P61010
PR
Gene name |
SRP54 |
Protein name |
Signal recognition particle 54 kDa protein |
Names |
SRP54 |
Species |
Canis lupus familiaris (Dog) (Canis familiaris) |
KEGG Pathway |
cfa:403953 |
EC number |
3.6.5.4: Acting on GTP; involved in cellular and subcellular movement |
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
No variants for P61010
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P61010 | |||||
No associated diseases with P61010
4 regional properties for P61010
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Signal recognition particle, SRP54 subunit, GTPase domain | 101 - 296 | IPR000897 |
| domain | AAA+ ATPase domain | 100 - 277 | IPR003593 |
| domain | Signal recognition particle, SRP54 subunit, M-domain | 326 - 431 | IPR004125 |
| domain | Signal recognition particle SRP54, helical bundle | 2 - 87 | IPR013822 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.5.4 | Acting on GTP; involved in cellular and subcellular movement |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| nuclear speck | A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. |
| 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. |
| signal recognition particle, endoplasmic reticulum targeting | A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 7S RNA binding | Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP). |
| endoplasmic reticulum signal peptide binding | Binding to an endoplasmic reticulum signal peptide, a specific peptide sequence that acts as a signal to localize the protein within the endoplasmic reticulum. |
| GDP binding | Binding to GDP, guanosine 5'-diphosphate. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| ribonucleoprotein complex binding | Binding to a complex of RNA and protein. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| exocrine pancreas development | The process whose specific outcome is the progression of the exocrine pancreas over time, from its formation to the mature structure. The exocrine pancreas produces and store zymogens of digestive enzymes, such as chymotrypsinogen and trypsinogen in the acinar cells. |
| granulocyte differentiation | The process in which a myeloid precursor cell acquires the specialized features of a granulocyte. Granulocytes are a class of leukocytes characterized by the presence of granules in their cytoplasm. These cells are active in allergic immune reactions such as arthritic inflammation and rashes. This class includes basophils, eosinophils and neutrophils. |
| neutrophil chemotaxis | The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding. |
| protein targeting to ER | The process of directing proteins towards the endoplasmic reticulum (ER) using signals contained within the protein. One common mechanism uses a 16- to 30-residue signal sequence, typically located at the N-terminus of the protein and containing positively charged amino acids followed by a continuous stretch of hydrophobic residues, which directs the ribosome to the ER membrane and initiates transport of the growing polypeptide across the ER membrane. |
| SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition | The process in which SRP binds to the signal peptide in a nascent protein, causing protein elongation to pause, during cotranslational membrane targeting. |
| SRP-dependent cotranslational protein targeting to membrane, translocation | The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P20424 | SRP54 | Signal recognition particle subunit SRP54 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q2T9U1 | SRP54 | Signal recognition particle 54 kDa protein | Bos taurus (Bovine) | PR |
| P61011 | SRP54 | Signal recognition particle 54 kDa protein | Homo sapiens (Human) | PR |
| P14576 | Srp54 | Signal recognition particle 54 kDa protein | Mus musculus (Mouse) | PR |
| Q6AYB5 | Srp54 | Signal recognition particle 54 kDa protein | Rattus norvegicus (Rat) | PR |
| P49966 | SRP-54B | Signal recognition particle 54 kDa protein 2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P37107 | FFC | Signal recognition particle 54 kDa protein, chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| P49972 | Signal recognition particle 54 kDa protein 2 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR | |
| P49971 | Signal recognition particle 54 kDa protein 1 | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVLADLGRKI | TSALRSLSNA | TIINEEVLNA | MLKEVCTALL | EADVNIKLVK | QLRENVKSAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLEEMASGLN | KRKMIQHAVF | KELVKLVDPG | VKAWTPTKGK | QNVIMFVGLQ | GSGKTTTCSK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LAYYYQRKGW | KTCLICADTF | RAGAFDQLKQ | NATKARIPFY | GSYTEMDPVI | IASEGVEKFK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NENFEIIIVD | TSGRHKQEDS | LFEEMLQVAN | AIQPDNIVYV | MDASIGQACE | AQAKAFKDKV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVASVIVTKL | DGHAKGGGAL | SAVAATKSPI | IFIGTGEHID | DFEPFKTQPF | ISKLLGMGDI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EGLIDKVNEL | KLDDNEALIE | KLKHGQFTLR | DMYEQFQNIM | KMGPFSQILG | MIPGFGTDFM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SKGNEQESMA | RLKKLMTIMD | SMNDQELDST | DGAKVFSKQP | GRIQRVARGS | GVSTRDVQEL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LTQYTKFAQM | VKKMGGIKGL | FKGGDMSKNV | SQSQMAKLNQ | QMAKMMDPRV | LHHMGGMAGL |
| 490 | 500 | ||||
| QSMMRQFQQG | AAGNMKGMMG | FNNM |