| General Information |
| MoonProt ID | 500 |
| First appeared in release | 3.0 |
| Name(s) | Asparaginyl endopeptidase 2
Gene: AEP2 |
| UniProt ID | A0A5P8PC26 (A0A5P8PC26_MOMCO) |
| GO terms | GO:0016787 hydrolase activity
GO:0006508 proteolysis
GO:0008233 peptidase 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
MTRIPAGASLFLFLVLFGLASGGRDLPGDFLRLPSEALKFFHRGASDATGDEDSVGTRWA
VLIAGSNGYWNYRHQADICHAYQLLRKGGLKDENIIVFMYDDIAFNPENPRPGVIINHPH
GSDVYHGVPKDYTGEDVNVENFFAAILGDKKAIKGGSGKVVDSGPNDHIFIFYSDHGGPG
VLGMPTYPYIYADGLIDVLKKKHASGSYKSLVFYLEACESGSIFEGLLPQDLNIYATTAS
NAVESSWGCYCPGDDTAPPPEYDTCLGDLYSVGWMEDSDRHNLKTESLRQQYELVKKRTL
NDYTVYGSHVMQYGDITLNKNALFSYLGTDPANENNTFVESNSLRPTTKVTNQRDADMVH
FWEKFRKAPEGSAQKIEAQKHFVEAMSHRVHIDNSVKLIGKLLFGIEKGPEVLNAVRPTG
QPLVNNWDCLKNMVRSFETHCGSLSQYGMKHMRSFANLCNAGIRNEQMAEASAQACVSVP
SGPWSSLHKGFTA |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | (7-24) signal sequence
# tr|A0A5P8PC26|A0A5P8PC26_MOMCO Number of predicted TMHs: 1
# tr|A0A5P8PC26|A0A5P8PC26_MOMCO Exp number of AAs in TMHs: 16.04101
# tr|A0A5P8PC26|A0A5P8PC26_MOMCO Exp number, first 60 AAs: 16.00169
# tr|A0A5P8PC26|A0A5P8PC26_MOMCO Total prob of N-in: 0.85464
# tr|A0A5P8PC26|A0A5P8PC26_MOMCO POSSIBLE N-term signal sequence
tr|A0A5P8PC26|A0A5P8PC26_MOMCO TMHMM2.0 inside 1 6
tr|A0A5P8PC26|A0A5P8PC26_MOMCO TMHMM2.0 TMhelix 7 24
tr|A0A5P8PC26|A0A5P8PC26_MOMCO TMHMM2.0 outside 25 493 |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
trA0A5P8PC26A0A5P8PC26_M 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.
Segment 1 - Short (< 30 residues) disordered segment
Segment is located between positions 337 and 356 in the sequence.
The segment is 20 residues long (4.06 % of the total sequence length).
Segment 2 - Short (< 30 residues) disordered segment
Segment is located between positions 364 and 369 in the sequence.
The segment is 6 residues long (1.22 % of the total sequence length). |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | Asparaginyl endopeptidase |
| References for function | Du J, Yap K, Chan LY, Rehm FBH, 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. Nat Commun. 2020 Mar 27;11(1):1575. doi: 10.1038/s41467-020-15418-2. PMID: 32221295; PMCID: PMC7101308. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | |
| Function 2 |
| Function description | cyclase |
| References for function | Du J, Yap K, Chan LY, Rehm FBH, 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. Nat Commun. 2020 Mar 27;11(1):1575. doi: 10.1038/s41467-020-15418-2. PMID: 32221295; PMCID: PMC7101308. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | |
| Comments | can perform both N-terminal proteolysis and C-terminal cyclization of cyclotide precursors. |