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Signal recognition particle subunit SRP54 (Signal recognition particle 54 kDa protein homolog)

 SRP54_YEAST             Reviewed;         541 AA.
P20424; D6W489;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
23-MAY-2018, entry version 171.
RecName: Full=Signal recognition particle subunit SRP54;
AltName: Full=Signal recognition particle 54 kDa protein homolog;
Name=SRP54; Synonyms=SRH1; OrderedLocusNames=YPR088C;
ORFNames=P9513.14;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
PubMed=2187859; DOI=10.1093/oxfordjournals.jbchem.a123067;
Amaya Y., Nakano A., Ito K., Mori M.;
"Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K
subunit of mammalian signal recognition particle.";
J. Biochem. 107:457-463(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2557350; DOI=10.1083/jcb.109.6.3223;
Hann B.C., Poritz M.A., Walter P.;
"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.";
J. Cell Biol. 109:3223-3230(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
RNA-BINDING.
PubMed=8382769; DOI=10.1128/MCB.13.3.1353;
Selinger D., Brennwald P., Liao X., Wise J.A.;
"Identification of RNA sequences and structural elements required for
assembly of fission yeast SRP54 protein with signal recognition
particle RNA.";
Mol. Cell. Biol. 13:1353-1362(1993).
[6]
IDENTIFICATION IN THE SRP COMPLEX.
PubMed=7925282;
Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,
Walter P.;
"Subunits of the Saccharomyces cerevisiae signal recognition particle
required for its functional expression.";
EMBO J. 13:4390-4400(1994).
[7]
FUNCTION.
PubMed=8805251; DOI=10.1016/S0960-9822(02)00484-0;
Powers T., Walter P.;
"The nascent polypeptide-associated complex modulates interactions
between the signal recognition particle and the ribosome.";
Curr. Biol. 6:331-338(1996).
[8]
FUNCTION.
PubMed=10676815; DOI=10.1016/S0092-8674(00)80669-8;
Song W., Raden D., Mandon E.C., Gilmore R.;
"Role of Sec61alpha in the regulated transfer of the ribosome-nascent
chain complex from the signal recognition particle to the
translocation channel.";
Cell 100:333-343(2000).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10676815, ECO:0000269|PubMed:8805251}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:7925282}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
domain binds the 7S RNA and also binds the signal sequence.
-!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X16908; CAA34781.1; -; Genomic_DNA.
EMBL; M55517; AAA35092.1; -; Genomic_DNA.
EMBL; X51614; CAA35952.1; -; Genomic_DNA.
EMBL; U51033; AAB68136.1; -; Genomic_DNA.
EMBL; BK006949; DAA11505.1; -; Genomic_DNA.
PIR; S69073; JX0112.
RefSeq; NP_015413.1; NM_001184185.1.
ProteinModelPortal; P20424; -.
SMR; P20424; -.
BioGrid; 36258; 269.
DIP; DIP-2943N; -.
IntAct; P20424; 23.
MINT; P20424; -.
STRING; 4932.YPR088C; -.
iPTMnet; P20424; -.
MaxQB; P20424; -.
PaxDb; P20424; -.
PRIDE; P20424; -.
EnsemblFungi; YPR088C; YPR088C; YPR088C.
GeneID; 856203; -.
KEGG; sce:YPR088C; -.
EuPathDB; FungiDB:YPR088C; -.
SGD; S000006292; SRP54.
GeneTree; ENSGT00550000074824; -.
HOGENOM; HOG000036165; -.
InParanoid; P20424; -.
KO; K03106; -.
OMA; DTAGRHK; -.
OrthoDB; EOG092C1WCZ; -.
BioCyc; YEAST:G3O-34231-MONOMER; -.
PRO; PR:P20424; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
GO; GO:0008312; F:7S RNA binding; IDA:SGD.
GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; ISS:SGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IMP:SGD.
GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
Gene3D; 1.10.260.30; -; 1.
HAMAP; MF_00306; SRP54; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
InterPro; IPR004125; Signal_recog_particle_SRP54_M.
InterPro; IPR036225; SRP/SRP_N.
InterPro; IPR022941; SRP54.
InterPro; IPR006325; SRP54_euk.
InterPro; IPR000897; SRP54_GTPase_dom.
PANTHER; PTHR11564; PTHR11564; 1.
Pfam; PF00448; SRP54; 1.
Pfam; PF02881; SRP54_N; 1.
Pfam; PF02978; SRP_SPB; 1.
SMART; SM00382; AAA; 1.
SMART; SM00962; SRP54; 1.
SMART; SM00963; SRP54_N; 1.
SUPFAM; SSF47364; SSF47364; 1.
SUPFAM; SSF47446; SSF47446; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01425; SRP54_euk; 1.
PROSITE; PS00300; SRP54; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; GTP-binding; GTPase activation;
Nucleotide-binding; Reference proteome; Ribonucleoprotein;
RNA-binding; Signal recognition particle.
CHAIN 1 541 Signal recognition particle subunit
SRP54.
/FTId=PRO_0000101203.
NP_BIND 116 123 GTP. {ECO:0000250}.
NP_BIND 198 202 GTP. {ECO:0000250}.
NP_BIND 256 259 GTP. {ECO:0000250}.
REGION 1 303 G-domain.
REGION 304 541 M-domain.
CONFLICT 136 136 R -> E (in Ref. 1; CAA34781).
{ECO:0000305}.
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


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