Q9TRZ7 (TIMP2_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
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: Metalloproteinase inhibitor 2 Alternative name(s): Tissue inhibitor of metalloproteinases 2 Short name=TIMP-2 | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 194 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. |
| Subunit structure | Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity By similarity. |
| Subcellular location | |
| Post-translational modification | The activity of TIMP2 is dependent on the presence of disulfide bonds By similarity. |
| Sequence similarities | Belongs to the protease inhibitor I35 (TIMP) family. [View classification] Contains 1 NTR domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Ligand | Metal-binding Zinc |
| Molecular function | Metalloenzyme inhibitor Metalloprotease inhibitor Protease inhibitor |
| PTM | Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase inhibitor activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 194 | 194 | Metalloproteinase inhibitor 2 | PRO_0000220984 | |||||||
Regions | |||||||||||
| Domain | 1 – 126 | 126 | NTR | ||||||||
| Region | 1 – 5 | 5 | Involved in metalloproteinase-binding By similarity | ||||||||
| Region | 69 – 70 | 2 | Involved in metalloproteinase-binding By similarity | ||||||||
Sites | |||||||||||
| Metal binding | 1 | 1 | Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 1 ↔ 72 | By similarity | |||||||||
| Disulfide bond | 3 ↔ 101 | By similarity | |||||||||
| Disulfide bond | 13 ↔ 126 | By similarity | |||||||||
| Disulfide bond | 128 ↔ 175 | By similarity | |||||||||
| Disulfide bond | 133 ↔ 138 | By similarity | |||||||||
| Disulfide bond | 146 ↔ 167 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 17 | 1 | I → V in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 25 – 26 | 2 | NK → SE in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 58 | 1 | Q → K in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 78 | 1 | I → V in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 93 – 95 | 3 | NGN → DGR in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 109 | 1 | T → S in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 112 | 1 | A → S in AAC95005. Ref.2 | ||||||||
| Sequence conflict | 131 | 1 | T → S in AAC95005. Ref.2 | ||||||||
Sequences
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References
| [1] | "Molecular cloning and characterization of rabbit TIMP2." Wertheimer S.J., Katz S.L. Inflamm. Res. 44:S121-S122(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Temporal alterations in mRNA levels for proteinases and inhibitors and their potential regulators in the healing medial collateral ligament." Reno C., Boykiw R., Martinez M.L., Hart D.A. Biochem. Biophys. Res. Commun. 252:757-763(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-154. Strain: New Zealand white. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF069713 mRNA. Translation: AAC95005.1. |
| UniGene | Ocu.2314. |
3D structure databases | |
| ProteinModelPortal | Q9TRZ7. |
| SMR | Q9TRZ7. Positions 1-192. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | I35.002. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | NOG243625. |
| HOGENOM | HOG000285981. |
| HOVERGEN | HBG068749. |
| OrthoDB | EOG4XPQGS. |
Family and domain databases | |
| InterPro | IPR001134. Netrin_domain. IPR001820. Prot_inh_TIMP. IPR008993. TIMP-like_OB-fold. IPR015613. TIMP2. [Graphical view] |
| PANTHER | PTHR11844. PTHR11844. 1 hit. PTHR11844:SF7. PTHR11844:SF7. 1 hit. |
| Pfam | PF00965. TIMP. 1 hit. [Graphical view] |
| SMART | SM00206. NTR. 1 hit. [Graphical view] |
| SUPFAM | SSF50242. TIMP_like. 1 hit. |
| PROSITE | PS50189. NTR. 1 hit. PS00288. TIMP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TIMP2_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q9TRZ7 Secondary accession number(s): O97589 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
