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Q9EQV6 (TPP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:Tpp1
Synonyms:Cln2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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. 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

Contains 1 peptidase S53 domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 4. Unstable above pH 7.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

nervous system development

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

peptide catabolic process

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

proteolysis

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

   Cellular_componentlysosome

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendopeptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

peptide binding

Inferred from direct assay PubMed 10679303. Source: RGD

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type peptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

tripeptidyl-peptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 195176Removed in mature form
PRO_0000027384
Chain196 – 563368Tripeptidyl-peptidase 1
PRO_0000027385

Regions

Domain199 – 563365Peptidase S53

Sites

Active site2721Charge relay system By similarity
Active site2761Charge relay system By similarity
Active site4751Charge relay system By similarity
Metal binding5171Calcium By similarity
Metal binding5181Calcium; via carbonyl oxygen By similarity
Metal binding5391Calcium; via carbonyl oxygen By similarity
Metal binding5411Calcium; via carbonyl oxygen By similarity
Metal binding5431Calcium By similarity

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 122 By similarity
Disulfide bond365 ↔ 526 By similarity
Disulfide bond522 ↔ 537 By similarity

Experimental info

Sequence conflict2101N → A AA sequence Ref.2
Sequence conflict216 – 2172VG → SQ AA sequence Ref.2
Sequence conflict389 – 3913GGT → SPP AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9EQV6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: B54F3C86205DFEC1

FASTA56361,332
        10         20         30         40         50         60 
MGLQARFLGL LALVIAGKCT HSPEPDQRWM LPPGWVSLGR VDPEEELSLT FALKQQNLDR 

        70         80         90        100        110        120 
LSELVQAVSD PSSPRYGKYL TLEDVAELVQ PSPLTLRTVQ KWLLAAGARD CHSVTTQDFL 

       130        140        150        160        170        180 
TCWLSVRQAE LLLPGAEFHR YVGGPAKTHI IRSPHPYQLP QALAPHVDLV AGLHRFPPLS 

       190        200        210        220        230        240 
SPRQRPEPQG VGPVGLHLGV TPSVLRQRYN LTARDVGSGT TNNSQACAQF LEQYFHNSDL 

       250        260        270        280        290        300 
TEFMRLFGSS FAHQASVARV VGKQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHEA 

       310        320        330        340        350        360 
QEPFLQWLLL LSNESSLPHV HTVSYGDDED SLSSVYIQRV NTEFMKAAAR GLTLLFASGD 

       370        380        390        400        410        420 
TGAGCWSVSG RHKFRPSFPA SSPYVTTVGG TSFKNPFLVT NEVVDYISGG GFSNVFPQPS 

       430        440        450        460        470        480 
YQEEAVAQFL KSSSHLPPSS YFNASGRAYP DVAALSDGYW VVSNMVPIPW VSGTSASTPV 

       490        500        510        520        530        540 
FGGILSLINE HRLLNGRPPL GFLNPRLYQQ HGAGLFDVTH GCHESCLNEE VEGQGFCSGP 

       550        560 
GWDPVTGWGT PNFPALLKTL LNP 

« Hide

References

[1]"Rat tripeptidyl peptidase I: its purification and molecular cloning."
Du P., Kato S., Li Y., Maeda T., Yamane T., Yamamoto S., Fujiwara M., Yamamoto Y., Nishi K., Ohkubo I.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen."
Vines D.J., Warburton M.J.
Biochim. Biophys. Acta 1384:233-242(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 196-217; 374-392 AND 395-429, CHARACTERIZATION.
Tissue: Spleen.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB043870 mRNA. Translation: BAB18570.1.
RefSeqNP_112647.1. NM_031357.1.
UniGeneRn.162472.

3D structure databases

ProteinModelPortalQ9EQV6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9EQV6. 1 interaction.

Protein family/group databases

MEROPSS53.003.

PTM databases

PhosphoSiteQ9EQV6.

Proteomic databases

PaxDbQ9EQV6.
PRIDEQ9EQV6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83534.
KEGGrno:83534.
UCSCRGD:621296. rat.

Organism-specific databases

CTD1200.
RGD621296. Tpp1.

Phylogenomic databases

eggNOGCOG4934.
HOGENOMHOG000171253.
HOVERGENHBG004449.
InParanoidQ9EQV6.
KOK01279.
PhylomeDBQ9EQV6.

Gene expression databases

GenevestigatorQ9EQV6.

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEPS51695. SEDOLISIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616037.
PROQ9EQV6.

Entry information

Entry nameTPP1_RAT
AccessionPrimary (citable) accession number: Q9EQV6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries