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Q60HH1 (TPP1_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 50. 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
ORF Names:QccE-12010, QtrA-16970
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length563 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 caution

The sequence BAD51944.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 195176Removed in mature form By similarity
PRO_0000027376
Chain196 – 563368Tripeptidyl-peptidase 1
PRO_0000027377

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 conflict4251A → V in BAC20587. Ref.1
Sequence conflict4631S → N in BAC20587. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60HH1 [UniParc].

Last modified March 15, 2005. Version 2.
Checksum: FCB1014BB43CABA2

FASTA56361,245
        10         20         30         40         50         60 
MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNLER 

        70         80         90        100        110        120 
LSELVQAVSD PNSPQYGKYL TLENVADLVR PSPLTLHMVQ KWLLAAGAQK CHSVITQDFL 

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

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

       250        260        270        280        290        300 
AQFMRLFGGN FAHQASVTRV 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 TSFQEPFLIT NEIVDYISGG GFSNVFPRPS 

       430        440        450        460        470        480 
YQEEAVAKFL SSSPHLPPSG YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV 

       490        500        510        520        530        540 
FGGLLSLINE HRILSGRPPL GFLNPRLYQQ HGAGLFDVTH GCHASCLDEE VEGQGFCSGP 

       550        560 
GWDPVTGWGT PNFPALLKTL LNP 

« Hide

References

[1]"Isolation and characterization of cDNA for macaque neurological disease genes."
Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex and Temporal cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB083308 mRNA. Translation: BAC20587.1.
AB125156 mRNA. Translation: BAD51944.1. Different initiation.
UniGeneMfa.726.

3D structure databases

ProteinModelPortalQ60HH1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS53.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG004449.

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_MACFA
AccessionPrimary (citable) accession number: Q60HH1
Secondary accession number(s): Q8HXY1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 50 of the entry and version 2 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