O13828
Gene name |
dcp2 (SPAC19A8.12) |
Protein name |
mRNA decapping complex subunit 2 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC19A8.12 |
EC number |
|
Protein Class |
M7GPPPN-MRNA HYDROLASE (PTHR23114) |
Descriptions
Autoinhibition of the Dcp1:Dcp2 complex is mediated by the disordered C-terminal extension containing linear interaction motifs (IM1 and IM2), which inhibit decapping activity by stabilizing a cap-occluded conformation of Dcp2. This prevents the formation of a composite active site necessary for decapping, thus regulating mRNA decay. Enhancers of decapping (Edc) 1 and 3 cooperate to activate decapping by different mechanisms: Edc3 alleviates autoinhibition by binding to the proximal region of Dcp2’s inhibitory motifs, whereas Edc1 stabilizes the transition state for catalysis.
Autoinhibitory domains (AIDs)
Target domain |
1-243 (Composite active site of Dcp2, which includes the regulatory, NRD, and catalytic domain, CD) |
Relief mechanism |
Ligand binding |
Assay |
Deletion assay, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
10 structures for O13828
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2A6T | X-ray | 250 A | A/B | 1-266 | PDB |
| 2QKL | X-ray | 233 A | B | 1-95 | PDB |
| 2QKM | X-ray | 280 A | B/D/F/H | 1-266 | PDB |
| 4A54 | NMR | - | B | 242-291 | PDB |
| 5J3T | X-ray | 160 A | B | 1-242 | PDB |
| 5J3Y | X-ray | 329 A | B/D | 1-242 | PDB |
| 5KQ1 | X-ray | 300 A | B/E | 1-244 | PDB |
| 5KQ4 | X-ray | 256 A | B/E | 1-244 | PDB |
| 5N2V | X-ray | 310 A | B/E | 1-243 | PDB |
| AF-O13828-F1 | Predicted | AlphaFoldDB |
14 variants for O13828
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_2464935_G_A | 6 | A>V | No | Jeffares_SNPs | |
| I_2464482_T_A | 157 | N>I | No | Jeffares_SNPs | |
| I_2464165_G_A | 263 | L>F | No | Jeffares_SNPs | |
| I_2463852_A_G | 367 | L>S | No | Jeffares_SNPs | |
| I_2463813_C_T | 380 | S>N | No | Jeffares_SNPs | |
| I_2463634_C_T | 440 | G>R | No | Jeffares_SNPs | |
| I_2463480_C_G | 491 | S>T | No | Jeffares_SNPs | |
| I_2463398_C_A | 518 | L>F | No | Jeffares_SNPs | |
| I_2463357_C_T | 532 | S>N | No | Jeffares_SNPs | |
| I_2463340_A_C | 538 | S>A | No | Jeffares_SNPs | |
| I_2463334_T_A | 540 | N>Y | No | Jeffares_SNPs | |
| I_2463312_T_A | 547 | N>I | No | Jeffares_SNPs | |
| I_2463040_T_C | 638 | R>G | No | Jeffares_SNPs | |
| I_2462796_T_A | 719 | K>I | No | Jeffares_SNPs |
No associated diseases with O13828
No regional properties for O13828
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for O13828 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR23114 | M7GPPPN-MRNA HYDROLASE |
| PANTHER Subfamily | PTHR23114:SF17 | M7GPPPN-MRNA HYDROLASE |
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoplasmic stress granule | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mRNA cap binding complex | Any protein complex that binds to an mRNA cap at any time in the lifetime of the mRNA. |
| 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. |
| P-body | A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. |
| RNA decapping complex | A protein complex consisting of a Dcp1 regulatory subunit and a Dcp2 catalytic subunit that has mRNA cap binding activity and is involved in decapping of nuclear-transcribed mRNA. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5'-(N(7)-methyl 5'-triphosphoguanosine)-mRNA diphosphatase activity | Catalysis of the reaction |
| 5'-(N(7)-methylguanosine 5'-triphospho)-mRNA hydrolase activity | Catalysis of the reaction |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| mRNA cap binding | Binding to a 7-methylguanosine (m7G) group or derivative located at the 5' end of an mRNA molecule. |
| single-stranded RNA binding | Binding to single-stranded RNA. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| deadenylation-dependent decapping of nuclear-transcribed mRNA | Cleavage of the 5'-cap of a nuclear mRNA triggered by shortening of the poly(A) tail to below a minimum functional length. |
| methylguanosine-cap decapping | Cleavage of the 5'-methylguanosine-cap of an mRNA. The methylguanosine-cap is present at the 5'-end of eukaryotic mRNAs. Decapping inactivates translation initiation and promotes 5'-to-3' decay of mRNA. |
| mRNA processing | Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide. |
| nuclear-transcribed mRNA catabolic process, exonucleolytic, 5'-3' | The chemical reactions and pathways resulting in the breakdown of the mRNA transcript body that occurs when the 5' end is not protected by a 5'-cap; degradation proceeds in the 5' to 3' direction. |
| nuclear-transcribed mRNA catabolic process, nonsense-mediated decay | The nonsense-mediated decay pathway for nuclear-transcribed mRNAs degrades mRNAs in which an amino-acid codon has changed to a nonsense codon; this prevents the translation of such mRNAs into truncated, and potentially harmful, proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSFTNATFSQ | VLDDLSARFI | LNLPAEEQSS | VERLCFQIEQ | AHWFYEDFIR | AQNDQLPSLG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LRVFSAKLFA | HCPLLWKWSK | VHEEAFDDFL | RYKTRIPVRG | AIMLDMSMQQ | CVLVKGWKAS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGWGFPKGKI | DKDESDVDCA | IREVYEETGF | DCSSRINPNE | FIDMTIRGQN | VRLYIIPGIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LDTRFESRTR | KEISKIEWHN | LMDLPTFKKN | KPQTMKNKFY | MVIPFLAPLK | KWIKKRNIAN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NTTKEKNISV | DVDADASSQL | LSLLKSSTAP | SDLATPQPST | FPQPPVESHS | SFDIKQKILH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLNEGNEPKS | PIQLPPVSNL | PLNPPIQSSN | SRLSHDNNSF | DPFAYLGLDP | KNPSASFPRV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VSQNNMLTNK | PVLNNHFQQS | MYSNLLKDQN | SVQHLFAASD | MPSPMELPSP | STVYHQVFYP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PTSTSVSSYG | LGKTPQPAYG | SSSPYVNGHQ | TQQISSLPPF | QSQTQFLARN | SDNSGQSYNS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EGDSNSKRLL | SMLSQQDTTP | SSSTLSKEAN | VQLANLFLTP | NSLETKKFSD | NSQGEEISDN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LHGESCNNPN | ANSVHSAQLL | QALLHPSATE | TKEETPKKTS | DSLSLLTLLK | SGLPTPANDL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QNKSQNNERK | ASSQVKELEV | KNYSKSTDLL | KKTLRIPRND | EPLEAANQFD | LLKVSPQQKS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EVPPKRNELS | QSKLKNRKKK | ENSETNKNHV | DMSPGFVKIL | KRSPLADQKK | EDTQESDFKG |
| 730 | 740 | ||||
| SDDHFLSYLQ | SVVSSNSNGL | H |