P79227
Gene name |
MMP12 |
Protein name |
Macrophage metalloelastase |
Names |
MME, Matrix metalloproteinase-12, MMP-12 |
Species |
Oryctolagus cuniculus (Rabbit) |
KEGG Pathway |
ocu:100009559 |
EC number |
3.4.24.65: Metalloendopeptidases |
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
1 structures for P79227
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P79227-F1 | Predicted | AlphaFoldDB |
No variants for P79227
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P79227 | |||||
No associated diseases with P79227
11 regional properties for P79227
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Hemopexin-like domain | 274 - 464 | IPR000585 |
| domain | Peptidase M10, metallopeptidase | 104 - 258 | IPR001818 |
| domain | Peptidoglycan binding-like | 22 - 82 | IPR002477 |
| domain | Peptidase, metallopeptidase | 100 - 259 | IPR006026 |
| conserved_site | Hemopexin, conserved site | 316 - 331 | IPR018486 |
| repeat | Hemopexin-like repeats | 274 - 325 | IPR018487-1 |
| repeat | Hemopexin-like repeats | 324 - 370 | IPR018487-2 |
| repeat | Hemopexin-like repeats | 372 - 422 | IPR018487-3 |
| repeat | Hemopexin-like repeats | 421 - 464 | IPR018487-4 |
| binding_site | Peptidase M10A, cysteine switch, zinc binding site | 85 - 92 | IPR021158 |
| domain | Peptidase M10A, catalytic domain | 104 - 258 | IPR033739 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.24.65 | Metalloendopeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKFLLLILTL | WVTSSGADPL | KENDMLFAEN | YLENFYGLKV | ERIPMTKMKT | NRNFIEEKVQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EMQQFLGLNV | TGQLDTSTLE | MMHKPRCGVP | DVYHFKTMPG | RPVWRKHYIT | YRIKNYTPDM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KREDVEYAIQ | KAFQVWSDVT | PLKFRKITTG | KADIMILFAS | GAHGDYGAFD | GRGGVIAHAF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GPGPGIGGDT | HFDEDEIWSK | SYKGTNLFLV | AVHELGHALG | LDHSNDPKAI | MFPTYGYIDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NTFHLSADDI | RGIQSLYGGP | EQHQPMPKPD | NPEPTACDHN | LKFDAVTTVG | NKIFFFKDSF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FWWKIPKSST | TSVRLISSLW | PTLPSGIEAA | YEIGDRHQVF | LFKGDKFWLI | SHLRLQPNYP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KSIHSLGFPD | FVKKIDAAVF | NPSLRKTYFF | VDNLYWRYDE | RREVMDAGYP | KLITKHFPGI |
| 430 | 440 | 450 | 460 | ||
| GPKIDAVFYF | QRYYYFFQGP | NQLEYDTFSS | RVTKKLKSNS | WFDC |