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Q9EQV6

- TPP1_RAT

UniProt

Q9EQV6 - TPP1_RAT

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Protein

Tripeptidyl-peptidase 1

Gene

Tpp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.

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

pH dependencei

Optimum pH is 4. Unstable above pH 7.

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. peptidase activity Source: UniProtKB
  4. peptide binding Source: RGD
  5. serine-type endopeptidase activity Source: InterPro
  6. serine-type peptidase activity Source: UniProtKB
  7. 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):
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase I
Short name:
TPP-I
Gene namesi
Name:Tpp1
Synonyms:Cln2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621296. Tpp1.

Subcellular locationi

Lysosome. Melanosome By similarity

GO - Cellular componenti

  1. lysosome Source: UniProtKB
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 form1 PublicationPRO_0000027384Add
BLAST
Chaini196 – 563368Tripeptidyl-peptidase 1PRO_0000027385Add
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

PaxDbiQ9EQV6.
PRIDEiQ9EQV6.

PTM databases

PhosphoSiteiQ9EQV6.

Expressioni

Gene expression databases

GenevestigatoriQ9EQV6.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9EQV6. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9EQV6.
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.
InParanoidiQ9EQV6.
KOiK01279.
PhylomeDBiQ9EQV6.

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.

Q9EQV6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGLQARFLGL LALVIAGKCT HSPEPDQRWM LPPGWVSLGR VDPEEELSLT
60 70 80 90 100
FALKQQNLDR LSELVQAVSD PSSPRYGKYL TLEDVAELVQ PSPLTLRTVQ
110 120 130 140 150
KWLLAAGARD CHSVTTQDFL TCWLSVRQAE LLLPGAEFHR YVGGPAKTHI
160 170 180 190 200
IRSPHPYQLP QALAPHVDLV AGLHRFPPLS SPRQRPEPQG VGPVGLHLGV
210 220 230 240 250
TPSVLRQRYN LTARDVGSGT TNNSQACAQF LEQYFHNSDL TEFMRLFGSS
260 270 280 290 300
FAHQASVARV VGKQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHEA
310 320 330 340 350
QEPFLQWLLL LSNESSLPHV HTVSYGDDED SLSSVYIQRV NTEFMKAAAR
360 370 380 390 400
GLTLLFASGD TGAGCWSVSG RHKFRPSFPA SSPYVTTVGG TSFKNPFLVT
410 420 430 440 450
NEVVDYISGG GFSNVFPQPS YQEEAVAQFL KSSSHLPPSS YFNASGRAYP
460 470 480 490 500
DVAALSDGYW VVSNMVPIPW VSGTSASTPV FGGILSLINE HRLLNGRPPL
510 520 530 540 550
GFLNPRLYQQ HGAGLFDVTH GCHESCLNEE VEGQGFCSGP GWDPVTGWGT
560
PNFPALLKTL LNP
Length:563
Mass (Da):61,332
Last modified:March 1, 2001 - v1
Checksum:iB54F3C86205DFEC1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101N → A AA sequence (PubMed:9659384)Curated
Sequence conflicti216 – 2172VG → SQ AA sequence (PubMed:9659384)Curated
Sequence conflicti389 – 3913GGT → SPP AA sequence (PubMed:9659384)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB043870 mRNA. Translation: BAB18570.1.
RefSeqiNP_112647.1. NM_031357.1.
UniGeneiRn.162472.

Genome annotation databases

GeneIDi83534.
KEGGirno:83534.
UCSCiRGD:621296. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB043870 mRNA. Translation: BAB18570.1 .
RefSeqi NP_112647.1. NM_031357.1.
UniGenei Rn.162472.

3D structure databases

ProteinModelPortali Q9EQV6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9EQV6. 1 interaction.

Protein family/group databases

MEROPSi S53.003.

PTM databases

PhosphoSitei Q9EQV6.

Proteomic databases

PaxDbi Q9EQV6.
PRIDEi Q9EQV6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 83534.
KEGGi rno:83534.
UCSCi RGD:621296. rat.

Organism-specific databases

CTDi 1200.
RGDi 621296. Tpp1.

Phylogenomic databases

eggNOGi COG4934.
HOGENOMi HOG000171253.
HOVERGENi HBG004449.
InParanoidi Q9EQV6.
KOi K01279.
PhylomeDBi Q9EQV6.

Miscellaneous databases

NextBioi 616037.
PROi Q9EQV6.

Gene expression databases

Genevestigatori Q9EQV6.

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. "Rat tripeptidyl peptidase I: its purification and molecular cloning."
    Du P., Kato S., Li Y., Maeda T., Yamane T., Yamamoto S., Fujiwara M., Yamamoto Y., Nishi K., Ohkubo I.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Purification and characterisation of a tripeptidyl aminopeptidase I from rat spleen."
    Vines D.J., Warburton M.J.
    Biochim. Biophys. Acta 1384:233-242(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 196-217; 374-392 AND 395-429, CHARACTERIZATION.
    Tissue: Spleen.

Entry informationi

Entry nameiTPP1_RAT
AccessioniPrimary (citable) accession number: Q9EQV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 88 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, Direct protein sequencing, 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