TPP2_BOVIN
ID TPP2_BOVIN Reviewed; 1249 AA.
AC A5PK39;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Tripeptidyl-peptidase 2;
DE Short=TPP-2;
DE EC=3.4.14.10 {ECO:0000250|UniProtKB:P29144};
DE AltName: Full=Tripeptidyl aminopeptidase;
DE AltName: Full=Tripeptidyl-peptidase II;
DE Short=TPP-II;
GN Name=TPP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cytosolic tripeptidyl-peptidase that releases N-terminal
CC tripeptides from polypeptides and is a component of the proteolytic
CC cascade acting downstream of the 26S proteasome in the ubiquitin-
CC proteasome pathway. It plays an important role in intracellular amino
CC acid homeostasis (By similarity). Stimulates adipogenesis (By
CC similarity). {ECO:0000250|UniProtKB:P29144,
CC ECO:0000250|UniProtKB:Q64514}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000250|UniProtKB:P29144};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
CC nucleus in response to gamma-irradiation. {ECO:0000250}.
CC -!- MISCELLANEOUS: The limitation of proteolytic products to tripeptides is
CC achieved by tailoring the size of the substrate-binding cleft: the two
CC negatively charged residues Glu-305 and Glu-331 that are blocking
CC position P4 limit the number of residues that can be accommodated in
CC the binding cleft and thus create a molecular ruler. At the same time,
CC they orient substrates so that the tripeptides are removed exclusively
CC from the N-terminus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC142343; AAI42344.1; -; mRNA.
DR RefSeq; NP_001092504.1; NM_001099034.2.
DR AlphaFoldDB; A5PK39; -.
DR SMR; A5PK39; -.
DR STRING; 9913.ENSBTAP00000035243; -.
DR MEROPS; S08.A56; -.
DR PaxDb; A5PK39; -.
DR PRIDE; A5PK39; -.
DR GeneID; 526052; -.
DR KEGG; bta:526052; -.
DR CTD; 7174; -.
DR eggNOG; KOG1114; Eukaryota.
DR InParanoid; A5PK39; -.
DR OrthoDB; 156304at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 3.40.50.200; -; 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; IPR022229; Peptidase_S8A_TPPII.
DR InterPro; IPR034051; TPP_II_domain.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Serine protease.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29144"
FT CHAIN 2..1249
FT /note="Tripeptidyl-peptidase 2"
FT /id="PRO_0000310394"
FT DOMAIN 9..508
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 998..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 449
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P29144"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64514"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29144"
SQ SEQUENCE 1249 AA; 138361 MW; F1A7C7F2ABBE6B92 CRC64;
MATAATEEPF PFHGLLPKKE TGAAAFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG
KPKIIDIIDT TGSGDVNTAT VVEPKDGEIV GLSGRVLKIP VTWTNPSGRY HIGIKNGYDF
YPKALKERIQ KERKEKIWDP VHRAALAEAC RKQEEFDVAN NCPSQANKLI KEELHSQVEL
LNSFEKKYSD PGPVYDCLVW FDGETWRACI DSSEDGDLSK STVLRNYKEA QEYGSFGAAE
MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNIIYVSSA
GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL
GVSVSAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKAND VNYTVHSVRR
ALENTAVKAD NIEVFAQGHG IIQVDKAYDY LVQNTSFANK LGFTVTVGTN RGIYLRDPVQ
VAAPSDHGVG IEPVFPENTE NSEKISLQLH LALTSNSSWV QCPSHLELMN QCRHVNIRVD
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESTHYDLALT DVHFKPGQIR
RHFIEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLTE
AFPVLGGKAI EFCIARWWAS LSDVNIDYTV SFHGIVCTAP QLNIHSSEGI NRFDVQSSLK
YEDLAPCITL KSWVQTLRPL SAKTKPLGSR DVLPNNRQLY EMILTYNFHQ PKSGEVTPSC
PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
ERLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSNLT LPPKYNQPFF VTSLPDDKIP
KGAGPGCYLT GSLTLSKTEL GKKADVIPVH YYLISPPTKT KNGSKDKEKD SEKEKDLKEE
FTEALRDLKI QWMTKLDSSD IYNELKETYP NYLPLYVARL HQLDAEKERM KRLNEIVEAA
NAVISHIDQT ALAVYIAMKT DPRPDAAIIK NDMDKQKSTL VDALCRKGCA LADHLLQAQD
QDGAVSSDSE GREEEGESTL DSLTETFWET TKWTDLFDNK VLTFAYKHAL VNKMYGRGLK
FATKLVEEKP TKENWKNCIQ LMKLLGWTHC ASFTENWLPI MYPPDYCVF
