40S ribosomal protein SA - Rattus norvegicus (Rat)

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P38983 (RSSA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
40S ribosomal protein SA

Alternative name(s):
37 kDa laminin receptor precursor
Short name=37LRP
37/67 kDa laminin receptor
Short name=LRP/LR
67 kDa laminin receptor
Short name=67LR
Laminin receptor 1
Short name=LamR
Laminin-binding protein precursor p40
Short name=LBP/p40

Gene names

Name:	Rpsa
Synonyms:	Lamr1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA By similarity. Ref.9
Subunit structure	Monomer (37LRP) and homodimer (67LR) By similarity. Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S). Interacts with RPS21 By similarity. Interacts with several laminins including at least LAMB1 By similarity. Interacts with MDK By similarity. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B By similarity. Ref.8
Subcellular location	Cell membrane. Cytoplasm. Nucleus By similarity. Note: 67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus. Co-localizes with PPP1R16B in the cell membrane By similarity. Ref.4
Tissue specificity	Expressed in most neurons and in a subset of glial cells. The overall distribution of LR correlates with that reported for laminin-1 but also with brain regions classically associated with prion-related neurodegeneration. Ref.4
Post-translational modification	Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association By similarity. Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions By similarity.
Miscellaneous	This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. It is thought that in vertebrates 37/67 kDa laminin receptor acquired a dual function during evolution. It developed from the ribosomal protein SA, playing an essential role in the protein biosynthesis lacking any laminin binding activity, to a cell surface receptor with laminin binding activity.
Sequence similarities	Belongs to the ribosomal protein S2P family.
Mass spectrometry	Molecular mass is 32734.1±1.3 Da from positions 2 - 295. Determined by ESI. Ref.10

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Domain	Repeat
Molecular function	Receptor Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell-cell adhesion Inferred from direct assay. Source: RGD endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from Biological aspect of Ancestor. Source: RefGenome endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from Biological aspect of Ancestor. Source: RefGenome epithelial cell differentiation Inferred from expression pattern Ref.6. Source: RGD rRNA export from nucleus Inferred from Biological aspect of Ancestor. Source: RefGenome ribosomal small subunit assembly Inferred from Biological aspect of Ancestor. Source: RefGenome translation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	90S preribosome Inferred from Biological aspect of Ancestor. Source: RefGenome basement membrane Inferred from direct assay. Source: RGD cytosolic small ribosomal subunit Inferred from direct assay Ref.1 Ref.8. Source: RGD membrane fraction Inferred from direct assay Ref.4. Source: RGD neuronal cell body Inferred from direct assay Ref.4. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	laminin receptor activity Traceable author statement Ref.6. Source: RGD structural constituent of ribosome Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 295

294

40S ribosomal protein SA

PRO_0000134360

Regions

Repeat

230 – 232

[DE]-W-[ST] 1

Repeat

247 – 249

[DE]-W-[ST] 2

Repeat

266 – 268

[DE]-W-[ST] 3

Repeat

275 – 277

[DE]-W-[ST] 4

Repeat

293 – 295

[DE]-W-[ST] 5

Region

54 – 113

Interaction with PPP1R16B By similarity

Region

161 – 180

Laminin-binding By similarity

Region

205 – 229

Laminin-binding By similarity

Region

242 – 295

Laminin-binding By similarity

Sites

Site

115 – 116

Cleavage; by ST3; site 1 By similarity

Site

133 – 134

Cleavage; by ST3; site 2 By similarity

Amino acid modifications

Modified residue

N-acetylserine Ref.4 Ref.5

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

139

Phosphotyrosine By similarity

Experimental info

Sequence conflict

177

M → V in ACJ13448. Ref.2

Sequence conflict

244

E → G in ACJ13448. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P38983 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D7DDD887DBDD340C
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FASTA

295

32,824

        10         20         30         40         50         60 
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL 

        70         80         90        100        110        120 
AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA GRFTPGTFTN QIQAAFREPR 

       130        140        150        160        170        180 
LLVVTDPRAD HQPLTEASYV NLPTIALCNT DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR 

       190        200        210        220        230        240 
EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA 

       250        260        270        280        290 
AQPEVADWSE GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural determination and characterization of a 40 kDa protein isolated from rat 40 S ribosomal subunit." Tohgo A., Takasawa S., Munakata H., Yonekura H., Hayashi N., Okamoto H. FEBS Lett. 340:133-138(1994) [PubMed: 8119397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Wistar. Tissue: Liver.
[2]	"Cloning and analysis of laminin receptor gene in SD rat." Ning Z., Luo M. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[4]	"Cellular prion protein/laminin receptor: distribution in adult central nervous system and characterization of an isoform associated with a subtype of cortical neurons." Baloui H., von Boxberg Y., Vinh J., Weiss S., Rossier J., Nothias F., Stettler O. Eur. J. Neurosci. 20:2605-2616(2004) [PubMed: 15548204] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 43-52; 90-102 AND 156-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	Bienvenut W.V., von Kriegsheim A., Kolch W. Submitted (JUN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 64-80; 90-102; 121-128 AND 156-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Fibroblast.
[6]	"Laminin receptor expression in rat intestine and liver during development and differentiation." Rao M., Manishen W.J., Maheshwari Y., Sykes D.E., Siyanova E.Y., Tyner A.L., Weiser M.M. Gastroenterology 107:764-772(1994) [PubMed: 8076763] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 199-295. Strain: Holtzman. Tissue: Intestinal epithelium.
[7]	Burns F.R., Rajnavolgy E., Yamashita K., Li X., Shen N., Heber-Katz E. Submitted (SEP-1989) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-295.
[8]	"Isolation of eukaryotic ribosomal proteins. Purification and characterization of the 40 S ribosomal subunit proteins Sa, Sc, S3a, S3b, S5', S9, S10, S11, S12, S14, S15, S15', S16, S17, S18, S19, S20, S21, S26, S27', and S29." Collatz E., Ulbrich N., Tsurugi K., Lightfoot H.N., MacKinlay W., Lin A., Wool I.G. J. Biol. Chem. 252:9071-9080(1977) [PubMed: 925037] [Abstract] Cited for: IDENTIFICATION IN SMALL RIBOSOMAL SUBUNIT.
[9]	"Isolation of a laminin-binding protein from muscle cell membranes." Lesot H., Kuehl U., von der Mark K. EMBO J. 2:861-865(1983) [PubMed: 16453457] [Abstract] Cited for: FUNCTION.
[10]	"Mass spectrometric analysis of 40 S ribosomal proteins from Rat-1 fibroblasts." Louie D.F., Resing K.A., Lewis T.S., Ahn N.G. J. Biol. Chem. 271:28189-28198(1996) [PubMed: 8910435] [Abstract] Cited for: MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D25224 mRNA. Translation: BAA04953.1. FJ386454 mRNA. Translation: ACJ13448.1. BC060578 mRNA. Translation: AAH60578.1. U04942 mRNA. Translation: AAB60453.1. M27798 mRNA. Translation: AAA41509.1.
IPI	IPI00215107.
PIR	S42405.
RefSeq	NP_058834.1. NM_017138.1.
UniGene	Rn.121972. Rn.161973. Rn.999.
3D structure databases
ProteinModelPortal	P38983.
SMR	P38983. Positions 9-205.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38983. 2 interactions.
MINT	MINT-4568881.
STRING	P38983.
PTM databases
PhosphoSite	P38983.
Proteomic databases
PRIDE	P38983.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000025225; ENSRNOP00000025224; ENSRNOG00000018645.
GeneID	29236.
KEGG	rno:29236.
NMPDR	fig\|10116.3.peg.29466.
UCSC	NM_017138. rat.
Organism-specific databases
CTD	3921.
RGD	71026. Rpsa.
Phylogenomic databases
eggNOG	maNOG11981.
GeneTree	ENSGT00390000015036.
HOVERGEN	HBG054466.
InParanoid	P38983.
OMA	TDAQAIK.
OrthoDB	EOG40ZQZ6.
PhylomeDB	P38983.
Gene expression databases
ArrayExpress	P38983.
Genevestigator	P38983.
GermOnline	ENSRNOG00000018645. Rattus norvegicus.
Family and domain databases
InterPro	IPR001865. Ribosomal_S2. IPR018130. Ribosomal_S2_CS. IPR005707. Ribosomal_S2_euk/arc. IPR023591. Ribosomal_S2_flav_dom. [Graphical view]
KO	K02998.
PANTHER	PTHR11489. Ribosomal_S2_e/a. 1 hit.
Pfam	PF00318. Ribosomal_S2. 1 hit. [Graphical view]
PRINTS	PR00395. RIBOSOMALS2.
SUPFAM	SSF52313. Ribosomal_S2. 1 hit.
TIGRFAMs	TIGR01012. Sa_S2_E_A. 1 hit.
PROSITE	PS00962. RIBOSOMAL_S2_1. 1 hit. PS00963. RIBOSOMAL_S2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	608498.

Entry information

Entry name

RSSA_RAT

Accession

Primary (citable) accession number: P38983
Secondary accession number(s): B6ZB78

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents