Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O89023

- TPP1_MOUSE

UniProt

O89023 - TPP1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tripeptidyl-peptidase 1

Gene

Tpp1

Organism
Mus musculus (Mouse)
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 (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 sitei271 – 2711Charge relay systemBy similarity
Active sitei275 – 2751Charge relay systemBy similarity
Active sitei474 – 4741Charge relay systemBy similarity
Metal bindingi516 – 5161CalciumBy similarity
Metal bindingi517 – 5171Calcium; via carbonyl oxygenBy similarity
Metal bindingi538 – 5381Calcium; via carbonyl oxygenBy similarity
Metal bindingi540 – 5401Calcium; via carbonyl oxygenBy similarity
Metal bindingi542 – 5421CalciumBy 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. epithelial cell differentiation Source: Ensembl
  3. lysosome organization Source: MGI
  4. nervous system development Source: UniProtKB
  5. neuromuscular process controlling balance Source: MGI
  6. peptide catabolic process Source: UniProtKB
  7. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1336194. Tpp1.

Subcellular locationi

Lysosome. Melanosome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. lysosome Source: UniProtKB
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Propeptidei20 – 194175Removed in mature formBy similarityPRO_0000027378Add
BLAST
Chaini195 – 562368Tripeptidyl-peptidase 1PRO_0000027379Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 122By similarity
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi221 – 2211N-linked (GlcNAc...) (high mannose)1 Publication
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi364 ↔ 525By similarity
Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi521 ↔ 536By 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

MaxQBiO89023.
PaxDbiO89023.
PRIDEiO89023.

PTM databases

PhosphoSiteiO89023.

Expressioni

Gene expression databases

BgeeiO89023.
CleanExiMM_TPP1.
ExpressionAtlasiO89023. baseline and differential.
GenevestigatoriO89023.

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Pot1Q91WC12EBI-7051084,EBI-7051001

Protein-protein interaction databases

BioGridi198754. 2 interactions.
IntActiO89023. 5 interactions.
MINTiMINT-3379633.

Structurei

3D structure databases

ProteinModelPortaliO89023.
SMRiO89023. Positions 20-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 562365Peptidase S53Add
BLAST

Sequence similaritiesi

Contains 1 peptidase S53 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4934.
GeneTreeiENSGT00390000008684.
HOGENOMiHOG000171253.
HOVERGENiHBG004449.
InParanoidiO89023.
KOiK01279.
OMAiCRVRSAR.
OrthoDBiEOG7RNJZW.
PhylomeDBiO89023.
TreeFamiTF333497.

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.

O89023-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGLQARLLGL LALVIAGKCT YNPEPDQRWM LPPGWVSLGR VDPEEELSLT
60 70 80 90 100
FALKQRNLER LSELVQAVSD PSSPQYGKYL TLEDVAELVQ PSPLTLLTVQ
110 120 130 140 150
KWLSAAGARN CDSVTTQDFL TCWLSVRQAE LLLPGAEFHR YVGGPTKTHV
160 170 180 190 200
IRSPHPYQLP QALAPHVDFV GGLHRFPPSS PRQRPEPQQV GTVSLHLGVT
210 220 230 240 250
PSVLRQRYNL TAKDVGSGTT NNSQACAQFL EQYFHNSDLT EFMRLFGGSF
260 270 280 290 300
THQASVAKVV GKQGRGRAGI EASLDVEYLM SAGANISTWV YSSPGRHEAQ
310 320 330 340 350
EPFLQWLLLL SNESSLPHVH TVSYGDDEDS LSSIYIQRVN TEFMKAAARG
360 370 380 390 400
LTLLFASGDT GAGCWSVSGR HKFRPSFPAS SPYVTTVGGT SFKNPFLITD
410 420 430 440 450
EVVDYISGGG FSNVFPRPPY QEEAVAQFLK SSSHLPPSSY FNASGRAYPD
460 470 480 490 500
VAALSDGYWV VSNMVPIPWV SGTSASTPVF GGILSLINEH RILNGRPPLG
510 520 530 540 550
FLNPRLYQQH GTGLFDVTHG CHESCLNEEV EGQGFCSGPG WDPVTGWGTP
560
NFPALLKTLL NP
Length:562
Mass (Da):61,342
Last modified:December 1, 2000 - v2
Checksum:i0AF8163EA1A66396
GO

Sequence cautioni

The sequence CAA09863.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V(PubMed:9989590)Curated
Sequence conflicti562 – 5621P → LDPFVP(PubMed:9989590)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ011912 mRNA. Translation: CAA09863.1. Different initiation.
AF124599 Genomic DNA. Translation: AAD32573.1.
AF111172 mRNA. Translation: AAD03083.1.
AK002418 mRNA. Translation: BAB22085.1.
AK048279 mRNA. Translation: BAC33293.1.
AK170781 mRNA. Translation: BAE42026.1.
BC024820 mRNA. Translation: AAH24820.1.
CCDSiCCDS21661.1.
RefSeqiNP_034036.1. NM_009906.5.
UniGeneiMm.20837.

Genome annotation databases

EnsembliENSMUST00000033184; ENSMUSP00000033184; ENSMUSG00000030894.
GeneIDi12751.
KEGGimmu:12751.
UCSCiuc009izg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ011912 mRNA. Translation: CAA09863.1 . Different initiation.
AF124599 Genomic DNA. Translation: AAD32573.1 .
AF111172 mRNA. Translation: AAD03083.1 .
AK002418 mRNA. Translation: BAB22085.1 .
AK048279 mRNA. Translation: BAC33293.1 .
AK170781 mRNA. Translation: BAE42026.1 .
BC024820 mRNA. Translation: AAH24820.1 .
CCDSi CCDS21661.1.
RefSeqi NP_034036.1. NM_009906.5.
UniGenei Mm.20837.

3D structure databases

ProteinModelPortali O89023.
SMRi O89023. Positions 20-562.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198754. 2 interactions.
IntActi O89023. 5 interactions.
MINTi MINT-3379633.

Protein family/group databases

MEROPSi S53.003.

PTM databases

PhosphoSitei O89023.

Proteomic databases

MaxQBi O89023.
PaxDbi O89023.
PRIDEi O89023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033184 ; ENSMUSP00000033184 ; ENSMUSG00000030894 .
GeneIDi 12751.
KEGGi mmu:12751.
UCSCi uc009izg.1. mouse.

Organism-specific databases

CTDi 1200.
MGIi MGI:1336194. Tpp1.

Phylogenomic databases

eggNOGi COG4934.
GeneTreei ENSGT00390000008684.
HOGENOMi HOG000171253.
HOVERGENi HBG004449.
InParanoidi O89023.
KOi K01279.
OMAi CRVRSAR.
OrthoDBi EOG7RNJZW.
PhylomeDBi O89023.
TreeFami TF333497.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.

Miscellaneous databases

NextBioi 282084.
PROi O89023.
SOURCEi Search...

Gene expression databases

Bgeei O89023.
CleanExi MM_TPP1.
ExpressionAtlasi O89023. baseline and differential.
Genevestigatori O89023.

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

« Hide 'large scale' publications
  1. "Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I."
    Vines D.J., Warburton M.J.
    FEBS Lett. 443:131-135(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Characterization and chromosomal mapping of a mouse ortholog of the late-infantile ceroid-lipofuscinosis gene CLN2."
    Katz M.L., Liu P.-C., Grob-Nunn S.E., Shibuya H., Johnson G.S.
    Mamm. Genome 10:1050-1053(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Murine homologue of the lysosomal pepstatin insensitive protease which is deficient in human classical late infantile neuronal ceroid lipofuscinosis."
    Sleat D.E., Lobel P.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head and Kidney.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Retina.
  6. "High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis."
    Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K., Monde K., Nishimura S.
    Mol. Cell. Proteomics 4:1977-1989(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221.
    Tissue: Epidermis.

Entry informationi

Entry nameiTPP1_MOUSE
AccessioniPrimary (citable) accession number: O89023
Secondary accession number(s): Q543Q8, Q9QUS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 119 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3