SRP54_YEAST
ID SRP54_YEAST Reviewed; 541 AA.
AC P20424; D6W489;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Signal recognition particle subunit SRP54;
DE AltName: Full=Signal recognition particle 54 kDa protein homolog;
GN Name=SRP54; Synonyms=SRH1; OrderedLocusNames=YPR088C; ORFNames=P9513.14;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=2187859; DOI=10.1093/oxfordjournals.jbchem.a123067;
RA Amaya Y., Nakano A., Ito K., Mori M.;
RT "Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K
RT subunit of mammalian signal recognition particle.";
RL J. Biochem. 107:457-463(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2557350; DOI=10.1083/jcb.109.6.3223;
RA Hann B.C., Poritz M.A., Walter P.;
RT "Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue
RT to the 54-kD subunit of the signal recognition particle that in S.
RT cerevisiae is essential for growth.";
RL J. Cell Biol. 109:3223-3230(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP RNA-BINDING.
RX PubMed=8382769; DOI=10.1128/mcb.13.3.1353-1362.1993;
RA Selinger D., Brennwald P., Liao X., Wise J.A.;
RT "Identification of RNA sequences and structural elements required for
RT assembly of fission yeast SRP54 protein with signal recognition particle
RT RNA.";
RL Mol. Cell. Biol. 13:1353-1362(1993).
RN [6]
RP IDENTIFICATION IN THE SRP COMPLEX.
RX PubMed=7925282; DOI=10.1002/j.1460-2075.1994.tb06759.x;
RA Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,
RA Walter P.;
RT "Subunits of the Saccharomyces cerevisiae signal recognition particle
RT required for its functional expression.";
RL EMBO J. 13:4390-4400(1994).
RN [7]
RP FUNCTION.
RX PubMed=8805251; DOI=10.1016/s0960-9822(02)00484-0;
RA Powers T., Walter P.;
RT "The nascent polypeptide-associated complex modulates interactions between
RT the signal recognition particle and the ribosome.";
RL Curr. Biol. 6:331-338(1996).
RN [8]
RP FUNCTION.
RX PubMed=10676815; DOI=10.1016/s0092-8674(00)80669-8;
RA Song W., Raden D., Mandon E.C., Gilmore R.;
RT "Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain
RT complex from the signal recognition particle to the translocation
RT channel.";
RL Cell 100:333-343(2000).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Signal-recognition-particle (SRP) assembly has a crucial role
CC in targeting secretory proteins to the rough endoplasmic reticulum (ER)
CC membrane. SRP is required for the cotranslational protein translocation
CC for ER import and preferentially recognizes strongly hydrophobic signal
CC sequences. It is involved in targeting the nascent chain-ribosome (RNC)
CC complex to the ER and is proposed to participate in the arrest of
CC nascent chain elongation during membrane targeting. SRP54 binds to the
CC signal sequence of presecretory protein when they emerge from the
CC ribosomes. SRP54 interacts with the scR1 RNA and mediates the
CC association of the resulting SRP-RNC complex with the signal
CC recognition particle receptor (SR) via its alpha subunit SRP101. Both,
CC SRP54 and SRP101, are locked in their GTP bound forms in the SRP-RNC-SR
CC complex, which dissociates upon transferring the signal sequence to the
CC protein-conducting channel (translocon). After signal sequence
CC transfer, SRP54 and SRP101 act as reciprocal GTPAse-activating proteins
CC (GAPs), thereby resolving their association.
CC {ECO:0000269|PubMed:10676815, ECO:0000269|PubMed:8805251}.
CC -!- SUBUNIT: Fungal signal recognition particle (SRP) complex consists of a
CC 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68,
CC SRP54, SEC65, SRP21 and SRP14. SRP54 interacts with SRP101.
CC {ECO:0000269|PubMed:7925282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
CC domain binds the 7S RNA and also binds the signal sequence.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; X16908; CAA34781.1; -; Genomic_DNA.
DR EMBL; M55517; AAA35092.1; -; Genomic_DNA.
DR EMBL; X51614; CAA35952.1; -; Genomic_DNA.
DR EMBL; U51033; AAB68136.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11505.1; -; Genomic_DNA.
DR PIR; S69073; JX0112.
DR RefSeq; NP_015413.1; NM_001184185.1.
DR AlphaFoldDB; P20424; -.
DR SMR; P20424; -.
DR BioGRID; 36258; 291.
DR ComplexPortal; CPX-609; Signal recognition particle.
DR DIP; DIP-2943N; -.
DR IntAct; P20424; 23.
DR MINT; P20424; -.
DR STRING; 4932.YPR088C; -.
DR iPTMnet; P20424; -.
DR MaxQB; P20424; -.
DR PaxDb; P20424; -.
DR PRIDE; P20424; -.
DR EnsemblFungi; YPR088C_mRNA; YPR088C; YPR088C.
DR GeneID; 856203; -.
DR KEGG; sce:YPR088C; -.
DR SGD; S000006292; SRP54.
DR VEuPathDB; FungiDB:YPR088C; -.
DR eggNOG; KOG0780; Eukaryota.
DR GeneTree; ENSGT00550000074824; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; P20424; -.
DR OMA; DTAGRHK; -.
DR BioCyc; YEAST:G3O-34231-MON; -.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:P20424; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P20424; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
DR GO; GO:0008312; F:7S RNA binding; IDA:SGD.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IDA:SGD.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; GTPase activation; Nucleotide-binding;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..541
FT /note="Signal recognition particle subunit SRP54"
FT /id="PRO_0000101203"
FT REGION 1..303
FT /note="G-domain"
FT REGION 304..541
FT /note="M-domain"
FT REGION 442..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 198..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 256..259
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 136
FT /note="R -> E (in Ref. 1; CAA34781)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 59624 MW; 05B1B2C262932F17 CRC64;
MVLADLGKRI NSAVNNAISN TQDDFTTSVD VMLKGIVTAL LESDVNIALV SKLRNNIRSQ
LLSENRSEKS TTNAQTKKLI QKTVFDELCK LVTCEGSEEK AFVPKKRKTN IIMFVGLQGS
GKTTSCTKLA VYYSKRGFKV GLVCADTFRA GAFDQLKQNA IRARIPFYGS YTETDPAKVA
EEGINKFKKE KFDIIIVDTS GRHHQEEELF QEMIEISNVI KPNQTIMVLD ASIGQAAEQQ
SKAFKESSDF GAIILTKMDG HARGGGAISA VAATNTPIIF IGTGEHIHDL EKFSPKSFIS
KLLGIGDIES LFEQLQTVSN KEDAKATMEN IQKGKFTLLD FKKQMQTIMK MGPLSNIAQM
IPGMSNMMNQ VGEEETSQKM KKMVYVLDSM TKEELESDGR MFIEEPTRMV RVAKGSGTSV
FEVEMILMQQ QMMARMAQTA TQQQPGAPGA NARMPGMPNM PGMPNMPGMP NMPGMPKVTP
QMMQQAQQKL KQNPGLMQNM MNMFGGGMGG GMGGGMPDMN EMMKMMQDPQ MQQMAKQFGM
G
