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O89023 (TPP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Lysosomal pepstatin-insensitive protease
Short name=LPIC
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
Short name=TPP-I
Gene names
Name:Tpp1
Synonyms:Cln2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length562 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 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. 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 CAA09863.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

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

lysosome organization

Inferred from mutant phenotype PubMed 15483130. Source: MGI

nervous system development

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

neuromuscular process controlling balance

Inferred from mutant phenotype PubMed 15483130. Source: MGI

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

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

   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

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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pot1Q91WC12EBI-7051084,EBI-7051001

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 194175Removed in mature form By similarity
PRO_0000027378
Chain195 – 562368Tripeptidyl-peptidase 1
PRO_0000027379

Regions

Domain198 – 562365Peptidase S53

Sites

Active site2711Charge relay system By similarity
Active site2751Charge relay system By similarity
Active site4741Charge relay system By similarity
Metal binding5161Calcium By similarity
Metal binding5171Calcium; via carbonyl oxygen By similarity
Metal binding5381Calcium; via carbonyl oxygen By similarity
Metal binding5401Calcium; via carbonyl oxygen By similarity
Metal binding5421Calcium By similarity

Amino acid modifications

Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2211N-linked (GlcNAc...) (high mannose) Ref.6
Glycosylation2851N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation4421N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 122 By similarity
Disulfide bond364 ↔ 525 By similarity
Disulfide bond521 ↔ 536 By similarity

Experimental info

Sequence conflict11M → V Ref.1
Sequence conflict5621P → LDPFVP Ref.1

Sequences

Sequence LengthMass (Da)Tools
O89023 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 0AF8163EA1A66396

FASTA56261,342
        10         20         30         40         50         60 
MGLQARLLGL LALVIAGKCT YNPEPDQRWM LPPGWVSLGR VDPEEELSLT FALKQRNLER 

        70         80         90        100        110        120 
LSELVQAVSD PSSPQYGKYL TLEDVAELVQ PSPLTLLTVQ KWLSAAGARN CDSVTTQDFL 

       130        140        150        160        170        180 
TCWLSVRQAE LLLPGAEFHR YVGGPTKTHV IRSPHPYQLP QALAPHVDFV GGLHRFPPSS 

       190        200        210        220        230        240 
PRQRPEPQQV GTVSLHLGVT PSVLRQRYNL TAKDVGSGTT NNSQACAQFL EQYFHNSDLT 

       250        260        270        280        290        300 
EFMRLFGGSF THQASVAKVV GKQGRGRAGI EASLDVEYLM SAGANISTWV YSSPGRHEAQ 

       310        320        330        340        350        360 
EPFLQWLLLL SNESSLPHVH TVSYGDDEDS LSSIYIQRVN TEFMKAAARG LTLLFASGDT 

       370        380        390        400        410        420 
GAGCWSVSGR HKFRPSFPAS SPYVTTVGGT SFKNPFLITD EVVDYISGGG FSNVFPRPPY 

       430        440        450        460        470        480 
QEEAVAQFLK SSSHLPPSSY FNASGRAYPD VAALSDGYWV VSNMVPIPWV SGTSASTPVF 

       490        500        510        520        530        540 
GGILSLINEH RILNGRPPLG FLNPRLYQQH GTGLFDVTHG CHESCLNEEV EGQGFCSGPG 

       550        560 
WDPVTGWGTP NFPALLKTLL NP 

« Hide

References

« Hide 'large scale' references
[1]"Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I."
Vines D.J., Warburton M.J.
FEBS Lett. 443:131-135(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Characterization and chromosomal mapping of a mouse ortholog of the late-infantile ceroid-lipofuscinosis gene CLN2."
Katz M.L., Liu P.-C., Grob-Nunn S.E., Shibuya H., Johnson G.S.
Mamm. Genome 10:1050-1053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Murine homologue of the lysosomal pepstatin insensitive protease which is deficient in human classical late infantile neuronal ceroid lipofuscinosis."
Sleat D.E., Lobel P.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Head and Kidney.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Retina.
[6]"High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
Tissue: Epidermis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ011912 mRNA. Translation: CAA09863.1. Different initiation.
AF124599 Genomic DNA. Translation: AAD32573.1.
AF111172 mRNA. Translation: AAD03083.1.
AK002418 mRNA. Translation: BAB22085.1.
AK048279 mRNA. Translation: BAC33293.1.
AK170781 mRNA. Translation: BAE42026.1.
BC024820 mRNA. Translation: AAH24820.1.
RefSeqNP_034036.1. NM_009906.5.
UniGeneMm.20837.

3D structure databases

ProteinModelPortalO89023.
SMRO89023. Positions 20-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198754. 2 interactions.
IntActO89023. 5 interactions.
MINTMINT-3379633.

Protein family/group databases

MEROPSS53.003.

PTM databases

PhosphoSiteO89023.

Proteomic databases

PaxDbO89023.
PRIDEO89023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033184; ENSMUSP00000033184; ENSMUSG00000030894.
GeneID12751.
KEGGmmu:12751.
UCSCuc009izg.1. mouse.

Organism-specific databases

CTD1200.
MGIMGI:1336194. Tpp1.

Phylogenomic databases

eggNOGCOG4934.
GeneTreeENSGT00390000008684.
HOGENOMHOG000171253.
HOVERGENHBG004449.
InParanoidO89023.
KOK01279.
OMAGNFAHQA.
OrthoDBEOG7RNJZW.
PhylomeDBO89023.
TreeFamTF333497.

Gene expression databases

ArrayExpressO89023.
BgeeO89023.
CleanExMM_TPP1.
GenevestigatorO89023.

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

NextBio282084.
PROO89023.
SOURCESearch...

Entry information

Entry nameTPP1_MOUSE
AccessionPrimary (citable) accession number: O89023
Secondary accession number(s): Q543Q8, Q9QUS7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 113 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot