P14206 (RSSA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein SA

Alternative name(s):
37 kDa laminin receptor precursor
Short name=37LRP
37 kDa oncofetal antigen
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
OFA/iLRP

Gene names

Name:	Rpsa
Synonyms:	Lamr1, P40-8

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Enables malignant tumor cells to penetrate laminin tissue and vessel barriers. Activates precursor thymic anti-OFA/iLRP specific cytotoxic T-cell. May induce CD8 T-suppressor cells secreting IL-10. Ref.3 Ref.10 Ref.11 Ref.12 Ref.13
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. Interacts with MDK. Interacts with PRNP. The mature dimeric form interacts with PPP1R16B (via its fourth ankyrin repeat). Interacts with PPP1CA only in the presence of PPP1R16B By similarity. Ref.11 Ref.12 Ref.14 Ref.15
Subcellular location	Cell membrane. Cytoplasm. Nucleus. 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. 37LRP shuttles to the nucleus upon midkine (MDK) binding. Ref.8 Ref.10 Ref.13 Ref.14 Ref.15 Ref.16
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. HAMAP-Rule MF_03016 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. HAMAP-Rule MF_03016
Miscellaneous	This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. HAMAP-Rule MF_03016 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. HAMAP-Rule MF_03016
Sequence similarities	Belongs to the ribosomal protein S2P family.

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	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 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 cytosolic small ribosomal subunit Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay PubMed 2146686. Source: MGI plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	laminin binding Inferred from direct assay PubMed 8452943. Source: MGI 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	1	1	Removed Ref.7
	Chain	2 – 295	294	40S ribosomal protein SA HAMAP-Rule MF_03016		PRO_0000134359
Regions
	Repeat	230 – 232	3	[DE]-W-[ST] 1 HAMAP-Rule MF_03016
	Repeat	247 – 249	3	[DE]-W-[ST] 2 HAMAP-Rule MF_03016
	Repeat	266 – 268	3	[DE]-W-[ST] 3 HAMAP-Rule MF_03016
	Repeat	275 – 277	3	[DE]-W-[ST] 4 HAMAP-Rule MF_03016
	Repeat	293 – 295	3	[DE]-W-[ST] 5 HAMAP-Rule MF_03016
	Region	54 – 113	60	Interaction with PPP1R16B By similarity
	Region	161 – 180	20	Laminin-binding By similarity
	Region	205 – 229	25	Laminin-binding By similarity
	Region	242 – 295	54	Laminin-binding By similarity
Sites
	Site	115 – 116	2	Cleavage; by ST3; site 1 By similarity
	Site	133 – 134	2	Cleavage; by ST3; site 2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.7
	Modified residue	43	1	Phosphoserine Ref.17
	Modified residue	52	1	N6-acetyllysine By similarity
	Modified residue	139	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	18	1	F → L in AAA39413. Ref.1
	Sequence conflict	29	1	N → H in BAB27355. Ref.5
	Sequence conflict	155	1	R → A in AAA39413. Ref.1
	Sequence conflict	243	1	P → T in AAH92041. Ref.6
	Sequence conflict	249	1	S → Y in BAC38701. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P14206 [UniParc]. Last modified May 1, 2007. Version 4. Checksum: C698CFA6B759FD2E	FASTA	295	32,838
	10 20 30 40 50 60 MSGALDVLQM 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor." Rao C.N., Castronovo V., Schmitt M.C., Wewer U.M., Claysmith A.P., Liotta L.A., Sobel M.E. Biochemistry 28:7476-7486(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence for a major messenger RNA for a 40 kilodalton polypeptide that is under translational control in mouse tumor cells." Makrides S., Chitpatima S.T., Bandyopadhyay R., Brawerman G. Nucleic Acids Res. 16:2349-2349(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"37 kilodalton oncofetal antigen protein and immature laminin receptor protein are identical, universal T-cell inducing immunogens on primary rodent and human cancers." Coggin J.H. Jr., Barsoum A.L., Rohrer J.W. Anticancer Res. 19:5535-5542(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: BALB/c. Tissue: Fibrosarcoma.
[4]	"Genomic sequence analysis of laminin receptor loci in mice." Lee I.Y., Baxter D.H., Qin S., Hood L.E. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CAST/Ei and SJL/J.
[5]	"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]. Strain: C57BL/6J and NOD. Tissue: Liver, Muellerian duct, Pancreas, Spleen and Thymus.
[6]	"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]. Strain: C57BL/6, Czech II and FVB/N. Tissue: Brain, Colon, Eye, Kidney, Mammary gland, Mammary tumor and Pancreas.
[7]	Kanor S., Quadroni M., Bienvenut W.V. Submitted (MAR-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Strain: C57BL/6J. Tissue: Skeletal muscle.
[8]	"Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40)." Sato M., Kinoshita K., Kaneda Y., Saeki Y., Iwamatsu A., Tanaka K. Biochem. Biophys. Res. Commun. 229:896-901(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-40; 43-50; 90-100 AND 155-163, SUBCELLULAR LOCATION.
[9]	Lubec G., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 64-80; 90-117 AND 129-155, MASS SPECTROMETRY. Tissue: Brain and Hippocampus.
[10]	"Isolation of a tumor cell laminin receptor." Rao N.C., Barsky S.H., Terranova V.P., Liotta L.A. Biochem. Biophys. Res. Commun. 111:804-808(1983) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS LAMININ RECEPTOR, SUBCELLULAR LOCATION.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
[12]	"Isolation of a cell surface receptor protein for laminin from murine fibrosarcoma cells." Malinoff H.L., Wicha M.S. J. Cell Biol. 96:1475-1479(1983) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LAMININ-1.
[13]	"A 33-kDa polypeptide with homology to the laminin receptor: component of translation machinery." Auth D., Brawerman G. Proc. Natl. Acad. Sci. U.S.A. 89:4368-4372(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN RIBOSOME, SUBCELLULAR LOCATION.
[14]	"The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein." Gauczynski S., Peyrin J.-M., Haik S., Leucht C., Hundt C., Rieger R., Krasemann S., Deslys J.-P., Dormont D., Lasmezas C.I., Weiss S. EMBO J. 20:5863-5875(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRNP, SUBCELLULAR LOCATION.
[15]	"Midkine binds to 37-kDa laminin binding protein precursor, leading to nuclear transport of the complex." Salama R.H.M., Muramatsu H., Zou K., Inui T., Kimura T., Muramatsu T. Exp. Cell Res. 270:13-20(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MDK, SUBCELLULAR LOCATION.
[16]	"Subcellular localization of prion proteins and the 37 kDa/67 kDa laminin receptor fused to fluorescent proteins." Nikles D., Vana K., Gauczynski S., Knetsch H., Ludewigs H., Weiss S. Biochim. Biophys. Acta 1782:335-340(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02870 mRNA. Translation: AAA39413.1. X06406 mRNA. Translation: CAA29696.1. AF140348 mRNA. Translation: AAD26866.1. DQ360291 Genomic DNA. Translation: ABC95972.1. DQ360292 Genomic DNA. Translation: ABC95977.1. AK010423 mRNA. Translation: BAB26926.1. AK010985 mRNA. Translation: BAB27306.1. AK011041 mRNA. Translation: BAB27353.1. AK011043 mRNA. Translation: BAB27355.1. AK075778 mRNA. Translation: BAC35952.1. AK075790 mRNA. Translation: BAC35960.1. AK082935 mRNA. Translation: BAC38701.1. AK088954 mRNA. Translation: BAC40671.1. AK134224 mRNA. Translation: BAE22057.1. AK135488 mRNA. Translation: BAE22550.1. AK160551 mRNA. Translation: BAE35867.1. AK160625 mRNA. Translation: BAE35924.1. AK165219 mRNA. Translation: BAE38083.1. AK166697 mRNA. Translation: BAE38953.1. AK166874 mRNA. Translation: BAE39085.1. AK167132 mRNA. Translation: BAE39278.1. BC003829 mRNA. Translation: AAH03829.1. BC037195 mRNA. Translation: AAH37195.1. BC055886 mRNA. Translation: AAH55886.1. BC081461 mRNA. Translation: AAH81461.1. BC084677 mRNA. Translation: AAH84677.1. BC092041 mRNA. Translation: AAH92041.1. BC094902 mRNA. Translation: AAH94902.1. BC099601 mRNA. Translation: AAH99601.1. BC110285 mRNA. Translation: AAI10286.1.
IPI	IPI00123604.
PIR	A29395.
RefSeq	NP_035159.3. NM_011029.4. XP_003086186.1. XM_003086138.3.
UniGene	Mm.311972. Mm.391708. Mm.4071.
3D structure databases
ProteinModelPortal	P14206.
SMR	P14206. Positions 9-205.
ModBase	Search...
Protein-protein interaction databases
IntAct	P14206. 5 interactions.
PTM databases
PhosphoSite	P14206.
2D gel databases
REPRODUCTION-2DPAGE	IPI00123604. P14206.
SWISS-2DPAGE	P14206.
Proteomic databases
PaxDb	P14206.
PRIDE	P14206.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
GeneID	100505031. 16785.
KEGG	mmu:100505031. mmu:16785.
UCSC	uc009scd.2. mouse.
Organism-specific databases
CTD	3921.
MGI	MGI:105381. Rpsa.
Phylogenomic databases
eggNOG	COG0052.
GeneTree	ENSGT00390000015036.
HOGENOM	HOG000232073.
HOVERGEN	HBG054466.
InParanoid	P14206.
KO	K02998.
OMA	ENVNFQM.
OrthoDB	EOG40ZQZ6.
Gene expression databases
Bgee	P14206.
CleanEx	MM_RPSA.
Genevestigator	P14206.
GermOnline	ENSMUSG00000032518. Mus musculus.
Family and domain databases
HAMAP	MF_03015. Ribosomal_S2_euk. MF_03016. Ribosomal_S2-laminin_receptor.
InterPro	IPR001865. Ribosomal_S2. IPR018130. Ribosomal_S2_CS. IPR005707. Ribosomal_S2_euk/arc. IPR023591. Ribosomal_S2_flav_dom. [Graphical view]
PANTHER	PTHR11489. PTHR11489. 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
ChEMBL	CHEMBL1075301.
ChiTaRS	RPSA. mouse.
NextBio	290650.
SOURCE	Search...

Entry information

Entry name

RSSA_MOUSE

Accession

Primary (citable) accession number: P14206
Secondary accession number(s): Q58E74 , Q8BHL0, Q8BNL2, Q91V31, Q9CY13

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program