| Tag | Content |
|---|
| CPLM ID | CPLM-023345 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tripeptidyl-peptidase 2 |
Protein Synonyms/Alias | TPP-2; Tripeptidyl aminopeptidase; Tripeptidyl-peptidase II; TPP-II; dTPP II |
Gene Name | TppII |
Gene Synonyms/Alias | CG3991 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 217 | FSDLLPSKVRNNIVA | acetylation | [1] | | 1396 | RMYKYVVKLIEEKRT | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala- polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly- polypeptide. |
Sequence Annotation | ACT_SITE 131 131 Charge relay system.
ACT_SITE 359 359 Charge relay system.
ACT_SITE 549 549 Charge relay system.
MOD_RES 1182 1182 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Protease; Reference proteome; Serine protease. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1441 AA |
Protein Sequence | MFNRFRLVHK QLRLYKNFGL LGQKASVGLT LPIISLSRPY MAYMGTERSV VMITAPATKE 60
FAESSERSNS SKKTTNKEQS DKSAESRMAT SGIVESFPTG ALVPKAETGV LNFLQKYPEY 120
DGRDVTIAIF DSGVDPRATG LETLCDGKTV KVIERYDCSG CGDVDMKKKV TPDENGNIKG 180
LSGNSLKLSP ELMALNTDPE KAVRVGLKSF SDLLPSKVRN NIVAQAKLKH WDKPHKTATA 240
NASRKIVEFE SQNPGEASKL PWDKKILKEN LDFELEMLNS YEKVYGDIKT SYDCILFPTA 300
DGWLTIVDTT EQGDLDQALR IGEYSRTHET RNVDDFLSIS VNVHDEGNVL EVVGMSSPHG 360
THVSSIASGN HSSRDVDGVA PNAKIVSMTI GDGRLGSMET GTALVRAMTK VMELCRDGRR 420
IDVINMSYGE HANWSNSGRI GELMNEVVNK YGVVWVASAG NHGPALCTVG TPPDISQPSL 480
IGVGAYVSPQ MMEAEYAMRE KLPGNVYTWT SRDPCIDGGQ GVTVCAPGGA IASVPQFTMS 540
KSQLMNGTSM AAPHVAGAVA LLISGLKQQN IEYSPYSIKR AISVTATKLG YVDPFAQGHG 600
LLNVEKAFEH LTEHRQSKDN MLRFSVRVGN NADKGIHLRQ GVQRNSIDYN VYIEPIFYND 660
KEADPKDKFN FNVRLNLIAS QPWVQCGAFL DLSYGTRSIA VRVDPTGLQP GVHSAVIRAY 720
DTDCVQKGSL FEIPVTVVQP HVLESDQNTP VFEPASSKGD NSVEFQPNTI QRDFILVPER 780
ATWAELRMRI TDPNRGEDIG KFFVHTNQLL PKQSCRKLET MKIVSVGSEN ESIMAFKVKS 840
GRILELCIAK YWSNYGQSHL KYSLRFRGVE AHNPNAYVMH AGRGIHKLEI EALVAEDVQP 900
QLQLKNAEVV LKPTEAKISP LSATRDVIPD GRQVYQNLLA FNLNVAKAAD VSIYAPIFND 960
LLYEAEFESQ MWMLFDANKA LVATGDAHSH TSFTKLDKGE YTIRLQVRHE KRDLLEKISE 1020
ANLVASFKLT SPLTLDFYEN YNQCIVGGRK YVSSPLRLST RVLYIAPITQ ERLTKANLPA 1080
QCAWLSGNLV FPQDEVGRRV AQHPFTYILN PAEKKSHTNG SSNGSSAAGS TATAAAVTTA 1140
NGAKPKAPAT PQAATSVTNP AAGDGISVQN DPPVDSSGSP ASPKKGKANA DDYAESFRDF 1200
QCSQIVKCEL EMAEKIYNDV VAAHPKHLQA NLLLIQNIES NQLKSQLPLT FVNAQKTSPP 1260
EAGESADKQK EDQKKVRSAL ERIVKLADKV IQETDSEALL SYYGLKNDTR ADAAKIKTNM 1320
DKQKNTLIEA LSKKGIAVAK LAVLDDCIKD SLAEINELYT EIIKFVDAND SKAIQFALWH 1380
AYAHGHYGRM YKYVVKLIEE KRTRDHFVEL AAINGALGHE HIRTVINRMM ITAFPSSFRL 1440
F 1441 |
Gene Ontology | GO:0005737; C:cytoplasm; NAS:FlyBase. GO:0005615; C:extracellular space; IBA:RefGenome. GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. GO:0004252; F:serine-type endopeptidase activity; IBA:RefGenome. GO:0008240; F:tripeptidyl-peptidase activity; IDA:UniProtKB. GO:0051260; P:protein homooligomerization; IDA:UniProtKB. GO:0006508; P:proteolysis; IDA:UniProtKB. |
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Pfam | |
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PRINTS | |