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O89023

- TPP1_MOUSE

UniProt

O89023 - TPP1_MOUSE

Protein

Tripeptidyl-peptidase 1

Gene

Tpp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei271 – 2711Charge relay systemBy similarity
    Active sitei275 – 2751Charge relay systemBy similarity
    Active sitei474 – 4741Charge relay systemBy similarity
    Metal bindingi516 – 5161CalciumBy similarity
    Metal bindingi517 – 5171Calcium; via carbonyl oxygenBy similarity
    Metal bindingi538 – 5381Calcium; via carbonyl oxygenBy similarity
    Metal bindingi540 – 5401Calcium; via carbonyl oxygenBy similarity
    Metal bindingi542 – 5421CalciumBy similarity

    GO - Molecular functioni

    1. endopeptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. peptidase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. serine-type endopeptidase activity Source: InterPro
    6. serine-type peptidase activity Source: UniProtKB
    7. tripeptidyl-peptidase activity Source: UniProtKB

    GO - Biological processi

    1. bone resorption Source: UniProtKB
    2. lysosome organization Source: MGI
    3. nervous system development Source: UniProtKB
    4. neuromuscular process controlling balance Source: MGI
    5. peptide catabolic process Source: UniProtKB
    6. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

    Protein family/group databases

    MEROPSiS53.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tripeptidyl-peptidase 1 (EC:3.4.14.9)
    Short name:
    TPP-1
    Alternative name(s):
    Lysosomal pepstatin-insensitive protease
    Short name:
    LPIC
    Tripeptidyl aminopeptidase
    Tripeptidyl-peptidase I
    Short name:
    TPP-I
    Gene namesi
    Name:Tpp1
    Synonyms:Cln2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1336194. Tpp1.

    Subcellular locationi

    Lysosome. Melanosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB
    2. melanosome Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Propeptidei20 – 194175Removed in mature formBy similarityPRO_0000027378Add
    BLAST
    Chaini195 – 562368Tripeptidyl-peptidase 1PRO_0000027379Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi111 ↔ 122By similarity
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi221 – 2211N-linked (GlcNAc...) (high mannose)1 Publication
    Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi364 ↔ 525By similarity
    Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi521 ↔ 536By similarity

    Post-translational modificationi

    Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity By similarity.By similarity

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiO89023.
    PaxDbiO89023.
    PRIDEiO89023.

    PTM databases

    PhosphoSiteiO89023.

    Expressioni

    Gene expression databases

    ArrayExpressiO89023.
    BgeeiO89023.
    CleanExiMM_TPP1.
    GenevestigatoriO89023.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Pot1Q91WC12EBI-7051084,EBI-7051001

    Protein-protein interaction databases

    BioGridi198754. 2 interactions.
    IntActiO89023. 5 interactions.
    MINTiMINT-3379633.

    Structurei

    3D structure databases

    ProteinModelPortaliO89023.
    SMRiO89023. Positions 20-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini198 – 562365Peptidase S53Add
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S53 domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4934.
    GeneTreeiENSGT00390000008684.
    HOGENOMiHOG000171253.
    HOVERGENiHBG004449.
    InParanoidiO89023.
    KOiK01279.
    OMAiCRVRSAR.
    OrthoDBiEOG7RNJZW.
    PhylomeDBiO89023.
    TreeFamiTF333497.

    Family and domain databases

    Gene3Di3.40.50.200. 1 hit.
    InterProiIPR015366. Peptidase_S53_propep.
    IPR000209. Peptidase_S8/S53_dom.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PfamiPF00082. Peptidase_S8. 1 hit.
    PF09286. Pro-kuma_activ. 1 hit.
    [Graphical view]
    SMARTiSM00944. Pro-kuma_activ. 1 hit.
    [Graphical view]
    SUPFAMiSSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEiPS51695. SEDOLISIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O89023-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLQARLLGL LALVIAGKCT YNPEPDQRWM LPPGWVSLGR VDPEEELSLT    50
    FALKQRNLER LSELVQAVSD PSSPQYGKYL TLEDVAELVQ PSPLTLLTVQ 100
    KWLSAAGARN CDSVTTQDFL TCWLSVRQAE LLLPGAEFHR YVGGPTKTHV 150
    IRSPHPYQLP QALAPHVDFV GGLHRFPPSS PRQRPEPQQV GTVSLHLGVT 200
    PSVLRQRYNL TAKDVGSGTT NNSQACAQFL EQYFHNSDLT EFMRLFGGSF 250
    THQASVAKVV GKQGRGRAGI EASLDVEYLM SAGANISTWV YSSPGRHEAQ 300
    EPFLQWLLLL SNESSLPHVH TVSYGDDEDS LSSIYIQRVN TEFMKAAARG 350
    LTLLFASGDT GAGCWSVSGR HKFRPSFPAS SPYVTTVGGT SFKNPFLITD 400
    EVVDYISGGG FSNVFPRPPY QEEAVAQFLK SSSHLPPSSY FNASGRAYPD 450
    VAALSDGYWV VSNMVPIPWV SGTSASTPVF GGILSLINEH RILNGRPPLG 500
    FLNPRLYQQH GTGLFDVTHG CHESCLNEEV EGQGFCSGPG WDPVTGWGTP 550
    NFPALLKTLL NP 562
    Length:562
    Mass (Da):61,342
    Last modified:December 1, 2000 - v2
    Checksum:i0AF8163EA1A66396
    GO

    Sequence cautioni

    The sequence CAA09863.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → V(PubMed:9989590)Curated
    Sequence conflicti562 – 5621P → LDPFVP(PubMed:9989590)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS21661.1.
    RefSeqiNP_034036.1. NM_009906.5.
    UniGeneiMm.20837.

    Genome annotation databases

    EnsembliENSMUST00000033184; ENSMUSP00000033184; ENSMUSG00000030894.
    GeneIDi12751.
    KEGGimmu:12751.
    UCSCiuc009izg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS21661.1.
    RefSeqi NP_034036.1. NM_009906.5.
    UniGenei Mm.20837.

    3D structure databases

    ProteinModelPortali O89023.
    SMRi O89023. Positions 20-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198754. 2 interactions.
    IntActi O89023. 5 interactions.
    MINTi MINT-3379633.

    Protein family/group databases

    MEROPSi S53.003.

    PTM databases

    PhosphoSitei O89023.

    Proteomic databases

    MaxQBi O89023.
    PaxDbi O89023.
    PRIDEi O89023.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033184 ; ENSMUSP00000033184 ; ENSMUSG00000030894 .
    GeneIDi 12751.
    KEGGi mmu:12751.
    UCSCi uc009izg.1. mouse.

    Organism-specific databases

    CTDi 1200.
    MGIi MGI:1336194. Tpp1.

    Phylogenomic databases

    eggNOGi COG4934.
    GeneTreei ENSGT00390000008684.
    HOGENOMi HOG000171253.
    HOVERGENi HBG004449.
    InParanoidi O89023.
    KOi K01279.
    OMAi CRVRSAR.
    OrthoDBi EOG7RNJZW.
    PhylomeDBi O89023.
    TreeFami TF333497.

    Enzyme and pathway databases

    Reactomei REACT_106572. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    NextBioi 282084.
    PROi O89023.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O89023.
    Bgeei O89023.
    CleanExi MM_TPP1.
    Genevestigatori O89023.

    Family and domain databases

    Gene3Di 3.40.50.200. 1 hit.
    InterProi IPR015366. Peptidase_S53_propep.
    IPR000209. Peptidase_S8/S53_dom.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    Pfami PF00082. Peptidase_S8. 1 hit.
    PF09286. Pro-kuma_activ. 1 hit.
    [Graphical view ]
    SMARTi SM00944. Pro-kuma_activ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEi PS51695. SEDOLISIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiTPP1_MOUSE
    AccessioniPrimary (citable) accession number: O89023
    Secondary accession number(s): Q543Q8, Q9QUS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3