Reviewed, UniProtKB/Swiss-Prot O89023 (TPP1_MOUSE)

Names and origin

Protein names

Recommended name:
    Tripeptidyl-peptidase 1
      Short name=TPP-1
    EC=3.4.14.9
Alternative name(s):
    Tripeptidyl-peptidase I
      Short name=TPP-I
    Tripeptidyl aminopeptidase
    Lysosomal pepstatin-insensitive protease
      Short name=LPIC

Gene names

Name:	Tpp1
Synonyms:	Cln2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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.
Subcellular location	Lysosome. Melanosome By similarity.
Post-translational modification	Activated by autocatalytic proteolytical processing upon acidification By similarity.
Sequence similarities	Belongs to the peptidase S53 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	bone resorption Inferred from sequence or structural similarity. Source: UniProtKB lysosome organization Inferred from mutant phenotype. Source: MGI nervous system development Inferred from sequence or structural similarity. Source: UniProtKB neuromuscular process controlling balance Inferred from mutant phenotype. Source: MGI peptide catabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	lysosome Inferred from sequence or structural similarity. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: MGI soluble fraction Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	protein binding Inferred from sequence or structural similarity. Source: UniProtKB serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro tripeptidyl-peptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	By similarity
	Propeptide	20 – 194	175	Removed in mature form By similarity		PRO_0000027378
	Chain	195 – 562	368	Tripeptidyl-peptidase 1		PRO_0000027379
Sites
	Active site	271	1	Charge relay system By similarity
	Active site	275	1	Charge relay system By similarity
	Active site	474	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	209	1	N-linked (GlcNAc...) Potential
	Glycosylation	221	1	N-linked (GlcNAc...) (high mannose) Ref.6
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	312	1	N-linked (GlcNAc...) Potential
	Glycosylation	442	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	1	1	M → V Ref.1
	Sequence conflict	562	1	P → LDPFVP Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O89023-1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 0AF8163EA1A66396	FASTA	562	61,342
	10 20 30 40 50 60 MGLQARLLGL LALVIAGKCT YNPEPDQRWM LPPGWVSLGR VDPEEELSLT FALKQRNLER 70 80 90 100 110 120 LSELVQAVSD PSSPQYGKYL TLEDVAELVQ PSPLTLLTVQ KWLSAAGARN CDSVTTQDFL 130 140 150 160 170 180 TCWLSVRQAE LLLPGAEFHR YVGGPTKTHV IRSPHPYQLP QALAPHVDFV GGLHRFPPSS 190 200 210 220 230 240 PRQRPEPQQV GTVSLHLGVT PSVLRQRYNL TAKDVGSGTT NNSQACAQFL EQYFHNSDLT 250 260 270 280 290 300 EFMRLFGGSF THQASVAKVV GKQGRGRAGI EASLDVEYLM SAGANISTWV YSSPGRHEAQ 310 320 330 340 350 360 EPFLQWLLLL SNESSLPHVH TVSYGDDEDS LSSIYIQRVN TEFMKAAARG LTLLFASGDT 370 380 390 400 410 420 GAGCWSVSGR HKFRPSFPAS SPYVTTVGGT SFKNPFLITD EVVDYISGGG FSNVFPRPPY 430 440 450 460 470 480 QEEAVAQFLK SSSHLPPSSY FNASGRAYPD VAALSDGYWV VSNMVPIPWV SGTSASTPVF 490 500 510 520 530 540 GGILSLINEH RILNGRPPLG FLNPRLYQQH GTGLFDVTHG CHESCLNEEV EGQGFCSGPG 550 560 WDPVTGWGTP NFPALLKTLL NP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9989590] [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: 10556422] [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: 16141072] [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: 15489334] [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: 16170054] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221, MASS SPECTROMETRY. Tissue: Epidermis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00130661.
RefSeq	NP_034036.1.
UniGene	Mm.20837
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O89023.
PTM databases
PhosphoSite	O89023.
Proteomic databases
PRIDE	O89023.
Genome annotation databases
Ensembl	ENSMUST00000033184; ENSMUSP00000033184; ENSMUSG00000030894; Mus musculus. [Genome view]
GeneID	12751.
KEGG	mmu:12751.
UCSC	uc009izg.1. mouse.
Organism-specific databases
CTD	12751.
MGI	MGI:1336194. Tpp1.
Phylogenomic databases
HOGENOM	O89023.
HOVERGEN	O89023.
OMA	SVIRKRY.
Enzyme and pathway databases
BRENDA	3.4.14.9. 244.
Gene expression databases
ArrayExpress	O89023.
Bgee	O89023.
CleanEx	MM_TPP1.
Genevestigator	O89023.
GermOnline	ENSMUSG00000030894. Mus musculus.
Family and domain databases
InterPro	IPR015366. Peptidase_S53_propep. IPR000209. Peptidase_S8/S53. [Graphical view]
Gene3D	G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
Pfam	PF00082. Peptidase_S8. 1 hit. PF09286. Pro-kuma_activ. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	282084.
SOURCE	Search...

Entry information

Entry name

TPP1_MOUSE

Accession

Primary (citable) accession number: O89023
Secondary accession number(s): Q543Q8, Q9QUS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 1, 2000
Last modified:	November 3, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)