P91240 · SRP72_CAEEL

  • Protein
    Signal recognition particle subunit SRP72
  • Gene
    srpa-72
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity).
The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (By similarity).
The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER (By similarity).
Binds the signal recognition particle RNA (7SL RNA) in presence of srpa-68 (By similarity).
Can bind 7SL RNA with low affinity (By similarity).
The SRP complex possibly participates in the elongation arrest function (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentsignal recognition particle, endoplasmic reticulum targeting
Molecular Function7S RNA binding
Biological ProcessSRP-dependent cotranslational protein targeting to membrane

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Signal recognition particle subunit SRP72
  • Short names
    SRP72
  • Alternative names
    • Signal recognition particle 72 kDa protein homolog

Gene names

    • Name
      srpa-72
    • ORF names
      F08D12.1

Organism names

  • Taxonomic identifier
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    P91240

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001352351-635Signal recognition particle subunit SRP72

Proteomic databases

Expression

Gene expression databases

    • WBGene00017245Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues

Interaction

Subunit

Heterodimer with srpa-68 (By similarity).
Srpa-68-srpa-72 heterodimer formation is stabilized by the presence of 7SL RNA (By similarity).
Component of a signal recognition particle (SRP) complex that consists of a 7SL RNA molecule of 300 nucleotides and six protein subunits: srpa-72, srpa-68, SRP54, F37F2.2/SRP19, F25G6.8/SRP14 and ZK512.4/SRP9 (By similarity).
Within the SRP complex, interacts (via N-terminus) with srpa-68 (via C-terminus) (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, region, compositional bias.

Type
IDPosition(s)Description
Repeat7-42TPR 1
Repeat75-105TPR 2
Repeat106-139TPR 3
Repeat171-204TPR 4
Repeat220-253TPR 5
Repeat255-290TPR 6
Repeat436-469TPR 7
Region539-635Disordered
Compositional bias583-601Polar residues

Sequence similarities

Belongs to the SRP72 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    635
  • Mass (Da)
    71,414
  • Last updated
    2008-01-15 v2
  • MD5 Checksum
    996C699A5533F74BF586BE61D1022FDB
MADASAGGLYQCLTDISRADTSGDYQKALTSANKLIRKYPKETFAFKCKLVAQIQLSQYADALELIRKTPAHQMGHVGFEKAYIHYRQDELDEAIKELNTCDKDDVKALELKAQVFYKQENYQQAYDIYLYLLKNHSDDSDELRRANFLAVQARLEAQGVKQAVAETEDSYSQLYNRACVEIEAEKLPQALESLEKALKTCRKSFEDEDREEDEIEEELDSIRVQKAYVLQRMGQKAEALAIYEKVQAANHPDSSVKATITNNIPAASSDFALPESRKRFKAALQIDQTKLTRRQRLTLMLNNALVLLLSNQREPCKRALEELVAKFGSSKDVALIEATLHFKMGDAEAALKVLAGSDLEQSLARLHVLLNAGRLPEAVGAIRDLPISGKLGASSLLTSTLIAADSRDEAVKELVAASTAKNQTPEALKSILEDLVEVEQQRGNETAATKHLEKLVEKFPEDLQLQCRLVGAYSKTDPKKAESLSAKLFPETMEVDVNVDELEDSDWILYGEKYRQKKEAKSPQTAEIAATRKLKIATKRKRKIRLPKNYNSAVTPDPERWLPRQERSTYKRKRKNREREIGRGTQGSSSANPNVEYVTASPNSPRPLPGPVAEGPRQQRPNFQKQKKKKNASKF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias583-601Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO081086
EMBL· GenBank· DDBJ
CCD69012.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help