Reviewed, UniProtKB/Swiss-Prot P20424 (SRP54_YEAST)

Names and origin

Protein names

Recommended name:
    Signal recognition particle subunit SRP54
Alternative name(s):
    Signal recognition particle 54 kDa protein homolog

Gene names

Name:	SRP54
Synonyms:	SRH1
Ordered Locus Names:	YPR088C
ORF Names:	P9513.14

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. Ref.6 Ref.7
Subunit structure	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.
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.
Sequence similarities	Belongs to the GTP-binding SRP family.

Ontologies

Keywords
Cellular component	Cytoplasm Signal recognition particle
Ligand	GTP-binding Nucleotide-binding RNA-binding
Molecular function	GTPase activation Ribonucleoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition Ref.5 Inferred by curator. Source: SGD
Cellular component	signal recognition particle, endoplasmic reticulum targeting Ref.5 Inferred from direct assay. Source: SGD
Molecular function	7S RNA binding Inferred from direct assay. Source: SGD GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct signal sequence binding Ref.5 Inferred from physical interaction. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADE2	P21264	1	EBI-17997,EBI-14252

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 541	541	Signal recognition particle subunit SRP54		PRO_0000101203
Regions
	Nucleotide binding	116 – 123	8	GTP By similarity
	Nucleotide binding	198 – 202	5	GTP By similarity
	Nucleotide binding	256 – 259	4	GTP By similarity
	Region	1 – 303	303	G-domain
	Region	304 – 541	238	M-domain
Experimental info
	Sequence conflict	136	1	R → E in CAA34781. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20424-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 05B1B2C262932F17	FASTA	541	59,624
	10 20 30 40 50 60 MVLADLGKRI NSAVNNAISN TQDDFTTSVD VMLKGIVTAL LESDVNIALV SKLRNNIRSQ 70 80 90 100 110 120 LLSENRSEKS TTNAQTKKLI QKTVFDELCK LVTCEGSEEK AFVPKKRKTN IIMFVGLQGS 130 140 150 160 170 180 GKTTSCTKLA VYYSKRGFKV GLVCADTFRA GAFDQLKQNA IRARIPFYGS YTETDPAKVA 190 200 210 220 230 240 EEGINKFKKE KFDIIIVDTS GRHHQEEELF QEMIEISNVI KPNQTIMVLD ASIGQAAEQQ 250 260 270 280 290 300 SKAFKESSDF GAIILTKMDG HARGGGAISA VAATNTPIIF IGTGEHIHDL EKFSPKSFIS 310 320 330 340 350 360 KLLGIGDIES LFEQLQTVSN KEDAKATMEN IQKGKFTLLD FKKQMQTIMK MGPLSNIAQM 370 380 390 400 410 420 IPGMSNMMNQ VGEEETSQKM KKMVYVLDSM TKEELESDGR MFIEEPTRMV RVAKGSGTSV 430 440 450 460 470 480 FEVEMILMQQ QMMARMAQTA TQQQPGAPGA NARMPGMPNM PGMPNMPGMP NMPGMPKVTP 490 500 510 520 530 540 QMMQQAQQKL KQNPGLMQNM MNMFGGGMGG GMGGGMPDMN EMMKMMQDPQ MQQMAKQFGM G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2187859] [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: 2557350] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 8382769] [Abstract] Cited for: RNA-BINDING.
[5]	"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: 7925282] [Abstract] Cited for: IDENTIFICATION IN THE SRP COMPLEX.
[6]	"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: 8805251] [Abstract] Cited for: FUNCTION.
[7]	"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: 10676815] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X16908 Genomic DNA. Translation: CAA34781.1. M55517 Genomic DNA. Translation: AAA35092.1. X51614 Genomic DNA. Translation: CAA35952.1. U51033 Genomic DNA. Translation: AAB68136.1.
PIR	JX0112. S69073.
RefSeq	NP_015413.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2943N.
IntAct	P20424. 24 interactions.
STRING	P20424.
Proteomic databases
PeptideAtlas	P20424.
PRIDE	P20424.
Genome annotation databases
Ensembl	YPR088C; YPR088C; YPR088C; Saccharomyces cerevisiae. [Genome view]
GeneID	856203.
KEGG	sce:YPR088C.
NMPDR	fig|4932.3.peg.6550.
Organism-specific databases
CYGD	YPR088c.
SGD	S000006292. SRP54.
Phylogenomic databases
HOGENOM	P20424.
OMA	GMPNMPG
OrthoDB	EOG9N5XDB
Gene expression databases
ArrayExpress	P20424.
Genevestigator	P20424.
GermOnline	YPR088C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR000897. Signal_recog_part_SRP54_GTPase. IPR013822. Signal_recog_particl_SRP54_hlx. IPR006325. Signal_recog_particle_SRP54. IPR004125. Signal_recog_particle_SRP54_M. [Graphical view]
Gene3D	G3DSA:1.20.120.140. SRP54_helical. 1 hit. G3DSA:1.10.260.30. SRP54_M. 1 hit.
Pfam	PF00448. SRP54. 1 hit. PF02881. SRP54_N. 1 hit. PF02978. SRP_SPB. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR01425. SRP54_euk. 1 hit.
PROSITE	PS00300. SRP54. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	981405.

Entry information

Entry name

SRP54_YEAST

Accession

Primary (citable) accession number: P20424

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	October 1, 1996
Last modified:	November 24, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)