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Protein

Tripeptidyl-peptidase 1

Gene

TPP1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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

Ca2+By similarityNote: Binds 1 Ca2+ 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

  • endopeptidase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • peptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: InterPro
  • serine-type peptidase activity Source: UniProtKB
  • tripeptidyl-peptidase activity Source: UniProtKB

GO - Biological processi

  • bone resorption Source: UniProtKB
  • nervous system development Source: UniProtKB
  • peptide catabolic process Source: UniProtKB
  • proteolysis Source: UniProtKB
Complete GO annotation...

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 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • lysosome Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
Complete GO annotation...

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

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009732.

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.
IPR030400. Sedolisin_dom.
[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

« Hide

        10         20         30         40         50
MRLRTCLLGL LALCVASKCS YSPEPDQQRT LPPGWVSLGR VDSEEELSLT
60 70 80 90 100
FALRQQNVER LSKLVQAVSD PGSPHYGKYL TLEDVAELVR PSPLTFRTVQ
110 120 130 140 150
KWLSAAGARN CHSVTTQDFL TCWLSVRQAE LLLSGAEFHR YVGGPTEIHV
160 170 180 190 200
IRSLRPYQLP KALAPHVDFV GGLHRFPPTS SLRQRPEPQV SGTVGLHLGV
210 220 230 240 250
TPSVIRQRYN LTAQDVGSGT TNNSQACAQF LEQYFHASDL AEFMRLFGGN
260 270 280 290 300
FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES
310 320 330 340 350
QEPFLQWLLL LSNESALPHV HTVSYGDDED SLSSAYIQRV NTEFMKAAAR
360 370 380 390 400
GLTLLFASGD SGAGCWSVSR RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT
410 420 430 440 450
TEIVDYISGG GFSNVFPQPS YQEEAVVQFL SSSPHLPPSS YFNASGRAYP
460 470 480 490 500
DVAALSDGYW VVSNSVPIPW VSGTSASTPV FGGILSLINE HRLLSGLPPL
510 520 530 540 550
GFLNPRLYQQ RGAGLFDVTR GCHESCLNEE VQGQGFCSGP GWDPVTGWGT
560
PNFPALLKAL IKP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF114167 Genomic DNA. Translation: AAD25043.1.
DQ100344 Genomic DNA. Translation: AAZ38727.1.
RefSeqiNP_001013869.1. NM_001013847.1.
UniGeneiCfa.18923.

3D structure databases

ProteinModelPortaliQ9XSB8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000009732.

Protein family/group databases

MEROPSiS53.003.

Proteomic databases

PaxDbiQ9XSB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi485337.
KEGGicfa:485337.

Organism-specific databases

CTDi1200.

Phylogenomic databases

eggNOGiCOG4934.
HOGENOMiHOG000171253.
HOVERGENiHBG004449.
InParanoidiQ9XSB8.
KOiK01279.

Miscellaneous databases

NextBioi20859374.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
IPR030400. Sedolisin_dom.
[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]
ProtoNetiSearch...

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: June 24, 2015
This is version 83 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.