40S ribosomal protein SA (RPSA)

The protein contains 295 amino acids for an estimated molecular weight of 32854 Da.

 

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. Acts as a PPP1R16B-dependent substrate of PPP1CA.', '(Microbial infection) Acts as a receptor for the Adeno-associated viruses 2,3,8 and 9.', '(Microbial infection) Acts as a receptor for the Dengue virus.', '(Microbial infection) Acts as a receptor for the Sindbis virus.', '(Microbial infection) Acts as a receptor for the Venezuelan equine encephalitis virus.', '(Microbial infection) Acts as a receptor for the pathogenic prion protein.', '(Microbial infection) Acts as a receptor for bacteria. (updated: March 28, 2018)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 100
MODL_I-TASSER-3.0

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VariantDescription
dbSNP:rs17856150
ICAS
ICAS
ICAS
ICAS
dbSNP:rs1214087389
ICAS
dbSNP:rs369708612
dbSNP:rs143085301

The reference OMIM entry for this protein is 150370

Ribosomal protein sa; rpsa
Laminin receptor 1; lamr1
Lambr
Laminin receptor, 67-kd; 67lr

CLONING

Gehlsen et al. (1988) isolated a receptor for the adhesive basement membrane protein laminin (150290, 150310, 150320) from human glioblastoma cells by affinity chromatography on laminin. These RuGli glioblastoma cells were later shown to be rat cells (Gehlsen et al., 1988). This receptor has a heterodimeric structure similar to that of receptors for other extracellular matrix proteins such as the fibronectin (135620) and vitronectin (193210) receptors. Incorporation of the laminin receptor into lysosomal membranes made it possible for lysosomes to attach to surfaces coated with laminin. Bignon et al. (1991) cloned 2 cDNAs for the human 67-kD laminin receptor. They found that these clones hybridize to many restriction fragments in Southern blot analyses in the human. The particular patterns were accounted for by the presence of up to 16 and 21 copies of the laminin receptor gene per haploid genome in human and mouse, respectively. In contrast, a single gene copy was found in the chicken. Yow et al. (1988) cloned a human colon carcinoma cDNA encoding a laminin-binding protein. The cDNA hybridized to a 1.2-kb transcript, the level of which was approximately 9-fold higher in colon carcinoma than in adjacent normal colonic epithelium. The deduced 295-amino acid protein has a highly negatively charged C-terminal segment and lacks consensus sequences for an N-terminal signal sequence, amphipathic alpha-helices, and N-glycosylation sites. Satoh et al. (1992) cloned cDNAs encoding the 67-kD laminin receptor from both a human lung cell line and a human lung cancer cell line. They demonstrated that the level of the laminin receptor transcript was higher in the lung cancer cell line than in the lung cell line. Tohgo et al. (1994) found that the amino acid sequence of the rat 40S ribosomal subunit is 99% identical to that of the human 68-kD laminin-binding protein, indicating that the 40S ribosomal subunit is identical to the 68-kD laminin-binding protein.

MAPPING

By fluorescence in situ hybridization, Jackers et al. (1996) localized the LAMR1 gene to chromosome 3p21.3. Kenmochi et al. (1998) mapped the LAMR1 gene, which they called RPSA, to 3p by somatic cell hybrid and radiation hybrid mapping panels. Bignon et al. (1991) identified laminin receptor pseudogenes on chromosomes 3, 12, 14, and X. The features suggested that the laminin receptor gene belongs to a retroposon family in mammals. Lafreniere et al. (1993) demonstrated that a laminin receptor pseudogene, which they symbolized LAMRP4, is located at Xq13 in a 2.6-Mb segment that also contains the XIST gene (314670).

GENE STRUCTURE

The 37-kD precursor of the 67-kD laminin receptor (37LRP) is a polypeptide whose expression is consistently upregulated in aggressive carcinoma. It appears to be a multifunctional protein involved in the translational machinery; it has also been identified as p40 ribosome-associated protein. Jackers et al. (1996) isolated the active 37LRP/p40 human gene. They found that it contains 7 exons. Ribonuclease protection experiments suggested multiple transcription start sites. The promoter area does not bear a TATA box but contains 4 Sp1 sites. The first intron is also GC-rich, containing 5 Sp1 sites. Intron 4 contains a full sequence of the small nucleolar E2 RNA (RNE2; 180646) between nucleotides 4365 and 4516, and intron 3 contains 2 Alu sequences.

GENE FUNCTION

Montuori et al. (1999) investigated the expression of in ... More on the omim web site

Subscribe to this protein entry history

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 16, 2018: Protein entry updated
Automatic update: model status changed

April 12, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 5, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 26, 2017: Protein entry updated
Automatic update: model status changed

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for RPSA

March 15, 2016: Protein entry updated
Automatic update: OMIM entry 150370 was added.

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed