Q07292
Gene name |
lin-45 (raf-1, Y73B6A.5) |
Protein name |
Raf homolog serine/threonine-protein kinase |
Names |
Abnormal cell lineage protein 45 |
Species |
Caenorhabditis elegans |
KEGG Pathway |
|
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with P04049)
Raf proteins are Ras-regulated serine/threonine protein kinases that control the activation of the ERK/MARK cascade, and consists of three isoforms, A-Raf, B-Raf, and Raf-1 (C-Raf). When the catalytic domain of Raf-1 is expressed alone, it exhibits a constitutive activity. Raf-1 is regulated by an N-terminal autoinhibitory domain including Ras binding domain (RBD) and cysteine-rich domain (CRD). The autoinhibitory region blocks the catalytic kinase domain and the autoinhibition is interrupted by the interaction with active PAK1 or Src.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
620-647 (Activation loop from InterPro)
Target domain |
481-748 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for Q07292
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q07292-F1 | Predicted | AlphaFoldDB |
No variants for Q07292
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q07292 | |||||
No associated diseases with Q07292
6 regional properties for Q07292
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 481 - 748 | IPR000719 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 484 - 743 | IPR001245 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 170 - 218 | IPR002219 |
| domain | Raf-like Ras-binding | 85 - 161 | IPR003116 |
| active_site | Serine/threonine-protein kinase, active site | 598 - 610 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 487 - 508 | IPR017441 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| MAP kinase kinase kinase activity | Catalysis of the phosphorylation and activation of a MAP kinase kinase; each MAP kinase kinase can be phosphorylated by any of several MAP kinase kinase kinases. |
| metal ion binding | Binding to a metal ion. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
| small GTPase binding | Binding to a small monomeric GTPase. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| cell fate specification | The process involved in the specification of cell identity. Once specification has taken place, a cell will be committed to differentiate down a specific pathway if left in its normal environment. |
| defense response to Gram-positive bacterium | Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism. |
| MAPK cascade | An intracellular protein kinase cascade containing at least a MAPK, a MAPKK and a MAP3K. The cascade can also contain an additional tiers: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell. |
| meiotic cell cycle | Progression through the phases of the meiotic cell cycle, in which canonically a cell replicates to produce four offspring with half the chromosomal content of the progenitor cell via two nuclear divisions. |
| nematode larval development | The process whose specific outcome is the progression of the nematode larva over time, from its formation to the mature structure. Nematode larval development begins with the newly hatched first-stage larva (L1) and ends with the end of the last larval stage (for example the fourth larval stage (L4) in C. elegans). Each stage of nematode larval development is characterized by proliferation of specific cell lineages and an increase in body size without alteration of the basic body plan. Nematode larval stages are separated by molts in which each stage-specific exoskeleton, or cuticle, is shed and replaced anew. |
| oogenesis | The complete process of formation and maturation of an ovum or female gamete from a primordial female germ cell. Examples of this process are found in Mus musculus and Drosophila melanogaster. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| Ras protein signal transduction | The series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state. |
| reproduction | The production of new individuals that contain some portion of genetic material inherited from one or more parent organisms. |
| vulval development | The process whose specific outcome is the progression of the egg-laying organ of female and hermaphrodite nematodes over time, from its formation to the mature structure. In nematodes, the vulva is formed from ventral epidermal cells during larval stages to give rise to a fully formed vulva in the adult. |
18 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A7E3S4 | RAF1 | RAF proto-oncogene serine/threonine-protein kinase | Bos taurus (Bovine) | SS |
| P05625 | RAF1 | RAF proto-oncogene serine/threonine-protein kinase | Gallus gallus (Chicken) | PR |
| Q04982 | BRAF | Serine/threonine-protein kinase B-raf | Gallus gallus (Chicken) | SS |
| P11346 | Raf | Raf homolog serine/threonine-protein kinase Raf | Drosophila melanogaster (Fruit fly) | PR |
| P15056 | BRAF | Serine/threonine-protein kinase B-raf | Homo sapiens (Human) | EV |
| P04049 | RAF1 | RAF proto-oncogene serine/threonine-protein kinase | Homo sapiens (Human) | EV |
| P10398 | ARAF | Serine/threonine-protein kinase A-Raf | Homo sapiens (Human) | PR |
| Q8NB16 | MLKL | Mixed lineage kinase domain-like protein | Homo sapiens (Human) | EV |
| P04627 | Araf | Serine/threonine-protein kinase A-Raf | Mus musculus (Mouse) | PR |
| Q99N57 | Raf1 | RAF proto-oncogene serine/threonine-protein kinase | Mus musculus (Mouse) | SS |
| Q9D2Y4 | Mlkl | Mixed lineage kinase domain-like protein | Mus musculus (Mouse) | SS |
| P28028 | Braf | Serine/threonine-protein kinase B-raf | Mus musculus (Mouse) | SS |
| O19004 | ARAF | Serine/threonine-protein kinase A-Raf | Sus scrofa (Pig) | PR |
| P11345 | Raf1 | RAF proto-oncogene serine/threonine-protein kinase | Rattus norvegicus (Rat) | SS |
| P14056 | Araf | Serine/threonine-protein kinase A-Raf | Rattus norvegicus (Rat) | PR |
| Q9TZC4 | pat-4 | Integrin-linked protein kinase homolog pat-4 | Caenorhabditis elegans | PR |
| Q9FPR3 | EDR1 | Serine/threonine-protein kinase EDR1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q05609 | CTR1 | Serine/threonine-protein kinase CTR1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSRINFKKSS | ASTTPTSPHC | PSPRLISLPR | CASSSIDRKD | QASPMASPST | PLYPKHSDSL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HSLSGHHSAG | GAGTSDKEPP | KFKYKMIMVH | LPFDQHSRVE | VRPGETARDA | ISKLLKKRNI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TPQLCHVNAS | SDPKQESIEL | SLTMEEIASR | LPGNELWVHS | EYLNTVSSIK | HAIVRRTFIP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PKSCDVCNNP | IWMMGFRCEF | CQFKFHQRCS | SFAPLYCDLL | QSVPKNEDLV | KELFGIASQV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGPDRSVAEI | VLANLAPTSG | QSPAATPDSS | HPDLTSIKRT | GGVKRHPMAV | SPQNETSQLS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PSGPYPRDRS | SSAPNINAIN | DEATVQHNQR | ILDALEAQRL | EEESRDKTGS | LLSTQARHRP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HFQSGHILSG | ARMNRLHPLV | DCTPLGSNSP | SSTCSSPPGG | LIGQPTLGQS | PNVSGSTTSS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LVAAHLHTLP | LTPPQSAPPQ | KISPGFFRNR | SRSPGERLDA | QRPRPPQKPH | HEDWEILPNE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| FIIQYKVGSG | SFGTVYRGEF | FGTVAIKKLN | VVDPTPSQMA | AFKNEVAVLK | KTRHLNVLLF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MGWVREPEIA | IITQWCEGSS | LYRHIHVQEP | RVEFEMGAII | DILKQVSLGM | NYLHSKNIIH |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RDLKTNNIFL | MDDMSTVKIG | DFGLATVKTK | WTVNGGQQQQ | QPTGSILWMA | PEVIRMQDDN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PYTPQSDVYS | FGICMYEILS | SHLPYSNINN | RDQILFMVGR | GYLRPDRSKI | RHDTPKSMLK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LYDNCIMFDR | NERPVFGEVL | ERLRDIILPK | LTRSQSAPNV | LHLDSQYSVM | DAVMRSQMLS |
| 790 | 800 | 810 | |||
| WSYIPPATAK | TPQSAAAAAA | ANKKAYYNVY | GLI |