Q5RAE1
Gene name |
CPNE3 |
Protein name |
Copine-3 |
Names |
Copine III |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100174464 |
EC number |
|
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 Q5RAE1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5RAE1-F1 | Predicted | AlphaFoldDB |
No variants for Q5RAE1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5RAE1 | |||||
No associated diseases with Q5RAE1
5 regional properties for Q5RAE1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1 - 115 | IPR000008-1 |
| domain | C2 domain | 124 - 247 | IPR000008-2 |
| domain | von Willebrand factor, type A | 289 - 495 | IPR002035 |
| domain | Copine, C-terminal | 263 - 524 | IPR010734 |
| domain | Copine, C2B domain | 139 - 251 | IPR037768 |
Functions
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell junction | A cellular component that forms a specialized region of connection between two or more cells, or between a cell and the extracellular matrix, or between two membrane-bound components of a cell, such as flagella. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium-dependent phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium. |
| calcium-dependent protein binding | Binding to a protein or protein complex in the presence of calcium. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to calcium ion | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a calcium ion stimulus. |
| cellular response to growth factor stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus. |
| ERBB2 signaling pathway | The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB2 on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. ERBB2 receptors are themselves unable to bind to ligands, but act as a signal-amplifying tyrosine kinase within a heterodimeric pair. |
| positive regulation of cell migration | Any process that activates or increases the frequency, rate or extent of cell migration. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAQCVTKVA | LNVSCANLLD | KDIGSKSDPL | CVLFLNTSGQ | QWYEVERTER | IKNCLNPQFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KTFIIDYYFE | VVQKLKFGVY | DIDNKTIELS | DDDFLGECEC | TLGQVVSSKK | LTRPLVMKNG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RPAGKGSITI | SAEEIKDNRV | VLFEMEARKP | DNKDLFGKSD | PYLEFHKQTS | DGNWLMVHRT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EVVKNNLNPV | WRPFKISLNS | LCYGDMDKTI | KVECYDYDND | GSHDLIGTFQ | TTMTKLKEAS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RCSPVEFECI | NEKKRQKKKS | YKNSGVISVK | QCEITVECTF | LDYIMGGCQL | NFTVGVDFTG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SNDDPRSPDS | LHYISPNGVN | EYLTALWSVG | LVIQDYDADK | MFPAFGFGAQ | IPPQWQVSHE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FPMNFNPSNP | YCNGIQGIVE | AYRSCLPQIK | LYGPTNFSPI | INHVARFAAA | AAQQQTASQY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FVLLIITDGV | ITDLDETRQA | IVNASRLPMS | IIIVGVGGAD | FSAMEFLDGD | GGGLRSPSGE |
| 490 | 500 | 510 | 520 | 530 | |
| VAIRDIVQFV | PFRQFQNAPK | EALAQCVLAE | IPQQVVGYFN | TYKLLPPKNP | ATKQQKQ |