P52176 (MMP9_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Matrix metalloproteinase-9 Short name=MMP-9 EC=3.4.24.35 Alternative name(s): 92 kDa gelatinase 92 kDa type IV collagenase Gelatinase B Short name=GELB | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 712 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments By similarity. |
| Catalytic activity | Cleavage of gelatin types I and V and collagen types IV and V. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. Binds 3 calcium ions per subunit By similarity. |
| Subunit structure | Exists as monomer or homodimer; disulfide-linked By similarity. Exists also as heterodimer with a 25 kDa protein By similarity. Interacts with ECM1 By similarity. |
| Subcellular location | Secreted › extracellular space › extracellular matrix Probable. |
| Domain | The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. |
| Post-translational modification | N- and O-glycosylated By similarity. |
| Sequence similarities | Belongs to the peptidase M10A family. Contains 3 fibronectin type-II domains. Contains 4 hemopexin-like domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Collagen degradation |
| Cellular component | Extracellular matrix Secreted |
| Domain | Repeat Signal |
| Ligand | Calcium Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular_component | extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrixInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | By similarity | ||||||||
| Propeptide | 20 – 106 | 87 | Activation peptide | PRO_0000028750 | |||||||
| Chain | 107 – 712 | 606 | Matrix metalloproteinase-9 | PRO_0000028751 | |||||||
Regions | |||||||||||
| Domain | 225 – 273 | 49 | Fibronectin type-II 1 | ||||||||
| Domain | 283 – 331 | 49 | Fibronectin type-II 2 | ||||||||
| Domain | 342 – 390 | 49 | Fibronectin type-II 3 | ||||||||
| Domain | 526 – 570 | 45 | Hemopexin-like 1 | ||||||||
| Domain | 572 – 613 | 42 | Hemopexin-like 2 | ||||||||
| Domain | 618 – 664 | 47 | Hemopexin-like 3 | ||||||||
| Domain | 666 – 709 | 44 | Hemopexin-like 4 | ||||||||
| Motif | 97 – 104 | 8 | Cysteine switch By similarity | ||||||||
Sites | |||||||||||
| Active site | 402 | 1 | By similarity | ||||||||
| Metal binding | 99 | 1 | Zinc 2; in inhibited form By similarity | ||||||||
| Metal binding | 131 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 165 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 175 | 1 | Zinc 1; structural By similarity | ||||||||
| Metal binding | 177 | 1 | Zinc 1; structural By similarity | ||||||||
| Metal binding | 182 | 1 | Calcium 3 By similarity | ||||||||
| Metal binding | 183 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 185 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 187 | 1 | Calcium 3; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 190 | 1 | Zinc 1; structural By similarity | ||||||||
| Metal binding | 197 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 199 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 201 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 203 | 1 | Zinc 1; structural By similarity | ||||||||
| Metal binding | 205 | 1 | Calcium 3 By similarity | ||||||||
| Metal binding | 206 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 208 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 208 | 1 | Calcium 3 By similarity | ||||||||
| Metal binding | 401 | 1 | Zinc 2; catalytic By similarity | ||||||||
| Metal binding | 405 | 1 | Zinc 2; catalytic By similarity | ||||||||
| Metal binding | 411 | 1 | Zinc 2; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 38 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 120 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 127 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 230 ↔ 256 | By similarity | |||||||||
| Disulfide bond | 244 ↔ 271 | By similarity | |||||||||
| Disulfide bond | 288 ↔ 314 | By similarity | |||||||||
| Disulfide bond | 302 ↔ 329 | By similarity | |||||||||
| Disulfide bond | 347 ↔ 373 | By similarity | |||||||||
| Disulfide bond | 361 ↔ 388 | By similarity | |||||||||
| Disulfide bond | 521 ↔ 709 | By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes." Baylis H.A., Megson A., Hall R. Mol. Biochem. Parasitol. 69:211-222(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukocyte. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X78324 mRNA. Translation: CAA55127.1. BC142430 mRNA. Translation: AAI42431.1. |
| IPI | IPI00686326. |
| PIR | I46031. |
| RefSeq | NP_777169.1. NM_174744.2. |
| UniGene | Bt.4714. |
3D structure databases | |
| ProteinModelPortal | P52176. |
| SMR | P52176. Positions 29-444, 518-712. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M10.004. |
Proteomic databases | |
| PaxDb | P52176. |
| PRIDE | P52176. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 282871. |
| KEGG | bta:282871. |
Organism-specific databases | |
| CTD | 4318. |
Phylogenomic databases | |
| eggNOG | NOG328372. |
| HOGENOM | HOG000217926. |
| HOVERGEN | HBG052484. |
| InParanoid | P52176. |
| KO | K01403. |
| OrthoDB | EOG4H9XJZ. |
Family and domain databases | |
| Gene3D | 2.10.10.10. 3 hits. 2.110.10.10. 1 hit. 3.40.390.10. 2 hits. |
| InterPro | IPR000562. FN_type2_col-bd. IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR013806. Kringle-like. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. IPR006970. PT. [Graphical view] |
| Pfam | PF00040. fn2. 3 hits. PF00045. Hemopexin. 3 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. PF04886. PT. 1 hit. [Graphical view] |
| PRINTS | PR00138. MATRIXIN. |
| SMART | SM00059. FN2. 3 hits. SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view] |
| SUPFAM | SSF50923. Hemopexin. 1 hit. SSF57440. Kringle-like. 3 hits. SSF47090. PGBD_like. 1 hit. |
| PROSITE | PS00546. CYSTEINE_SWITCH. 1 hit. PS00023. FN2_1. 3 hits. PS51092. FN2_2. 3 hits. PS00024. HEMOPEXIN. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL5846. |
| NextBio | 20806399. |
Entry information
| Entry name | MMP9_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P52176 Secondary accession number(s): A5PKB8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
