Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Signal recognition particle subunit SRP54

Gene

SRP54

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP54 binds to the signal sequence of presecretory protein when they emerge from the ribosomes. SRP54 interacts with the scR1 RNA and mediates the association of the resulting SRP-RNC complex with the signal recognition particle receptor (SR) via its alpha subunit SRP101. Both, SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR complex, which dissociates upon transferring the signal sequence to the protein-conducting channel (translocon). After signal sequence transfer, SRP54 and SRP101 act as reciprocal GTPAse-activating proteins (GAPs), thereby resolving their association.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi116 – 1238GTPBy similarity
Nucleotide bindingi198 – 2025GTPBy similarity
Nucleotide bindingi256 – 2594GTPBy similarity

GO - Molecular functioni

  • 7S RNA binding Source: SGD
  • endoplasmic reticulum signal peptide binding Source: SGD
  • GTPase activator activity Source: UniProtKB-KW
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • SRP-dependent cotranslational protein targeting to membrane Source: SGD
  • SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation, Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34231-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle subunit SRP54
Alternative name(s):
Signal recognition particle 54 kDa protein homolog
Gene namesi
Name:SRP54
Synonyms:SRH1
Ordered Locus Names:YPR088C
ORF Names:P9513.14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPR088C.
SGDiS000006292. SRP54.

Subcellular locationi

GO - Cellular componenti

  • signal recognition particle, endoplasmic reticulum targeting Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Signal recognition particle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Signal recognition particle subunit SRP54PRO_0000101203Add
BLAST

Proteomic databases

MaxQBiP20424.
PeptideAtlasiP20424.

PTM databases

iPTMnetiP20424.

Interactioni

Subunit structurei

Fungal signal recognition particle (SRP) complex consists of a 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14. SRP54 interacts with SRP101.1 Publication

Protein-protein interaction databases

BioGridi36258. 163 interactions.
DIPiDIP-2943N.
IntActiP20424. 25 interactions.
MINTiMINT-484768.

Structurei

3D structure databases

ProteinModelPortaliP20424.
SMRiP20424. Positions 1-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 303303G-domainAdd
BLAST
Regioni304 – 541238M-domainAdd
BLAST

Domaini

Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA and also binds the signal sequence.

Sequence similaritiesi

Belongs to the GTP-binding SRP family. SRP54 subfamily.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074824.
HOGENOMiHOG000036165.
InParanoidiP20424.
KOiK03106.
OMAiFLKMGPL.
OrthoDBiEOG7NCVCS.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR006325. SRP54_euk.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01425. SRP54_euk. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLADLGKRI NSAVNNAISN TQDDFTTSVD VMLKGIVTAL LESDVNIALV
60 70 80 90 100
SKLRNNIRSQ LLSENRSEKS TTNAQTKKLI QKTVFDELCK LVTCEGSEEK
110 120 130 140 150
AFVPKKRKTN IIMFVGLQGS GKTTSCTKLA VYYSKRGFKV GLVCADTFRA
160 170 180 190 200
GAFDQLKQNA IRARIPFYGS YTETDPAKVA EEGINKFKKE KFDIIIVDTS
210 220 230 240 250
GRHHQEEELF QEMIEISNVI KPNQTIMVLD ASIGQAAEQQ SKAFKESSDF
260 270 280 290 300
GAIILTKMDG HARGGGAISA VAATNTPIIF IGTGEHIHDL EKFSPKSFIS
310 320 330 340 350
KLLGIGDIES LFEQLQTVSN KEDAKATMEN IQKGKFTLLD FKKQMQTIMK
360 370 380 390 400
MGPLSNIAQM IPGMSNMMNQ VGEEETSQKM KKMVYVLDSM TKEELESDGR
410 420 430 440 450
MFIEEPTRMV RVAKGSGTSV FEVEMILMQQ QMMARMAQTA TQQQPGAPGA
460 470 480 490 500
NARMPGMPNM PGMPNMPGMP NMPGMPKVTP QMMQQAQQKL KQNPGLMQNM
510 520 530 540
MNMFGGGMGG GMGGGMPDMN EMMKMMQDPQ MQQMAKQFGM G
Length:541
Mass (Da):59,624
Last modified:October 1, 1996 - v2
Checksum:i05B1B2C262932F17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361R → E in CAA34781 (PubMed:2187859).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16908 Genomic DNA. Translation: CAA34781.1.
M55517 Genomic DNA. Translation: AAA35092.1.
X51614 Genomic DNA. Translation: CAA35952.1.
U51033 Genomic DNA. Translation: AAB68136.1.
BK006949 Genomic DNA. Translation: DAA11505.1.
PIRiS69073. JX0112.
RefSeqiNP_015413.1. NM_001184185.1.

Genome annotation databases

EnsemblFungiiYPR088C; YPR088C; YPR088C.
GeneIDi856203.
KEGGisce:YPR088C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16908 Genomic DNA. Translation: CAA34781.1.
M55517 Genomic DNA. Translation: AAA35092.1.
X51614 Genomic DNA. Translation: CAA35952.1.
U51033 Genomic DNA. Translation: AAB68136.1.
BK006949 Genomic DNA. Translation: DAA11505.1.
PIRiS69073. JX0112.
RefSeqiNP_015413.1. NM_001184185.1.

3D structure databases

ProteinModelPortaliP20424.
SMRiP20424. Positions 1-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36258. 163 interactions.
DIPiDIP-2943N.
IntActiP20424. 25 interactions.
MINTiMINT-484768.

PTM databases

iPTMnetiP20424.

Proteomic databases

MaxQBiP20424.
PeptideAtlasiP20424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPR088C; YPR088C; YPR088C.
GeneIDi856203.
KEGGisce:YPR088C.

Organism-specific databases

EuPathDBiFungiDB:YPR088C.
SGDiS000006292. SRP54.

Phylogenomic databases

GeneTreeiENSGT00550000074824.
HOGENOMiHOG000036165.
InParanoidiP20424.
KOiK03106.
OMAiFLKMGPL.
OrthoDBiEOG7NCVCS.

Enzyme and pathway databases

BioCyciYEAST:G3O-34231-MONOMER.

Miscellaneous databases

PROiP20424.

Family and domain databases

Gene3Di1.10.260.30. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_00306. SRP54.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR013822. Signal_recog_particl_SRP54_hlx.
IPR004125. Signal_recog_particle_SRP54_M.
IPR022941. SRP54.
IPR006325. SRP54_euk.
IPR000897. SRP54_GTPase_dom.
[Graphical view]
PfamiPF00448. SRP54. 1 hit.
PF02881. SRP54_N. 1 hit.
PF02978. SRP_SPB. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00962. SRP54. 1 hit.
SM00963. SRP54_N. 1 hit.
[Graphical view]
SUPFAMiSSF47364. SSF47364. 1 hit.
SSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01425. SRP54_euk. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K subunit of mammalian signal recognition particle."
    Amaya Y., Nakano A., Ito K., Mori M.
    J. Biochem. 107:457-463(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 38626 / AH22 / NRRL Y-12843.
  2. "Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth."
    Hann B.C., Poritz M.A., Walter P.
    J. Cell Biol. 109:3223-3230(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Identification of RNA sequences and structural elements required for assembly of fission yeast SRP54 protein with signal recognition particle RNA."
    Selinger D., Brennwald P., Liao X., Wise J.A.
    Mol. Cell. Biol. 13:1353-1362(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  6. "Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression."
    Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L., Walter P.
    EMBO J. 13:4390-4400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SRP COMPLEX.
  7. "The nascent polypeptide-associated complex modulates interactions between the signal recognition particle and the ribosome."
    Powers T., Walter P.
    Curr. Biol. 6:331-338(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel."
    Song W., Raden D., Mandon E.C., Gilmore R.
    Cell 100:333-343(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRP54_YEAST
AccessioniPrimary (citable) accession number: P20424
Secondary accession number(s): D6W489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.