Q5RFD6
Gene name |
CPM |
Protein name |
Carboxypeptidase M |
Names |
CPM |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100171502 |
EC number |
3.4.17.12: Metallocarboxypeptidases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5RFD6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RFD6-F1 | Predicted | AlphaFoldDB |
No variants for Q5RFD6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RFD6 | |||||
No associated diseases with Q5RFD6
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.17.12 | Metallocarboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchored component of membrane | The component of a membrane consisting of the gene products that are tethered to the membrane only by a covalently attached anchor, such as a lipid group that is embedded in the membrane. Gene products with peptide sequences that are embedded in the membrane are excluded from this grouping. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metallocarboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDFPCLWLGL | LLPLVAALDF | NYHHQEGMEA | FLKTVAQNYS | SITHLHSIGK | SVKGRNLWVL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVGRFPKEHR | IGIPEFKYVA | NMHGDETVGR | ELLLHLIDYL | VTSDGKDPEI | TNLINSTRIH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IMPSMNPDGF | EAVKKPDCYY | SIGRENYNQY | DLNRNFPDAF | EYNNVSRQPE | TVAVMKWLKT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ETFVLSANLH | GGALVASYPF | DNGVQATGAL | YSRSLTPDDD | VFQYLAHTYA | SRNPNMKKGD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ECKNKMNFPN | GVTNGYSWYP | LQGGMQDYNY | IWAQCFEITL | ELSCCKYPRE | EKLPSFWNNN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KASLIEYIKQ | VHLGVKGQVF | DQNGNPLPDV | IVEVQDRKHI | CPYRTNKYGE | YYLLLLPGSY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IINVTVSGHD | PHLTKVIIPE | KSQNFSALKK | DILLPFQGQL | DSIPVSNPSC | PMIPLYRNLP |
| 430 | 440 | ||||
| DHSAATKPSL | FLFLVSLLHI | FFK |