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Protein

40S ribosomal protein SA

Gene

Rpsa

Organism
Mus musculus (Mouse)
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 (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.UniRule annotation5 Publications

Sites

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

GO - Molecular functioni

  1. laminin binding Source: MGI
  2. laminin receptor activity Source: UniProtKB-HAMAP
  3. poly(A) RNA binding Source: MGI
  4. ribosome binding Source: MGI
  5. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. cell adhesion Source: UniProtKB-HAMAP
  2. 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) Source: GO_Central
  3. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: GO_Central
  4. ribosomal small subunit assembly Source: GO_Central
  5. rRNA export from nucleus Source: GO_Central
  6. translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Receptor, Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

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 kDa oncofetal antigen
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
OFA/iLRP
Gene namesi
Name:Rpsa
Synonyms:Lamr1, P40-8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:105381. Rpsa.

Subcellular locationi

  1. Cell membrane
  2. Cytoplasm
  3. Nucleus

  4. 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). 37LRP shuttles to the nucleus upon midkine (MDK) binding.UniRule annotation

GO - Cellular componenti

  1. 90S preribosome Source: GO_Central
  2. cytoplasm Source: UniProtKB
  3. cytosolic small ribosomal subunit Source: MGI
  4. extracellular vesicular exosome Source: MGI
  5. membrane Source: MGI
  6. nucleus Source: MGI
  7. plasma membrane Source: UniProtKB
  8. small ribosomal subunit Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation1 Publication
Chaini2 – 29529440S ribosomal protein SAPRO_0000134359Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineUniRule annotation1 Publication
Modified residuei89 – 891N6-acetyllysine1 Publication
Modified residuei139 – 1391PhosphotyrosineBy 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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP14206.
PaxDbiP14206.
PRIDEiP14206.

2D gel databases

REPRODUCTION-2DPAGEIPI00123604.
P14206.
SWISS-2DPAGEP14206.

PTM databases

PhosphoSiteiP14206.

Expressioni

Gene expression databases

BgeeiP14206.
CleanExiMM_RPSA.
GenevestigatoriP14206.

Interactioni

Subunit structurei

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).UniRule annotation

Protein-protein interaction databases

BioGridi201107. 4 interactions.
DIPiDIP-38089N.
IntActiP14206. 9 interactions.
MINTiMINT-1862996.

Structurei

3D structure databases

ProteinModelPortaliP14206.
SMRiP14206. 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

eggNOGiCOG0052.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
HOVERGENiHBG054466.
InParanoidiP14206.
KOiK02998.
OMAiTEWDVVV.
OrthoDBiEOG73NG4F.
PhylomeDBiP14206.
TreeFamiTF300100.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
InterProiIPR027504. 40S_ribosomal_SA.
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.
PfamiPF00318. Ribosomal_S2. 1 hit.
[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.

P14206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGALDVLQM 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):32,838
Last modified:May 1, 2007 - v4
Checksum:iC698CFA6B759FD2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181F → L in AAA39413 (PubMed:2531008).Curated
Sequence conflicti29 – 291N → H in BAB27355 (PubMed:16141072).Curated
Sequence conflicti155 – 1551R → A in AAA39413 (PubMed:2531008).Curated
Sequence conflicti243 – 2431P → T in AAH92041 (PubMed:15489334).Curated
Sequence conflicti249 – 2491S → Y in BAC38701 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23623.1.
PIRiA29395.
RefSeqiNP_035159.3. NM_011029.4.
XP_006543536.1. XM_006543473.2.
UniGeneiMm.311972.
Mm.391708.
Mm.4071.

Genome annotation databases

EnsembliENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
GeneIDi102642689.
16785.
KEGGimmu:102642689.
mmu:16785.
UCSCiuc009scd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23623.1.
PIRiA29395.
RefSeqiNP_035159.3. NM_011029.4.
XP_006543536.1. XM_006543473.2.
UniGeneiMm.311972.
Mm.391708.
Mm.4071.

3D structure databases

ProteinModelPortaliP14206.
SMRiP14206. Positions 9-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201107. 4 interactions.
DIPiDIP-38089N.
IntActiP14206. 9 interactions.
MINTiMINT-1862996.

Chemistry

ChEMBLiCHEMBL1075301.

PTM databases

PhosphoSiteiP14206.

2D gel databases

REPRODUCTION-2DPAGEIPI00123604.
P14206.
SWISS-2DPAGEP14206.

Proteomic databases

MaxQBiP14206.
PaxDbiP14206.
PRIDEiP14206.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035105; ENSMUSP00000035105; ENSMUSG00000032518.
GeneIDi102642689.
16785.
KEGGimmu:102642689.
mmu:16785.
UCSCiuc009scd.2. mouse.

Organism-specific databases

CTDi3921.
MGIiMGI:105381. Rpsa.

Phylogenomic databases

eggNOGiCOG0052.
GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
HOVERGENiHBG054466.
InParanoidiP14206.
KOiK02998.
OMAiTEWDVVV.
OrthoDBiEOG73NG4F.
PhylomeDBiP14206.
TreeFamiTF300100.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi290650.
PROiP14206.
SOURCEiSearch...

Gene expression databases

BgeeiP14206.
CleanExiMM_RPSA.
GenevestigatoriP14206.

Family and domain databases

HAMAPiMF_03015. Ribosomal_S2_euk.
MF_03016. Ribosomal_S2_laminin_receptor.
InterProiIPR027504. 40S_ribosomal_SA.
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.
PfamiPF00318. Ribosomal_S2. 1 hit.
[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...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Hippocampus.
  10. 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. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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.
  18. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRSSA_MOUSE
AccessioniPrimary (citable) accession number: P14206
Secondary accession number(s): Q58E74
, Q8BHL0, Q8BNL2, Q91V31, Q9CY13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: May 1, 2007
Last modified: April 29, 2015
This is version 145 of the entry and version 4 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  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.