Q55CT0 (TPP1_DICDI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 54.
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 | Dictyostelium discoideum (Slime mold) [Reference proteome] | ||||
| Taxonomic identifier | 44689 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium![]() |
Protein attributes
| Sequence length | 600 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Serine protease with tripeptidyl-peptidase I activity 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 | Secreted Potential. |
| 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
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Autocatalytic cleavage Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from sequence or structural similarity. Source: dictyBase |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro tripeptidyl-peptidase activityInferred from sequence or structural similarity. Source: dictyBase |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Propeptide | 23 – 220 | 198 | Removed in mature form By similarity | PRO_0000327570 | |||||||
| Chain | 221 – 600 | 380 | Tripeptidyl-peptidase 1 | PRO_0000327571 | |||||||
Sites | |||||||||||
| Active site | 318 | 1 | Charge relay system By similarity | ||||||||
| Active site | 322 | 1 | Charge relay system By similarity | ||||||||
| Active site | 514 | 1 | Charge relay system By similarity | ||||||||
| Metal binding | 559 | 1 | Calcium By similarity | ||||||||
| Metal binding | 560 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 579 | 1 | Calcium; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 581 | 1 | Calcium By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 91 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 259 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 266 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 475 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 483 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 411 ↔ 570 | By similarity | |||||||||
Sequences
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References
| [1] | "The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. Kuspa A.Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAFI02000005 Genomic DNA. Translation: EAL72307.1. |
| RefSeq | XP_646401.1. XM_641309.1. |
3D structure databases | |
| ProteinModelPortal | Q55CT0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblProtists | DDB0234303; DDB0234303; DDB_G0269914. |
| GeneID | 8617356. |
| KEGG | ddi:DDB_G0269914. |
Organism-specific databases | |
| dictyBase | DDB_G0269914. tpp1. |
Phylogenomic databases | |
| eggNOG | COG4934. |
| KO | K01279. |
| OMA | YIMAMAP. |
| ProtClustDB | CLSZ2429688. |
Family and domain databases | |
| Gene3D | 3.40.50.200. 1 hit. |
| InterPro | IPR015366. Peptidase_S53_propep. IPR000209. Peptidase_S8/S53_dom. IPR023828. Peptidase_S8_Ser-AS. 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... |
Entry information
| Entry name | TPP1_DICDI | ||||||||
| Accession | Primary (citable) accession number: Q55CT0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Dictyostelium discoideum Dictyostelium discoideum: entries, gene names and cross-references to dictyBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
