P32916 · SRPR_YEAST

Function

function

Component of the SRP (signal recognition particle) receptor (SR). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction. It is important but not essential for cell growth. May be directly involved in mitochondrial protein import.

Miscellaneous

Present with 2000 molecules/cell in log phase SD medium.

Features

Showing features for binding site.

162150100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site404-411GTP (UniProtKB | ChEBI)
Binding site510-514GTP (UniProtKB | ChEBI)
Binding site572-575GTP (UniProtKB | ChEBI)

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 Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Cellular Componentsignal recognition particle receptor complex
Molecular FunctionATP hydrolysis activity
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionsignal recognition particle binding
Biological Processprotein targeting to ER
Biological ProcessSRP-dependent cotranslational protein targeting to membrane, signal sequence recognition

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Signal recognition particle receptor subunit alpha homolog
  • Short names
    SR-alpha
  • Alternative names
    • Docking protein alpha (DP-alpha)

Gene names

    • Name
      SRP101
    • ORF names
      D9819.3
    • Ordered locus names
      YDR292C

Organism names

Accessions

  • Primary accession
    P32916
  • Secondary accessions
    • D6VSS1
    • Q05553

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Peripheral membrane protein
Note: Thought to be anchored in the membrane through an interaction with SRP102/SR-beta, which contains a bona fide transmembrane domain.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001012161-621Signal recognition particle receptor subunit alpha homolog
Modified residue239Phosphoserine
Modified residue523Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Heterodimer of an alpha and a beta chain.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P32916SRP102 P360576EBI-18098, EBI-18091
View interactors in UniProtKB
View CPX-780 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-158SRX
Region167-217Disordered
Compositional bias169-184Polar residues
Region398-620NG domain

Domain

The SRX domain is sufficient for interaction with GTP-bound SRP102/SR-beta.
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the signal recognition particle (SRP) complex subunit SRP54 (By similarity).
The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (By similarity).
GTPase induced rearrangement of SR drives SRP-mediated cotranslational protein translocation into the ER (By similarity).

Sequence similarities

Belongs to the GTP-binding SRP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    621
  • Mass (Da)
    69,278
  • Last updated
    1997-11-01 v2
  • Checksum
    032400E5B3310C91
MFDQLAVFTPQGQVLYQYNCLGKKFSEIQINSFISQLITSPVTRKESVANANTDGFDFNLLTINSEHKNSPSFNALFYLNKQPELYFVVTFAEQTLELNQETQQTLALVLKLWNSLHLSESILKNRQGQNEKNKHNYVDILQGIEDDLKKFEQYFRIKYEESIKQDHINPDNFTKNGSVPQSHNKNTKKKLRDTKGKKQSTGNVGSGRKWGRDGGMLDEMNHEDAAKLDFSSSNSHNSSQVALDSTINKDSFGDRTEGGDFLIKEIDDLLSSHKDEITSGNEAKNSGYVSTAFGFLQKHVLGNKTINESDLKSVLEKLTQQLITKNVAPEAADYLTQQVSHDLVGSKTANWTSVENTARESLTKALTQILTPGVSVDLLREIQSKRSKKDEEGKCDPYVFSIVGVNGVGKSTNLSKLAFWLLQNNFKVLIVACDTFRSGAVEQLRVHVENLAQLMDDSHVRGSKNKRGKTGNDYVELFEAGYGGSDLVTKIAKQAIKYSRDQNFDIVLMDTAGRRHNDPTLMSPLKSFADQAKPDKIIMVGEALVGTDSVQQAKNFNDAFGKGRNLDFFIISKCDTVGEMLGTMVNMVYATGIPILFVGVGQTYTDLRTLSVKWAVNTLMS

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias169-184Polar residues
Sequence conflict499in Ref. 1; AAA35093

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M77274
EMBL· GenBank· DDBJ
AAA35093.1
EMBL· GenBank· DDBJ
Genomic DNA
U51031
EMBL· GenBank· DDBJ
AAB64468.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA12131.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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