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Protein

Signal recognition particle 54 kDa protein

Gene

Srp54

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to the signal sequence of presecretory protein when they emerge from the ribosomes and transfers them to TRAM (translocating chain-associating membrane protein).

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1158GTPBy similarity
Nucleotide bindingi190 – 1945GTPBy similarity
Nucleotide bindingi248 – 2514GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_331340. SRP-dependent cotranslational protein targeting to membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle 54 kDa protein
Short name:
SRP54
Gene namesi
Name:Srp54
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1346087. Srp54.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Signal recognition particle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Signal recognition particle 54 kDa proteinPRO_0000101194Add
BLAST

Proteomic databases

MaxQBiP14576.
PaxDbiP14576.
PRIDEiP14576.

PTM databases

PhosphoSiteiP14576.

Expressioni

Gene expression databases

BgeeiP14576.
ExpressionAtlasiP14576. baseline and differential.
GenevisibleiP14576. MM.

Interactioni

Subunit structurei

Interacts with RNPS1 (By similarity). Signal recognition particle consists of a 7S RNA molecule of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9.By similarity

Protein-protein interaction databases

BioGridi204879. 1 interaction.
IntActiP14576. 2 interactions.
MINTiMINT-247596.
STRINGi10090.ENSMUSP00000106336.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1915Combined sources
Helixi25 – 4016Combined sources
Helixi46 – 5712Combined sources
Helixi69 – 8517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY1electron microscopy12.00W326-434[»]
1WGWNMR-A4-92[»]
ProteinModelPortaliP14576.
SMRiP14576. Positions 8-488.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14576.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 295295G-domainAdd
BLAST
Regioni296 – 504209M-domainAdd
BLAST

Domaini

Has a two domain structure: the G-domain binds GTP; the M-domain binds the 7S RNA in presence of SRP19 and also binds the signal sequence.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0541.
GeneTreeiENSGT00550000074824.
HOGENOMiHOG000036165.
HOVERGENiHBG061072.
InParanoidiP14576.
KOiK03106.
OMAiMLPGMGQ.
OrthoDBiEOG747PHN.
PhylomeDBiP14576.
TreeFamiTF106249.

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]
SUPFAMiSSF47446. SSF47446. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01425. SRP54_euk. 1 hit.
PROSITEiPS00300. SRP54. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P14576-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCTALL EADVNIKLVK
60 70 80 90 100
QLRENVKSAI DLEEMASGLN KRKMIQHAVF KELVKLVDPG VKAWTPTKGK
110 120 130 140 150
QNVIMFVGLQ GSGKTTTCSK LAYYYQRKGW KTCLICADTF RAGAFDQLKQ
160 170 180 190 200
NATKARIPFY GSYTEMDPVI IASEGVEKFK NENFEIIIVD TSGRHKQEDS
210 220 230 240 250
LFEEMLQVSN AIQPDNIVYV MDASIGQACE AQAKAFKDKV DVASVIVTKL
260 270 280 290 300
DGHAKGGGAL SAVAATKSPI IFIGTGEHID DFEPFKTQPF ISKLLGMGDI
310 320 330 340 350
EGLIDKVNEL KLDDNEALIE KLKHGQFTLR DMYEQFQNIM KMGPFSQILG
360 370 380 390 400
MIPGFGTDFM SKGNEQESMA RLKKLMTIMD SMNDQELDST DGAKVFSKQP
410 420 430 440 450
GRIQRVARGS GVSTRDVQEL LTQYTKFAQM VKKMGGIKGL FKGGDMSKNV
460 470 480 490 500
SQSQMAKLNQ QMAKMMDPRV LHHMGGMAGL QSMMRQFQQG AAGNMKGMMG

FNNM
Length:504
Mass (Da):55,721
Last modified:August 16, 2005 - v2
Checksum:i79AD58BE6D1E89CA
GO
Isoform 2 (identifier: P14576-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     86-103: LVDPGVKAWTPTKGKQNV → VKVYQHYESINSVLLSPF
     104-504: Missing.

Note: No experimental confirmation available.
Show »
Length:103
Mass (Da):11,569
Checksum:i5B84FCFFD2ABEE15
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051M → R in CAA34386 (PubMed:2502718).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei86 – 10318LVDPG…GKQNV → VKVYQHYESINSVLLSPF in isoform 2. 1 PublicationVSP_014953Add
BLAST
Alternative sequencei104 – 504401Missing in isoform 2. 1 PublicationVSP_014954Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16319 mRNA. Translation: CAA34386.1.
AK010716 mRNA. Translation: BAB27138.1.
AK011928 mRNA. Translation: BAB27921.1.
AK136033 mRNA. Translation: BAE22786.1.
BC019683 mRNA. Translation: AAH19683.1.
CCDSiCCDS36449.1. [P14576-1]
CCDS49065.1. [P14576-1]
PIRiS05198.
RefSeqiNP_001093579.1. NM_001100109.1. [P14576-1]
NP_036029.2. NM_011899.4. [P14576-1]
UniGeneiMm.12848.
Mm.471968.

Genome annotation databases

EnsembliENSMUST00000021407; ENSMUSP00000021407; ENSMUSG00000073079. [P14576-1]
ENSMUST00000110708; ENSMUSP00000106336; ENSMUSG00000079108. [P14576-1]
GeneIDi24067.
665155.
KEGGimmu:24067.
mmu:665155.
UCSCiuc007nof.1. mouse. [P14576-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16319 mRNA. Translation: CAA34386.1.
AK010716 mRNA. Translation: BAB27138.1.
AK011928 mRNA. Translation: BAB27921.1.
AK136033 mRNA. Translation: BAE22786.1.
BC019683 mRNA. Translation: AAH19683.1.
CCDSiCCDS36449.1. [P14576-1]
CCDS49065.1. [P14576-1]
PIRiS05198.
RefSeqiNP_001093579.1. NM_001100109.1. [P14576-1]
NP_036029.2. NM_011899.4. [P14576-1]
UniGeneiMm.12848.
Mm.471968.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY1electron microscopy12.00W326-434[»]
1WGWNMR-A4-92[»]
ProteinModelPortaliP14576.
SMRiP14576. Positions 8-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204879. 1 interaction.
IntActiP14576. 2 interactions.
MINTiMINT-247596.
STRINGi10090.ENSMUSP00000106336.

PTM databases

PhosphoSiteiP14576.

Proteomic databases

MaxQBiP14576.
PaxDbiP14576.
PRIDEiP14576.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021407; ENSMUSP00000021407; ENSMUSG00000073079. [P14576-1]
ENSMUST00000110708; ENSMUSP00000106336; ENSMUSG00000079108. [P14576-1]
GeneIDi24067.
665155.
KEGGimmu:24067.
mmu:665155.
UCSCiuc007nof.1. mouse. [P14576-1]

Organism-specific databases

CTDi24067.
665155.
MGIiMGI:1346087. Srp54.

Phylogenomic databases

eggNOGiCOG0541.
GeneTreeiENSGT00550000074824.
HOGENOMiHOG000036165.
HOVERGENiHBG061072.
InParanoidiP14576.
KOiK03106.
OMAiMLPGMGQ.
OrthoDBiEOG747PHN.
PhylomeDBiP14576.
TreeFamiTF106249.

Enzyme and pathway databases

ReactomeiREACT_331340. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

EvolutionaryTraceiP14576.
NextBioi304041.
PROiP14576.
SOURCEiSearch...

Gene expression databases

BgeeiP14576.
ExpressionAtlasiP14576. baseline and differential.
GenevisibleiP14576. MM.

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]
SUPFAMiSSF47446. 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. "Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle."
    Bernstein H.D., Poritz M.A., Strub K., Hoben P.J., Brenner S., Walter P.
    Nature 340:482-486(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Egg, Embryo and Embryonic stem cell.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence."
    Zopf D., Bernstein H.D., Johnson A.E., Walter P.
    EMBO J. 9:4511-4517(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: M-DOMAIN RNA-BINDING.
  5. "Structure of the signal recognition particle interacting with the elongation-arrested ribosome."
    Halic M., Becker T., Pool M.R., Spahn C.M.T., Grassucci R.A., Frank J., Beckmann R.
    Nature 427:808-814(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS) OF 326-434 IN COMPLEX WITH 80S RIBOSOME.
  6. "Solution structure of the N-terminal domain of mouse putative signal recoginition particle 54 (SRP54)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 4-89.

Entry informationi

Entry nameiSRP54_MOUSE
AccessioniPrimary (citable) accession number: P14576
Secondary accession number(s): Q3UWX8, Q9CWH7, Q9D008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 16, 2005
Last modified: June 24, 2015
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.