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Q0V8B6

- TPP1_BOVIN

UniProt

Q0V8B6 - TPP1_BOVIN

Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      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. serine-type endopeptidase activity Source: InterPro
    4. 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

    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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Lysosome By similarity. 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_0000291586Add
    BLAST
    Chaini196 – 563368Tripeptidyl-peptidase 1PRO_0000291587Add
    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

    PaxDbiQ0V8B6.
    PRIDEiQ0V8B6.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000020469.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0V8B6.
    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.
    InParanoidiQ0V8B6.
    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.

    Q0V8B6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPRSGLLGL FALFVAGKCS YSPEPDQQRR LPPGWVSLGR ADPEEELSLT    50
    FALRQQNVKR LSELVQAVSD PGSPRYGKYL TLEDVAELVR PSPLTLHTVQ 100
    KWLLAAGARN CHSVTTQDFL TCWLSVRQAE LLLSGAEFHH YVGGPAETHA 150
    VRSLHPYRLP KALAPHVDFV GGLHRFPPTS TLRQHPEPQV PGTVGLHLGV 200
    TPSVIRKRYN LTAQDVGSGT TNNSQACAQF LEQYFHDSDL AEFMRLFGGD 250
    FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES 300
    QEPFLQWLLL LSNESALPYV HTVSYGDDED SLSSTYIQRV NTELMKAAAR 350
    GLTLLFASGD SGAGCWSVSG RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT 400
    DEVVDYISGG GFSNVFPRPS YQEEAVTRYL SSSPHLPPSS YFNASGRAYP 450
    DVAALSDGYW VVSNHVPIPW VSGTSASTPV FGGLLSLINE HRILRGLPPL 500
    GFLNPRLYQK HGAGLFDVTR GCHESCLNEE VEGQGFCSGP GWDPVTGWGT 550
    PNFPALLKTL MNP 563
    Length:563
    Mass (Da):61,352
    Last modified:September 5, 2006 - v1
    Checksum:i6D23396D375612C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT026303 mRNA. Translation: ABG81459.1.
    BC119827 mRNA. Translation: AAI19828.1.
    RefSeqiNP_001069186.1. NM_001075718.1.
    UniGeneiBt.35140.

    Genome annotation databases

    GeneIDi515575.
    KEGGibta:515575.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT026303 mRNA. Translation: ABG81459.1 .
    BC119827 mRNA. Translation: AAI19828.1 .
    RefSeqi NP_001069186.1. NM_001075718.1.
    UniGenei Bt.35140.

    3D structure databases

    ProteinModelPortali Q0V8B6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000020469.

    Proteomic databases

    PaxDbi Q0V8B6.
    PRIDEi Q0V8B6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 515575.
    KEGGi bta:515575.

    Organism-specific databases

    CTDi 1200.

    Phylogenomic databases

    eggNOGi COG4934.
    HOGENOMi HOG000171253.
    HOVERGENi HBG004449.
    InParanoidi Q0V8B6.
    KOi K01279.

    Miscellaneous databases

    NextBioi 20871898.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Heart ventricle.

    Entry informationi

    Entry nameiTPP1_BOVIN
    AccessioniPrimary (citable) accession number: Q0V8B6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 54 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