | Peptidase M10A, cysteine switch, zinc binding site | 95 - 102 | IPR021158 |
| domain | Peptidase M10A, catalytic domain | 113 - 268 | IPR033739 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular matrix | A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| Golgi apparatus | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. |
| intercellular canaliculus | An extremely narrow tubular channel located between adjacent cells. An instance of this is the secretory canaliculi occurring between adjacent parietal cells in the gastric mucosa of vertebrates. |
| lysosome | A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions. |
9 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent protein binding | Binding to a protein or protein complex in the presence of calcium. |
| collagen binding | Binding to collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%). |
| endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
| fibronectin binding | Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids. |
| low-density lipoprotein particle receptor binding | Binding to a low-density lipoprotein receptor. |
| metalloendopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
| zinc ion binding | Binding to a zinc ion (Zn). |
13 GO annotations of biological process
| Name | Definition |
|---|---|
| bone mineralization | The deposition of hydroxyapatite, a form of calcium phosphate with the formula Ca10(PO4)6(OH)2, in bone tissue. |
| bone morphogenesis | The process in which bones are generated and organized. |
| collagen catabolic process | The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
| endochondral ossification | Replacement ossification wherein bone tissue replaces cartilage. |
| extracellular matrix disassembly | A process that results in the breakdown of the extracellular matrix. |
| extracellular matrix organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. |
| growth plate cartilage development | The process whose specific outcome is the progression of the cartilage that will provide a scaffold for mineralization of endochondral bones as they elongate or grow. |
| heart development | The process whose specific outcome is the progression of the heart over time, from its formation to the mature structure. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood. |
| positive regulation of pancreatic trypsinogen secretion | Any process that activates or increases the frequency, rate or extent of pancreatic trypsinogen secretion. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| protein metabolic process | The chemical reactions and pathways involving a protein. Includes protein modification. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
| response to hormone | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hormone stimulus. |
17 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q3SZV7 | HPX | Hemopexin | Bos taurus (Bovine) | PR |
| Q9GLE5 | MMP2 | 72 kDa type IV collagenase | Bos taurus (Bovine) | PR |
| O77656 | MMP13 | Collagenase 3 | Bos taurus (Bovine) | PR |
| Q90611 | MMP2 | 72 kDa type IV collagenase | Gallus gallus (Chicken) | PR |
| Q8MPP3 | Mmp2 | Matrix metalloproteinase-2 | Drosophila melanogaster (Fruit fly) | PR |
| P04004 | VTN | Vitronectin | Homo sapiens (Human) | PR |
| Q99542 | MMP19 | Matrix metalloproteinase-19 | Homo sapiens (Human) | PR |
| Q9NPA2 | MMP25 | Matrix metalloproteinase-25 | Homo sapiens (Human) | PR |
| Q9H239 | MMP28 | Matrix metalloproteinase-28 | Homo sapiens (Human) | PR |
| P45452 | MMP13 | Collagenase 3 | Homo sapiens (Human) | PR |
| P34960 | Mmp12 | Macrophage metalloelastase | Mus musculus (Mouse) | PR |
| P33434 | Mmp2 | 72 kDa type IV collagenase | Mus musculus (Mouse) | PR |
| P28862 | Mmp3 | Stromelysin-1 | Mus musculus (Mouse) | PR |
| Q63341 | Mmp12 | Macrophage metalloelastase | Rattus norvegicus (Rat) | PR |
| P33436 | Mmp2 | 72 kDa type IV collagenase | Rattus norvegicus (Rat) | PR |
| P23097 | Mmp13 | Collagenase 3 | Rattus norvegicus (Rat) | PR |
| Q6PHG2 | hpx | Hemopexin | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHSAILATFF | LLSWTPCWSL | PLPYGDDDDD | DLSEEDLVFA | EHYLKSYYHP | ATLAGILKKS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TVTSTVDRLR | EMQSFFGLEV | TGKLDDPTLD | IMRKPRCGVP | DVGEYNVFPR | TLKWSQTNLT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YRIVNYTPDM | SHSEVEKAFR | KAFKVWSDVT | PLNFTRIYDG | TADIMISFGT | KEHGDFYPFD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GPSGLLAHAF | PPGPNYGGDA | HFDDDETWTS | SSKGYNLFIV | AAHELGHSLG | LDHSKDPGAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MFPIYTYTGK | SHFMLPDDDV | QGIQFLYGPG | DEDPNPKHPK | TPEKCDPALS | LDAITSLRGE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TMIFKDRFFW | RLHPQQVEAE | LFLTKSFWPE | LPNHVDAAYE | HPSRDLMFIF | RGRKFWALNG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YDILEGYPRK | ISDLGFPKEV | KRLSAAVHFE | NTGKTLFFSE | NHVWSYDDVN | QTMDKDYPRL |
| 430 | 440 | 450 | 460 | 470 | |
| IEEEFPGIGN | KVDAVYEKNG | YIYFFNGPIQ | FEYSIWSNRI | VRVMPTNSIL | WC |