Q5IS74 (TPP1_PANTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 49.
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 | Pan troglodytes (Chimpanzee) | ||||
| Taxonomic identifier | 9598 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan |
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_0000027380 | |||||||
| Chain | 196 – 563 | 368 | Tripeptidyl-peptidase 1 | PRO_0000027381 | |||||||
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] | "Accelerated evolution of nervous system genes in the origin of Homo sapiens." Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T. Cell 119:1027-1040(2004) [PubMed: 15620360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY665254 mRNA. Translation: AAV74292.1. |
| RefSeq | NP_001013025.1. NM_001013007.1. |
| UniGene | Ptr.6178. |
3D structure databases | |
| ProteinModelPortal | Q5IS74. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5IS74. |
Protein family/group databases | |
| MEROPS | S53.003. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSPTRT00000006261; ENSPTRP00000005774; ENSPTRG00000003299. ENSPTRT00000006262; ENSPTRP00000005775; ENSPTRG00000003299. |
| GeneID | 450999. |
| KEGG | ptr:450999. |
Organism-specific databases | |
| CTD | 1200. |
Phylogenomic databases | |
| eggNOG | maNOG12815. |
| GeneTree | ENSGT00390000008684. |
| HOVERGEN | HBG004449. |
| OMA | LQWLMLL. |
Family and domain databases | |
| InterPro | IPR015366. Peptidase_S53_propep. IPR000209. Peptidase_S8/S53. IPR009020. Prot_inh_propept. [Graphical view] |
| Gene3D | G3DSA:3.40.50.200. Pept_S8_S53. 1 hit. |
| KO | K01279. |
| 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... |
Entry information
| Entry name | TPP1_PANTR | ||||||||
| Accession | Primary (citable) accession number: Q5IS74 | ||||||||
| 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