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Q5IS74

- TPP1_PANTR

UniProt

Q5IS74 - TPP1_PANTR

Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      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 sitei272 – 2721Charge relay systemBy similarity
    Active sitei276 – 2761Charge relay systemBy similarity
    Active sitei475 – 4751Charge relay systemBy similarity
    Metal bindingi517 – 5171CalciumBy similarity
    Metal bindingi518 – 5181Calcium; via carbonyl oxygenBy similarity
    Metal bindingi539 – 5391Calcium; via carbonyl oxygenBy similarity
    Metal bindingi541 – 5411Calcium; via carbonyl oxygenBy similarity
    Metal bindingi543 – 5431CalciumBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Calcium, Metal-binding

    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):
    Tripeptidyl aminopeptidase
    Tripeptidyl-peptidase I
    Short name:
    TPP-I
    Gene namesi
    Name:TPP1
    Synonyms:CLN2
    OrganismiPan troglodytes (Chimpanzee)
    Taxonomic identifieri9598 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
    ProteomesiUP000002277: Chromosome 11

    Subcellular locationi

    Lysosome By similarity. Melanosome By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Propeptidei20 – 195176Removed in mature formBy similarityPRO_0000027380Add
    BLAST
    Chaini196 – 563368Tripeptidyl-peptidase 1PRO_0000027381Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi111 ↔ 122By similarity
    Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi313 – 3131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi365 ↔ 526By similarity
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi522 ↔ 537By 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

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9598.ENSPTRP00000054786.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5IS74.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini199 – 563365Peptidase S53Add
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S53 domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4934.
    GeneTreeiENSGT00390000008684.
    HOGENOMiHOG000171253.
    HOVERGENiHBG004449.
    KOiK01279.
    OMAiCRVRSAR.
    OrthoDBiEOG7RNJZW.
    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.

    Q5IS74-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT    50
    FALRQQNVER LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLRTVQ 100
    KWLLAAGARK CHSVITQDFL TCWLSIRQAE LLLPGAEFHH YVGGPTETHV 150
    VRSPHPYQLP QALAPHVDFV GGLHRFPPTS SLRQRPEPQV TGTVGLHLGV 200
    TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN 250
    FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 300
    QEPFLQWLML LSNESALPHV HTVSYGDDED SLSSAYIQRV NTELMKAAAR 350
    GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT 400
    NEIVDYISGG GFSNVFPRPS YQEEAVTKFL SSSPHLPPSS YFNASGRAYP 450
    DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGILSLINE HRILSGRPPL 500
    GFLNPRLYQQ HGAGLFDVTR GCHESCLDEE VEGQGFCSGP GWDPVTGWGT 550
    PNFPALLKTL LNP 563
    Length:563
    Mass (Da):61,295
    Last modified:February 15, 2005 - v1
    Checksum:iF8B1991276E8F361
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY665254 mRNA. Translation: AAV74292.1.
    RefSeqiNP_001013025.1. NM_001013007.1.
    UniGeneiPtr.6178.

    Genome annotation databases

    EnsembliENSPTRT00000006261; ENSPTRP00000005774; ENSPTRG00000003299.
    GeneIDi450999.
    KEGGiptr:450999.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY665254 mRNA. Translation: AAV74292.1 .
    RefSeqi NP_001013025.1. NM_001013007.1.
    UniGenei Ptr.6178.

    3D structure databases

    ProteinModelPortali Q5IS74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9598.ENSPTRP00000054786.

    Protein family/group databases

    MEROPSi S53.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSPTRT00000006261 ; ENSPTRP00000005774 ; ENSPTRG00000003299 .
    GeneIDi 450999.
    KEGGi ptr:450999.

    Organism-specific databases

    CTDi 1200.

    Phylogenomic databases

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

    Miscellaneous databases

    NextBioi 20833675.

    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. "Accelerated evolution of nervous system genes in the origin of Homo sapiens."
      Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.
      Cell 119:1027-1040(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiTPP1_PANTR
    AccessioniPrimary (citable) accession number: Q5IS74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3