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Q9XSB8

- TPP1_CANFA

UniProt

Q9XSB8 - TPP1_CANFA

Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. endopeptidase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. peptidase activity Source: UniProtKB
    4. serine-type endopeptidase activity Source: InterPro
    5. serine-type peptidase activity Source: UniProtKB
    6. tripeptidyl-peptidase activity Source: UniProtKB

    GO - Biological processi

    1. bone resorption Source: UniProtKB
    2. nervous system development Source: UniProtKB
    3. peptide catabolic process Source: UniProtKB
    4. 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):
    Lysosomal pepstatin-insensitive protease
    Short name:
    LPIC
    Tripeptidyl aminopeptidase
    Tripeptidyl-peptidase I
    Short name:
    TPP-I
    Gene namesi
    Name:TPP1
    Synonyms:CLN2
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Unplaced

    Subcellular locationi

    Lysosome. Melanosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB
    2. melanosome Source: UniProtKB-SubCell

    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_0000027372Add
    BLAST
    Chaini196 – 563368Tripeptidyl-peptidase 1PRO_0000027373Add
    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

    Proteomic databases

    PaxDbiQ9XSB8.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XSB8.
    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.
    HOGENOMiHOG000171253.
    HOVERGENiHBG004449.
    InParanoidiQ9XSB8.
    KOiK01279.

    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.

    Q9XSB8-1 [UniParc]FASTAAdd to Basket

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    MRLRTCLLGL LALCVASKCS YSPEPDQQRT LPPGWVSLGR VDSEEELSLT    50
    FALRQQNVER LSKLVQAVSD PGSPHYGKYL TLEDVAELVR PSPLTFRTVQ 100
    KWLSAAGARN CHSVTTQDFL TCWLSVRQAE LLLSGAEFHR YVGGPTEIHV 150
    IRSLRPYQLP KALAPHVDFV GGLHRFPPTS SLRQRPEPQV SGTVGLHLGV 200
    TPSVIRQRYN LTAQDVGSGT TNNSQACAQF LEQYFHASDL AEFMRLFGGN 250
    FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES 300
    QEPFLQWLLL LSNESALPHV HTVSYGDDED SLSSAYIQRV NTEFMKAAAR 350
    GLTLLFASGD SGAGCWSVSR RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT 400
    TEIVDYISGG GFSNVFPQPS YQEEAVVQFL SSSPHLPPSS YFNASGRAYP 450
    DVAALSDGYW VVSNSVPIPW VSGTSASTPV FGGILSLINE HRLLSGLPPL 500
    GFLNPRLYQQ RGAGLFDVTR GCHESCLNEE VQGQGFCSGP GWDPVTGWGT 550
    PNFPALLKAL IKP 563
    Length:563
    Mass (Da):61,362
    Last modified:November 1, 1999 - v1
    Checksum:i21465A44C34934F4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti427 – 4271V → A.2 Publications

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114167 Genomic DNA. Translation: AAD25043.1.
    DQ100344 Genomic DNA. Translation: AAZ38727.1.
    RefSeqiNP_001013869.1. NM_001013847.1.
    UniGeneiCfa.18923.

    Genome annotation databases

    GeneIDi485337.
    KEGGicfa:485337.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114167 Genomic DNA. Translation: AAD25043.1 .
    DQ100344 Genomic DNA. Translation: AAZ38727.1 .
    RefSeqi NP_001013869.1. NM_001013847.1.
    UniGenei Cfa.18923.

    3D structure databases

    ProteinModelPortali Q9XSB8.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S53.003.

    Proteomic databases

    PaxDbi Q9XSB8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 485337.
    KEGGi cfa:485337.

    Organism-specific databases

    CTDi 1200.

    Phylogenomic databases

    eggNOGi COG4934.
    HOGENOMi HOG000171253.
    HOVERGENi HBG004449.
    InParanoidi Q9XSB8.
    KOi K01279.

    Miscellaneous databases

    NextBioi 20859374.

    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. "Coding sequence and exon/intron organization of the canine CLN2 gene and its exclusion as the locus for ceroid lipofuscinosis in English setter dogs."
      Liu P.-C., Katz M.L., Siakotos A.N., Grob S.E., Johnson G.S.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Evaluation of the canine TPP1 gene as a candidate for neuronal ceroid lipofuscinosis in Tibetan terrier and Polish Owczarek Nizinny dogs."
      Droegemueller C., Woehlke A., Distl O.
      Anim. Genet. 36:178-179(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-427.
      Strain: Tibetan terrier.
    3. "Coding sequence and exon/intron organization of the canine TTP-1 gene and exclusion of TPP-1 mutations as the cause of hereditary ceroid lipofuscinosis in English Setter and Tibetan Terrier dogs."
      Sanders D.N., Katz M.L., Johnson G.S.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-427.
      Strain: Tibetan terrier.

    Entry informationi

    Entry nameiTPP1_CANFA
    AccessioniPrimary (citable) accession number: Q9XSB8
    Secondary accession number(s): Q45VT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 79 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