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Q9XSB8 (TPP1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tripeptidyl-peptidase 1
Short name=TPP-1
EC=3.4.14.9
Alternative name(s):
Lysosomal pepstatin-insensitive protease
Short name=LPIC
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
Short name=TPP-I
Gene names
Name:TPP1
Synonyms:CLN2
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Lysosome. Melanosome By similarity.

Post-translational modification

Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity By similarity.

Sequence similarities

Belongs to the peptidase S53 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Serine protease
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone resorption

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

lysosome organization

Inferred from electronic annotation. Source: Compara

nervous system development

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Compara

peptide catabolic process

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

proteolysis

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

   Cellular_componentlysosome

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Compara

   Molecular_functionendopeptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

tripeptidyl-peptidase activity

Inferred from sequence or structural similarity PubMed 14609438. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 195176Removed in mature form By similarity
PRO_0000027372
Chain196 – 563368Tripeptidyl-peptidase 1
PRO_0000027373

Sites

Active site2721Charge relay system By similarity
Active site2761Charge relay system By similarity
Active site4751Charge relay system By similarity
Metal binding5171Calcium By similarity
Metal binding5181Calcium; via carbonyl oxygen By similarity
Metal binding5391Calcium; via carbonyl oxygen By similarity
Metal binding5411Calcium; via carbonyl oxygen By similarity
Metal binding5431Calcium By similarity

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3131N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 122 By similarity
Disulfide bond365 ↔ 526 By similarity
Disulfide bond522 ↔ 537 By similarity

Natural variations

Natural variant4271V → A. Ref.2 Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9XSB8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 21465A44C34934F4

FASTA56361,362
        10         20         30         40         50         60 
MRLRTCLLGL LALCVASKCS YSPEPDQQRT LPPGWVSLGR VDSEEELSLT FALRQQNVER 

        70         80         90        100        110        120 
LSKLVQAVSD PGSPHYGKYL TLEDVAELVR PSPLTFRTVQ KWLSAAGARN CHSVTTQDFL 

       130        140        150        160        170        180 
TCWLSVRQAE LLLSGAEFHR YVGGPTEIHV IRSLRPYQLP KALAPHVDFV GGLHRFPPTS 

       190        200        210        220        230        240 
SLRQRPEPQV SGTVGLHLGV TPSVIRQRYN LTAQDVGSGT TNNSQACAQF LEQYFHASDL 

       250        260        270        280        290        300 
AEFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES 

       310        320        330        340        350        360 
QEPFLQWLLL LSNESALPHV HTVSYGDDED SLSSAYIQRV NTEFMKAAAR GLTLLFASGD 

       370        380        390        400        410        420 
SGAGCWSVSR RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT TEIVDYISGG GFSNVFPQPS 

       430        440        450        460        470        480 
YQEEAVVQFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNSVPIPW VSGTSASTPV 

       490        500        510        520        530        540 
FGGILSLINE HRLLSGLPPL GFLNPRLYQQ RGAGLFDVTR GCHESCLNEE VQGQGFCSGP 

       550        560 
GWDPVTGWGT PNFPALLKAL IKP

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF114167 Genomic DNA. Translation: AAD25043.1.
DQ100344 Genomic DNA. Translation: AAZ38727.1.
RefSeqNP_001013869.1. NM_001013847.1.
UniGeneCfa.18923.

3D structure databases

ProteinModelPortalQ9XSB8.
ModBaseSearch...

Protein family/group databases

MEROPSS53.003.

Proteomic databases

PaxDbQ9XSB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID485337.
KEGGcfa:485337.

Organism-specific databases

CTD1200.

Phylogenomic databases

eggNOGCOG4934.
HOGENOMHOG000171253.
HOVERGENHBG004449.
InParanoidQ9XSB8.
KOK01279.
OrthoDBEOG42Z4PZ.

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMSSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 1 hit.
ProtoNetSearch...

Other

NextBio20859374.

Entry information

Entry nameTPP1_CANFA
AccessionPrimary (citable) accession number: Q9XSB8
Secondary accession number(s): Q45VT9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: November 1, 1999
Last modified: April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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