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Q5RFL1

- TPP1_PONAB

UniProt

Q5RFL1 - TPP1_PONAB

Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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 bindingi518 – 5181CalciumBy similarity
    Metal bindingi519 – 5191Calcium; via carbonyl oxygenBy similarity
    Metal bindingi540 – 5401Calcium; via carbonyl oxygenBy similarity
    Metal bindingi542 – 5421Calcium; via carbonyl oxygenBy similarity
    Metal bindingi544 – 5441CalciumBy 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

    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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: 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_0000027382Add
    BLAST
    Chaini196 – 564369Tripeptidyl-peptidase 1PRO_0000027383Add
    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 ↔ 527By similarity
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi523 ↔ 538By 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

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RFL1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini199 – 564366Peptidase S53Add
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S53 domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG004449.
    InParanoidiQ5RFL1.
    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.

    Q5RFL1-1 [UniParc]FASTAAdd to Basket

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    MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT    50
    FALRQQNVER LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ 100
    KWLLAAGAQK CHSVITQDFL TCWLSIRQAE LLLPGAEFHH YVGGPTETHV 150
    VRSPHPYQLP QALAPHVDFV GGLHRFPPTS SLRQHPEPQV TGTVGLHLGV 200
    TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN 250
    FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG 300
    QEPFLQWLML LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR 350
    GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFLEPFLTT 400
    NEIVDYISGG GFSNVFPRPS YQEEAVTKFL SSSPHLPPSS YFNASGRAYP 450
    DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGGILSLIN EHRILSGRPP 500
    LGFLNPRLYQ QHGAGLFDVT HGCHESCLDE EVEGQGFCSG PGWDPVTGWG 550
    TPNFPALPKT LLNP 564
    Length:564
    Mass (Da):61,238
    Last modified:December 21, 2004 - v1
    Checksum:i381FDB588837B0F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857144 mRNA. Translation: CAH89446.1.
    RefSeqiNP_001124619.1. NM_001131147.1.
    UniGeneiPab.9208.

    Genome annotation databases

    GeneIDi100440001.
    KEGGipon:100440001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857144 mRNA. Translation: CAH89446.1 .
    RefSeqi NP_001124619.1. NM_001131147.1.
    UniGenei Pab.9208.

    3D structure databases

    ProteinModelPortali Q5RFL1.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100440001.
    KEGGi pon:100440001.

    Organism-specific databases

    CTDi 1200.

    Phylogenomic databases

    HOVERGENi HBG004449.
    InParanoidi Q5RFL1.
    KOi K01279.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiTPP1_PONAB
    AccessioniPrimary (citable) accession number: Q5RFL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 58 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