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Protein

40S ribosomal protein SA

Gene

Rpsa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

GO - Molecular functioni

  • laminin receptor activity Source: RGD
  • structural constituent of ribosome Source: GO_Central
  • structural molecule activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus.
R-RNO-72649. Translation initiation complex formation.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein SAUniRule annotation
Alternative name(s):
37 kDa laminin receptor precursorUniRule annotation
Short name:
37LRPUniRule annotation
37/67 kDa laminin receptorUniRule annotation
Short name:
LRP/LRUniRule annotation
67 kDa laminin receptorUniRule annotation
Short name:
67LRUniRule annotation
Laminin receptor 1UniRule annotation
Short name:
LamRUniRule annotation
Laminin-binding protein precursor p40UniRule annotation
Short name:
LBP/p40UniRule annotation
Gene namesi
Name:Rpsa
Synonyms:Lamr1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi71026. Rpsa.

Subcellular locationi

  • Cell membrane UniRule annotation1 Publication
  • Cytoplasm UniRule annotation1 Publication
  • Nucleus UniRule annotation

  • 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. Colocalizes with PPP1R16B in the cell membrane (By similarity).UniRule annotation

GO - Cellular componenti

  • 90S preribosome Source: GO_Central
  • basement membrane Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • cytosolic small ribosomal subunit Source: RGD
  • extracellular matrix Source: RGD
  • membrane Source: RGD
  • neuronal cell body Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedUniRule annotation2 Publications
Chaini2 – 29529440S ribosomal protein SAPRO_0000134360Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotation2 Publications
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei97 – 971PhosphothreonineBy similarity

Post-translational modificationi

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.UniRule annotation
Cleaved by stromelysin-3 (ST3) at the cell surface. Cleavage by stromelysin-3 may be a mechanism to alter cell-extracellular matrix interactions.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei115 – 1162Cleavage; by ST3; site 1UniRule annotation
Sitei133 – 1342Cleavage; by ST3; site 2UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP38983.
PRIDEiP38983.

PTM databases

iPTMnetiP38983.
PhosphoSiteiP38983.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiENSRNOG00000018645.
GenevisibleiP38983. RN.

Interactioni

Subunit structurei

Monomer (37LRP) and homodimer (67LR). 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. Interacts with several laminins including at least LAMB1. Interacts with MDK. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B.UniRule annotation

Protein-protein interaction databases

BioGridi247913. 3 interactions.
IntActiP38983. 3 interactions.
MINTiMINT-4568881.
STRINGi10116.ENSRNOP00000025224.

Structurei

3D structure databases

ProteinModelPortaliP38983.
SMRiP38983. Positions 9-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati230 – 2323[DE]-W-[ST] 1
Repeati247 – 2493[DE]-W-[ST] 2
Repeati266 – 2683[DE]-W-[ST] 3
Repeati275 – 2773[DE]-W-[ST] 4
Repeati293 – 2953[DE]-W-[ST] 5

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 11360Interaction with PPP1R16BUniRule annotationAdd
BLAST
Regioni161 – 18020Laminin-bindingUniRule annotationAdd
BLAST
Regioni205 – 22925Laminin-bindingUniRule annotationAdd
BLAST
Regioni242 – 29554Laminin-bindingUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
HOVERGENiHBG054466.
InParanoidiP38983.
KOiK02998.
OMAiMATQREE.
OrthoDBiEOG091G0J0Q.
PhylomeDBiP38983.
TreeFamiTF300100.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_03015. Ribosomal_S2_euk. 1 hit.
MF_03016. Ribosomal_S2_laminin_receptor. 1 hit.
InterProiIPR027504. 40S_ribosomal_SA.
IPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGLDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN
60 70 80 90 100
LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA
110 120 130 140 150
GRFTPGTFTN QIQAAFREPR LLVVTDPRAD HQPLTEASYV NLPTIALCNT
160 170 180 190 200
DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD
210 220 230 240 250
LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA AQPEVADWSE
260 270 280 290
GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS
Length:295
Mass (Da):32,824
Last modified:January 23, 2007 - v3
Checksum:iD7DDD887DBDD340C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771M → V in ACJ13448 (Ref. 2) Curated
Sequence conflicti244 – 2441E → G in ACJ13448 (Ref. 2) Curated

Mass spectrometryi

Molecular mass is 32734.1±1.3 Da from positions 2 - 295. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS42405.
RefSeqiNP_058834.1. NM_017138.2.
UniGeneiRn.121972.
Rn.161973.
Rn.999.

Genome annotation databases

EnsembliENSRNOT00000025225; ENSRNOP00000025224; ENSRNOG00000018645.
GeneIDi29236.
KEGGirno:29236.
UCSCiRGD:71026. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS42405.
RefSeqiNP_058834.1. NM_017138.2.
UniGeneiRn.121972.
Rn.161973.
Rn.999.

3D structure databases

ProteinModelPortaliP38983.
SMRiP38983. Positions 9-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247913. 3 interactions.
IntActiP38983. 3 interactions.
MINTiMINT-4568881.
STRINGi10116.ENSRNOP00000025224.

PTM databases

iPTMnetiP38983.
PhosphoSiteiP38983.

Proteomic databases

PaxDbiP38983.
PRIDEiP38983.

Protocols and materials databases

DNASUi29236.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025225; ENSRNOP00000025224; ENSRNOG00000018645.
GeneIDi29236.
KEGGirno:29236.
UCSCiRGD:71026. rat.

Organism-specific databases

CTDi3921.
RGDi71026. Rpsa.

Phylogenomic databases

eggNOGiKOG0830. Eukaryota.
COG0052. LUCA.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
HOVERGENiHBG054466.
InParanoidiP38983.
KOiK02998.
OMAiMATQREE.
OrthoDBiEOG091G0J0Q.
PhylomeDBiP38983.
TreeFamiTF300100.

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-RNO-6791226. Major pathway of rRNA processing in the nucleolus.
R-RNO-72649. Translation initiation complex formation.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-RNO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-RNO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP38983.

Gene expression databases

BgeeiENSRNOG00000018645.
GenevisibleiP38983. RN.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_03015. Ribosomal_S2_euk. 1 hit.
MF_03016. Ribosomal_S2_laminin_receptor. 1 hit.
InterProiIPR027504. 40S_ribosomal_SA.
IPR032281. 40S_SA_C.
IPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF16122. 40S_SA_C. 1 hit.
PF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSSA_RAT
AccessioniPrimary (citable) accession number: P38983
Secondary accession number(s): B6ZB78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 139 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.