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Q9XSB8

- TPP1_CANFA

UniProt

Q9XSB8 - TPP1_CANFA

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Protein

Tripeptidyl-peptidase 1

Gene
TPP1, CLN2
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - 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.

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 system By similarity
Active sitei276 – 2761Charge relay system By similarity
Active sitei475 – 4751Charge relay system By similarity
Metal bindingi517 – 5171Calcium By similarity
Metal bindingi518 – 5181Calcium; via carbonyl oxygen By similarity
Metal bindingi539 – 5391Calcium; via carbonyl oxygen By similarity
Metal bindingi541 – 5411Calcium; via carbonyl oxygen By similarity
Metal bindingi543 – 5431Calcium By 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
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: Unplaced

Subcellular locationi

Lysosome. Melanosome By similarity

GO - Cellular componenti

  1. lysosome Source: UniProtKB
  2. melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarityAdd
BLAST
Propeptidei20 – 195176Removed in mature form By similarityPRO_0000027372Add
BLAST
Chaini196 – 563368Tripeptidyl-peptidase 1PRO_0000027373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 122 By similarity
Glycosylationi210 – 2101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi222 – 2221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi286 – 2861N-linked (GlcNAc...) Reviewed prediction
Glycosylationi313 – 3131N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi365 ↔ 526 By similarity
Glycosylationi443 – 4431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi522 ↔ 537 By similarity

Post-translational modificationi

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

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9XSB8.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9XSB8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini199 – 563365Peptidase S53Add
BLAST

Sequence similaritiesi

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: April 16, 2014
This is version 78 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

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