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Database: UniProt
Entry: Q3TW28_MOUSE
LinkDB: Q3TW28_MOUSE
Original site: Q3TW28_MOUSE 
ID   Q3TW28_MOUSE            Unreviewed;      1249 AA.
AC   Q3TW28;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE            EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE   AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
GN   Name=Tpp2 {ECO:0000313|MGI:MGI:102724};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE35439.1};
RN   [1] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE35439.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35439.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC         EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   EMBL; AK159865; BAE35439.1; -; mRNA.
DR   AlphaFoldDB; Q3TW28; -.
DR   MEROPS; S08.A56; -.
DR   SwissPalm; Q3TW28; -.
DR   PeptideAtlas; Q3TW28; -.
DR   AGR; MGI:102724; -.
DR   MGI; MGI:102724; Tpp2.
DR   ChiTaRS; Tpp2; mouse.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR   Gene3D; 1.25.40.710; -; 1.
DR   Gene3D; 2.60.40.3170; -; 1.
DR   Gene3D; 6.10.250.3080; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034051; TPP_II_domain.
DR   InterPro; IPR022232; TPPII_C_art.
DR   InterPro; IPR046939; TPPII_C_sf.
DR   InterPro; IPR048384; TPPII_GBD.
DR   InterPro; IPR048383; TPPII_Ig-like-1.
DR   InterPro; IPR022229; TPPII_Ig-like-2.
DR   InterPro; IPR046940; TPPII_Ig-like_sf.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF12580; TPPII; 1.
DR   Pfam; PF12583; TPPII_C; 1.
DR   Pfam; PF21316; TPPII_GBD; 1.
DR   Pfam; PF21223; TPPII_Ig-like-1; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          35..500
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          522..634
FT                   /note="Tripeptidyl-peptidase II first Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF21223"
FT   DOMAIN          654..741
FT                   /note="Tripeptidyl-peptidase II galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21316"
FT   DOMAIN          777..963
FT                   /note="Tripeptidyl peptidase II second Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF12580"
FT   DOMAIN          1010..1069
FT                   /note="Tripeptidyl peptidase II C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12583"
FT   ACT_SITE        44
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        264
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        449
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1249 AA;  138464 MW;  33E744E929DAD888 CRC64;
     MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG
     EPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP ANWTNPLGKY HIGIKNGYDF
     YPKALKERIQ KERKEKIWDP IHRVALAEAC RKQEEFDIAN NGSSQANKLI KEELQSQVEL
     LNSFEKKYSD PGPVYDCLVW HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE
     MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
     LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNTIYVSSA
     GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL
     GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKANN VDYTVHSVRR
     ALENTAIKAD NIEVFAQGHG IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ
     VAAPSDHGVG IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD
     PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT DVHFKPGQIR
     RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLIE
     AFPVLGGKAI EFCIARWWAS LSDVNIDYTI SFHGIVCTAP QLNIHASEGI NRFDVQSSLK
     YEDLAPCITL KSWVQTLRPV NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC
     PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
     DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF VTSLPDDKIP
     KGAGPGCYLA GSLTLSKTEL GKKADVIPVH YYLIPPPTKI KNGSKDKEKD SEKEKDLKEE
     FTEALRDLKI QWMTKLDSTD IYNELKETYP AYLPLYVARL HQLDAEKERM KRLNEIVDAA
     NAVISHIDQT ALAVYIAMKT DPRPDAATIK NDMDKQKSTL IDALCRKGCA LADHLLHTQP
     HDGAAAGDAE AKEEEGESTM ESLSETYWET TKWTDLFDTK VLIFAYKHAL VNKMYGRGLK
     FATKLVEEKP TKENWKNCIQ LMKLLGWTHC ASFTENWLPI MYPPDYCVF
//
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