P38688 · SRP72_YEAST

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) (PubMed:10921896, PubMed:7925282).
The SRP complex interacts with the signal sequence in nascent secretory and membrane proteins and directs them to the membrane of the ER (PubMed:10921896, PubMed:7925282).
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 signal recognition particle RNA (7SL RNA) in presence of SRP68 (By similarity).
Can bind 7SL RNA with low affinity (By similarity).
The SRP complex possibly participates in the elongation arrest function (PubMed:10921896).

Miscellaneous

Present with 11800 molecules/cell in log phase SD medium.

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 membrane
Cellular Componentnucleolus
Cellular Componentsignal recognition particle, endoplasmic reticulum targeting
Molecular Function7S RNA binding
Biological ProcessSRP-dependent cotranslational protein targeting to membrane
Biological ProcessSRP-dependent cotranslational protein targeting to membrane, signal sequence recognition

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      SRP72
    • Ordered locus names
      YPL210C

Organism names

Accessions

  • Primary accession
    P38688
  • Secondary accessions
    • D6W3G0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus, nucleolus
Note: Transiently localizes to the nucleolus during biogenesis of the SRP. The SRP-RNC complex is bound to the endoplasmic reticulum membrane due to the interaction of the SRP with the membrane SRP-receptor (SRP101-SRP102).

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001352381-640Signal recognition particle subunit SRP72

Proteomic databases

PTM databases

Interaction

Subunit

Component of a fungal signal recognition particle (SRP) complex that consists of a 7SL RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14 (PubMed:7925282).
At least SRP14, SRP21, SRP68 and SRP72 are proposed to get assembled together with scR1 RNA as a pre-SRP complex in the nucleolus which is exported to the cytoplasm (PubMed:7925282).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P38688SEC65 P294789EBI-18011, EBI-16641
BINARY P38688SRP14 P389857EBI-18011, EBI-17977

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for repeat, compositional bias, region.

TypeIDPosition(s)Description
Repeat188-221TPR
Compositional bias574-596Basic and acidic residues
Region574-640Disordered
Compositional bias598-612Polar residues

Sequence similarities

Belongs to the SRP72 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    640
  • Mass (Da)
    73,541
  • Last updated
    2005-11-08 v2
  • Checksum
    DB2F536212F0871B
MAKDNLTNLLSQLNIQLSQDEHSQVEQTCVKLLDSGCENPADVFRRCLVAVIQQDKYQKALHYLKKFKHIDDKYGRKFALEKLYIFYKLNMPDEFNTLYTAIITDDLDTVLKKDIESLRGILHVRAQYCYKNGLYQEAFKIYQHLASHNEKDQDSQIELSCNERVPLSVATELMNRSPLVTPMDESSYDLLFNESFIMASVGKYDKAIELLEKALQGATNEGYQNDINTIKLQLSFVLQMVGKTAQSKEILKGLLQELKADSPFSLICQNNLNAFVDFSKYNTNFNLLLRELNVEKLNTFNLQTFTHEQWSNIQRNVLFLRLFNNVKIHSQESLLSRTFDKYSKLVDNVTLESYKTQAKKLYHHTTKTILSGTDGSTIGILLLTIQLLIIEKEWENAIRIGELFLNESWKSSFEKFNDSQAIVCYILFELYKIKGRNNSKSVLLKKLGSVRVQLSGKIQENIPFWKHVGFELLSMGNAKESKALLREISNFSKGDADVLVDRVVSSDSLDIAQGIDLVRDIDIDKLIQLGVKPLESSAKRSKNTAVSKVQKRKVLELKKKRKIKRLEKFLQGRDTSKLPDPERWLPLRDRSTYRPKKKQQGAKQTQGGAMNKKSEQALDISKKGKPTVNKKPKNKKKGRK

Sequence caution

The sequence AAA53400.1 differs from that shown. Reason: Erroneous initiation
The sequence CAA97925.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias574-596Basic and acidic residues
Compositional bias598-612Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L35178
EMBL· GenBank· DDBJ
AAA53400.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
Z73566
EMBL· GenBank· DDBJ
CAA97925.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
BK006949
EMBL· GenBank· DDBJ
DAA11226.1
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.
FeedbackHelp