Q9EQV8
Gene name |
Cpn1 |
Protein name |
Carboxypeptidase N catalytic chain |
Names |
CPN, Carboxypeptidase N polypeptide 1, Carboxypeptidase N small subunit |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:365466 |
EC number |
3.4.17.3: 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 Q9EQV8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9EQV8-F1 | Predicted | AlphaFoldDB |
No variants for Q9EQV8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9EQV8 | |||||
No associated diseases with Q9EQV8
1 regional properties for Q9EQV8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Peptidase M14, carboxypeptidase A | 25 - 436 | IPR000834 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.17.3 | Metallocarboxypeptidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| carboxypeptidase activity | Catalysis of the hydrolysis of a single C-terminal amino acid residue from a polypeptide chain. |
| 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). |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| bradykinin catabolic process | The chemical reactions and pathways resulting in the breakdown of the peptide bradykinin. |
| peptide metabolic process | The chemical reactions and pathways involving peptides, compounds of two or more amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. |
| protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
| protein processing | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
| response to glucocorticoid | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucocorticoid stimulus. Glucocorticoids are hormonal C21 corticosteroids synthesized from cholesterol with the ability to bind with the cortisol receptor and trigger similar effects. Glucocorticoids act primarily on carbohydrate and protein metabolism, and have anti-inflammatory effects. |
16 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P04836 | CPE | Carboxypeptidase E | Bos taurus (Bovine) | PR |
| Q2KJ83 | CPN1 | Carboxypeptidase N catalytic chain | Bos taurus (Bovine) | PR |
| Q8QGP3 | CPZ | Carboxypeptidase Z | Gallus gallus (Chicken) | PR |
| Q8IUX7 | AEBP1 | Adipocyte enhancer-binding protein 1 | Homo sapiens (Human) | PR |
| O75976 | CPD | Carboxypeptidase D | Homo sapiens (Human) | PR |
| Q8N436 | CPXM2 | Inactive carboxypeptidase-like protein X2 | Homo sapiens (Human) | PR |
| Q66K79 | CPZ | Carboxypeptidase Z | Homo sapiens (Human) | PR |
| Q96SM3 | CPXM1 | Probable carboxypeptidase X1 | Homo sapiens (Human) | PR |
| P14384 | CPM | Carboxypeptidase M | Homo sapiens (Human) | PR |
| Q80V42 | Cpm | Carboxypeptidase M | Mus musculus (Mouse) | PR |
| O89001 | Cpd | Carboxypeptidase D | Mus musculus (Mouse) | PR |
| Q9Z100 | Cpxm1 | Probable carboxypeptidase X1 | Mus musculus (Mouse) | PR |
| Q9D2L5 | Cpxm2 | Inactive carboxypeptidase-like protein X2 | Mus musculus (Mouse) | PR |
| Q640N1 | Aebp1 | Adipocyte enhancer-binding protein 1 | Mus musculus (Mouse) | PR |
| Q9JJN5 | Cpn1 | Carboxypeptidase N catalytic chain | Mus musculus (Mouse) | PR |
| A2RUV9 | Aebp1 | Adipocyte enhancer-binding protein 1 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPDLPSAFLP | LLLLSKFVTP | VTFRHHRYDD | LVRTLYKVHN | QCPDITRLYN | IGRSVKGRYL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YVLEFSDYPG | THEPLEPEVK | YVGNMHGNEV | LGRELLLQLS | EFLCEEFRNR | NQRILRLIQD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TRIHILPSMN | PDGYEVAAAQ | GPNTSGYLVG | RNNANGVDLN | RNFPDLNTYF | YYNSKYGGPN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HHLPLPDNWK | SQVEPETRAV | IQWIRSLNFV | LSANMHGGAV | VANYPYDKSL | EHRFRSPHRT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SNSPTPDDEL | FQTLAKVYSY | AHGWMHQGWN | CGDYFPDGIT | NGASWYSLSK | GMQDFNYLHT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NCFEITLELS | CNKFPRQEEL | QREWLGNREA | LIQFLEQVHQ | GIKGMVLDEN | YNNLTGAVIS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VTGINHDVTS | GEHGDYFRLL | LPGTYSVTAK | ASGYEPKTVT | VTVGPAGPTL | VDFQLKRSTT |
| 430 | 440 | 450 | |||
| QVHPVQKAPG | RGQGSRAKQP | RTSRKKDQAA | KRHRGPA |