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Q5RFL1 (TPP1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Contains 1 peptidase S53 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 195176Removed in mature form By similarity
PRO_0000027382
Chain196 – 564369Tripeptidyl-peptidase 1
PRO_0000027383

Regions

Domain199 – 564366Peptidase S53

Sites

Active site2721Charge relay system By similarity
Active site2761Charge relay system By similarity
Active site4751Charge relay system By similarity
Metal binding5181Calcium By similarity
Metal binding5191Calcium; via carbonyl oxygen By similarity
Metal binding5401Calcium; via carbonyl oxygen By similarity
Metal binding5421Calcium; via carbonyl oxygen By similarity
Metal binding5441Calcium 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 ↔ 527 By similarity
Disulfide bond523 ↔ 538 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RFL1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 381FDB588837B0F1

FASTA56461,238
        10         20         30         40         50         60 
MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNVER 

        70         80         90        100        110        120 
LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ KWLLAAGAQK CHSVITQDFL 

       130        140        150        160        170        180 
TCWLSIRQAE LLLPGAEFHH YVGGPTETHV VRSPHPYQLP QALAPHVDFV GGLHRFPPTS 

       190        200        210        220        230        240 
SLRQHPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL 

       250        260        270        280        290        300 
AQFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 

       310        320        330        340        350        360 
QEPFLQWLML LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR GLTLLFASGD 

       370        380        390        400        410        420 
SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFLEPFLTT NEIVDYISGG GFSNVFPRPS 

       430        440        450        460        470        480 
YQEEAVTKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV 

       490        500        510        520        530        540 
FGGGILSLIN EHRILSGRPP LGFLNPRLYQ QHGAGLFDVT HGCHESCLDE EVEGQGFCSG 

       550        560 
PGWDPVTGWG TPNFPALPKT LLNP 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857144 mRNA. Translation: CAH89446.1.
RefSeqNP_001124619.1. NM_001131147.1.
UniGenePab.9208.

3D structure databases

ProteinModelPortalQ5RFL1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100440001.
KEGGpon:100440001.

Organism-specific databases

CTD1200.

Phylogenomic databases

HOVERGENHBG004449.
InParanoidQ5RFL1.
KOK01279.

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...

Entry information

Entry nameTPP1_PONAB
AccessionPrimary (citable) accession number: Q5RFL1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 57 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