P27489
Gene name |
CAB13 (LHBC1) |
Protein name |
Chlorophyll a-b binding protein 13, chloroplastic |
Names |
ADABP, Adenosine deaminase complexing protein 2, ADCP-2, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, TP103, LHCII type III CAB-13 |
Species |
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
KEGG Pathway |
sly:101243766 |
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 P27489
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P27489-F1 | Predicted | AlphaFoldDB |
7 variants for P27489
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| vcZ1ZOHBU | 13 | V>I | No | Ensembl | |
| vcZ1ZOHBY | 26 | A>S | No | Ensembl | |
| vcZ1ZOHC0 | 34 | A>V | No | Ensembl | |
| vcZ1ZOHC2 | 35 | M>I | No | Ensembl | |
| vcZ1ZOHC1 | 35 | M>V | No | Ensembl | |
| vcZ1ZOHD2 | 65 | S>P | No | Ensembl | |
| vcZ1ZOHER | 229 | V>I | No | Ensembl |
No associated diseases with P27489
No regional properties for P27489
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P27489 | |||
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast thylakoid membrane | The pigmented membrane of a chloroplast thylakoid. An example of this component is found in Arabidopsis thaliana. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| photosystem I | A photosystem that contains an iron-sulfur reaction center associated with accessory pigments and electron carriers. In cyanobacteria and chloroplasts, photosystem I functions as a light-dependent plastocyanin-ferredoxin oxidoreductase, transferring electrons from plastocyanin to ferredoxin; in photosynthetic bacteria that have only a single type I photosystem, such as the green sulfur bacteria, electrons can go either to ferredoxin (Fd) -> NAD+ or to menaquinone (MK) -> Cytb/FeS -> Cytc555 -> photosystem I (cyclic photophosphorylation). |
| photosystem II | A photosystem that contains a pheophytin-quinone reaction center with associated accessory pigments and electron carriers. In cyanobacteria and chloroplasts, in the presence of light, PSII functions as a water-plastoquinone oxidoreductase, transferring electrons from water to plastoquinone, whereas other photosynthetic bacteria carry out anoxygenic photosynthesis and oxidize other compounds to re-reduce the photoreaction center. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| chlorophyll binding | Binding to a chlorophyll; a compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| photosynthesis, light harvesting in photosystem I | After a photon of light is absorbed by one of the many chlorophyll molecules, in one of the light-harvesting complexes of an antenna on photosystem I, some of the absorbed energy is transferred to the pair of chlorophyll molecules in the reaction center. |
| response to light stimulus | 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 light stimulus, electromagnetic radiation of wavelengths classified as infrared, visible or ultraviolet light. |
2 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASMAATASS | TTVVKATPFL | GQTKNANPLR | DVVAMGSARF | TMSNDLWYGP | DRVKYLGPFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AQTPSYLNGE | FPGDYGWDTA | GLSADPEAFA | KNRALEVIHG | RWAMLGALGC | IFPEVLEKWV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KVDFKEPVWF | KAGSQIFSDG | GLDYLGNPNL | VHAQSILAVL | GFQVVLMGLV | EGFRINGLPG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VGEGNDLYPG | GQYFDPLGLA | DDPTTFAELK | VKEIKNGRLA | MFSMFGFFVQ | AIVTGKGPLE |
| 250 | 260 | ||||
| NLLDHLDNPV | ANNAWVYATK | FVPGA |