Q9TUL9 (TIMP3_HORSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 73.
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 3 Alternative name(s): Tissue inhibitor of metalloproteinases 3 Short name=TIMP-3 | ||
| Gene names |
| ||
| Organism | Equus caballus (Horse) [Reference proteome] | ||
| Taxonomic identifier | 9796 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › ![]() |
Protein attributes
| Sequence length | 211 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 | Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. |
| Subunit structure | Interacts with EFEMP1 By similarity. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Sequence similarities | Belongs to the protease inhibitor I35 (TIMP) family. [View classification] Contains 1 NTR domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Metalloenzyme inhibitor Metalloprotease inhibitor Protease inhibitor |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular response to organic substance Inferred from electronic annotation. Source: Compara negative regulation of membrane protein ectodomain proteolysisInferred from electronic annotation. Source: Compara |
| Cellular_component | basement membrane Inferred from electronic annotation. Source: Compara |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||||
| Chain | 24 – 211 | 188 | Metalloproteinase inhibitor 3 | PRO_0000034340 | |||||||
Regions | |||||||||||
| Domain | 24 – 143 | 120 | NTR | ||||||||
| Region | 24 – 28 | 5 | Involved in metalloproteinase-binding By similarity | ||||||||
| Region | 88 – 89 | 2 | Involved in metalloproteinase-binding By similarity | ||||||||
| Region | 105 – 188 | 84 | Mediates interaction with EFEMP1 By similarity | ||||||||
Sites | |||||||||||
| Metal binding | 24 | 1 | Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 207 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 24 ↔ 91 | By similarity | |||||||||
| Disulfide bond | 26 ↔ 118 | By similarity | |||||||||
| Disulfide bond | 36 ↔ 143 | By similarity | |||||||||
| Disulfide bond | 145 ↔ 192 | By similarity | |||||||||
| Disulfide bond | 150 ↔ 155 | By similarity | |||||||||
| Disulfide bond | 163 ↔ 184 | By similarity | |||||||||
Sequences
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References
| [1] | "Molecular cloning and sequencing of the cDNA encoding equine tissue inhibitor of metalloproteinase-3 (TIMP-3)." Kyaw-Tanner M.T., Mungall B.A., Pollitt C.C. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ243283 mRNA. Translation: CAB51854.1. |
| RefSeq | NP_001075339.1. NM_001081870.1. |
| UniGene | Eca.12656. |
3D structure databases | |
| ProteinModelPortal | Q9TUL9. |
| SMR | Q9TUL9. Positions 24-144. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9796.ENSECAP00000015840. |
Protein family/group databases | |
| MEROPS | I35.003. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSECAT00000019359; ENSECAP00000015840; ENSECAG00000018314. |
| GeneID | 100033947. |
| KEGG | ecb:100033947. |
Organism-specific databases | |
| CTD | 7078. |
Phylogenomic databases | |
| eggNOG | NOG250837. |
| GeneTree | ENSGT00390000004555. |
| HOGENOM | HOG000285981. |
| HOVERGEN | HBG068749. |
| InParanoid | Q9TUL9. |
| OMA | KEGYCSW. |
| OrthoDB | EOG47D9H3. |
Family and domain databases | |
| InterPro | IPR001134. Netrin_domain. IPR001820. Prot_inh_TIMP. IPR008993. TIMP-like_OB-fold. IPR015612. Tissue_inhib_metalloprotease_3. [Graphical view] |
| PANTHER | PTHR11844. PTHR11844. 1 hit. PTHR11844:SF6. PTHR11844:SF6. 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 | TIMP3_HORSE | ||||||||
| Accession | Primary (citable) accession number: Q9TUL9 | ||||||||
| 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
