Q0V8B6 (TPP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 50.
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: Tripeptidyl-peptidase 1 Short name=TPP-1 EC=3.4.14.9 Alternative name(s): Tripeptidyl aminopeptidase Tripeptidyl-peptidase I Short name=TPP-I | ||||
| 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 | 563 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 | Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus By similarity. |
| Catalytic activity | Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity. |
| Cofactor | Binds 1 calcium ion per subunit By similarity. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Lysosome By similarity. Melanosome By similarity. |
| Post-translational modification | Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity By similarity. |
| Sequence similarities | Belongs to the peptidase S53 family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | By similarity | ||||||||
| Propeptide | 20 – 195 | 176 | Removed in mature form By similarity | PRO_0000291586 | |||||||
| Chain | 196 – 563 | 368 | Tripeptidyl-peptidase 1 | PRO_0000291587 | |||||||
Sites | |||||||||||
| Active site | 272 | 1 | Charge relay system By similarity | ||||||||
| Active site | 276 | 1 | Charge relay system By similarity | ||||||||
| Active site | 475 | 1 | Charge relay system By similarity | ||||||||
| Metal binding | 517 | 1 | Calcium By similarity | ||||||||
| Metal binding | 518 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 539 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 541 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 543 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 210 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 222 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 286 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 313 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 443 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 111 ↔ 122 | By similarity | |||||||||
| Disulfide bond | 365 ↔ 526 | By similarity | |||||||||
| Disulfide bond | 522 ↔ 537 | By similarity | |||||||||
Sequences
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References
| [1] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Heart ventricle. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT026303 mRNA. Translation: ABG81459.1. BC119827 mRNA. Translation: AAI19828.1. |
| IPI | IPI00721428. |
| RefSeq | NP_001069186.1. NM_001075718.1. |
| UniGene | Bt.35140. |
3D structure databases | |
| ProteinModelPortal | Q0V8B6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000020469. |
Proteomic databases | |
| PaxDb | Q0V8B6. |
| PRIDE | Q0V8B6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 515575. |
| KEGG | bta:515575. |
Organism-specific databases | |
| CTD | 1200. |
Phylogenomic databases | |
| eggNOG | COG4934. |
| HOGENOM | HOG000171253. |
| HOVERGEN | HBG004449. |
| InParanoid | Q0V8B6. |
| KO | K01279. |
| OrthoDB | EOG42Z4PZ. |
Family and domain databases | |
| Gene3D | 3.40.50.200. 1 hit. |
| InterPro | IPR015366. Peptidase_S53_propep. IPR000209. Peptidase_S8/S53_dom. IPR009020. Prot_inh_propept. [Graphical view] |
| Pfam | PF00082. Peptidase_S8. 1 hit. PF09286. Pro-kuma_activ. 1 hit. [Graphical view] |
| SMART | SM00944. Pro-kuma_activ. 1 hit. [Graphical view] |
| SUPFAM | SSF52743. Pept_S8_S53. 1 hit. SSF54897. Prot_inh_propept. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 20871898. |
Entry information
| Entry name | TPP1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0V8B6 | ||||||||
| Entry history |
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| 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
