| General Information |
| MoonProt ID | 490 |
| First appeared in release | 3.0 |
| Name(s) | Asparaginyl endopeptidase 2 |
| UniProt ID | A0A5P8PC26 (A0A5P8PC26_MOMCO) |
| GO terms | GO:0006508 proteolysis
GO:0008233 peptidase activity
GO:0051603 proteolysis involved in cellular protein catabolic process
GO:0004197 cysteine-type endopeptidase activity
GO:0016787 hydrolase activity |
| Organisms for which functions have been demonstrated | Momordica cochinchinensis (Spiny bitter cucumber) (Muricia cochinchinensis) |
| Sequence length | 493 amino acids |
| FASTA sequence | >tr|A0A5P8PC26|A0A5P8PC26_MOMCO Asparaginyl endopeptidase 2 OS=Momordica cochinchinensis OX=3674 GN=AEP2 PE=2 SV=1
MTRIPAGASLFLFLVLFGLASGGRDLPGDFLRLPSEALKFFHRGASDATGDEDSVGTRWAVLIAGSNGYWNYRHQADICHAYQLLRKGGLKDENIIVFMYDDIAFNPENPRPGVIINHPHGSDVYHGVPKDYTGEDVNVENFFAAILGDKKAIKGGSGKVVDSGPNDHIFIFYSDHGGPGVLGMPTYPYIYADGLIDVLKKKHASGSYKSLVFYLEACESGSIFEGLLPQDLNIYATTASNAVESSWGCYCPGDDTAPPPEYDTCLGDLYSVGWMEDSDRHNLKTESLRQQYELVKKRTLNDYTVYGSHVMQYGDITLNKNALFSYLGTDPANENNTFVESNSLRPTTKVTNQRDADMVHFWEKFRKAPEGSAQKIEAQKHFVEAMSHRVHIDNSVKLIGKLLFGIEKGPEVLNAVRPTGQPLVNNWDCLKNMVRSFETHCGSLSQYGMKHMRSFANLCNAGIRNEQMAEASAQACVSVPSGPWSSLHKGFTA |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | (7-24) signal sequence |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
tr_A0A5P8PC26_A0A5P8PC26 is 493 residues long, with 26 residues (5.27 %) predicted as disordered. The protein has 2 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Asparaginyl endopeptidases (AEPs), N-terminal excision |
| References for function | Du J, Yap K, Chan LY, Rehm FB, Looi FY, Poth AG, Gilding EK, Kaas Q, Durek T, Craik DJ. A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors. Nature communications. 2020 Mar 27;11(1):1-1.
Craik DJ. Circling the enemy: cyclic proteins in plant defence. Trends in plant science. 2009 Jun 1;14(6):328-35. |
| E.C. number | 3.4.22.34 |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | cytoplasm |
| Function 2 |
| Function description | C-terminal cyclization of cyclotide precursors |
| References for function | Du J, Yap K, Chan LY, Rehm FB, Looi FY, Poth AG, Gilding EK, Kaas Q, Durek T, Craik DJ. A bifunctional asparaginyl endopeptidase efficiently catalyzes both cleavage and cyclization of cyclic trypsin inhibitors. Nature communications. 2020 Mar 27;11(1):1-1.
Gruber CW, Anderson MA, Craik DJ. Insecticidal plant cyclotides and related cystine knot toxins. Toxicon. 2007 Mar 15;49(4):561-75. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |