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P14206

- RSSA_MOUSE

UniProt

P14206 - RSSA_MOUSE

Protein

40S ribosomal protein SA

Gene

Rpsa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (01 May 2007)
      Previous versions | rss
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    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-10.5 PublicationsUniRule annotation

    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. structural constituent of ribosome Source: RefGenome

    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: RefGenome
    3. endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: RefGenome
    4. ribosomal small subunit assembly Source: RefGenome
    5. rRNA export from nucleus Source: RefGenome
    6. translation Source: RefGenome

    Keywords - Molecular functioni

    Receptor, Ribonucleoprotein, Ribosomal protein

    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: Chromosome 9

    Organism-specific databases

    MGIiMGI:105381. Rpsa.

    Subcellular locationi

    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. 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: RefGenome
    2. cytoplasm Source: UniProtKB
    3. cytosolic small ribosomal subunit Source: RefGenome
    4. membrane Source: MGI
    5. nucleus Source: MGI
    6. plasma membrane Source: UniProtKB
    7. small ribosomal subunit Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 29529440S ribosomal protein SAPRO_0000134359Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 PublicationUniRule annotation
    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. Sa_S2_E_A. 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

    MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN    50
    LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLKF AAATGATPIA 100
    GRFTPGTFTN QIQAAFREPR LLVVTDPRAD HQPLTEASYV NLPTIALCNT 150
    DSPLRYVDIA IPCNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD 200
    LYFYRDPEEI EKEEQAAAEK AVTKEEFQGE WTAPAPEFTA AQPEVADWSE 250
    GVQVPSVPIQ QFPTEDWSAQ PATEDWSAAP TAQATEWVGA TTEWS 295
    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:
    EMBL
    GenBank
    DDBJ
    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_006543473.1.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS23623.1.
    PIRi A29395.
    RefSeqi NP_035159.3. NM_011029.4.
    XP_006543536.1. XM_006543473.1.
    UniGenei Mm.311972.
    Mm.391708.
    Mm.4071.

    3D structure databases

    ProteinModelPortali P14206.
    SMRi P14206. Positions 9-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201107. 4 interactions.
    DIPi DIP-38089N.
    IntActi P14206. 9 interactions.
    MINTi MINT-1862996.

    Chemistry

    ChEMBLi CHEMBL1075301.

    PTM databases

    PhosphoSitei P14206.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00123604.
    P14206.
    SWISS-2DPAGE P14206.

    Proteomic databases

    MaxQBi P14206.
    PaxDbi P14206.
    PRIDEi P14206.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035105 ; ENSMUSP00000035105 ; ENSMUSG00000032518 .
    GeneIDi 102642689.
    16785.
    KEGGi mmu:102642689.
    mmu:16785.
    UCSCi uc009scd.2. mouse.

    Organism-specific databases

    CTDi 3921.
    MGIi MGI:105381. Rpsa.

    Phylogenomic databases

    eggNOGi COG0052.
    GeneTreei ENSGT00390000015036.
    HOGENOMi HOG000232073.
    HOVERGENi HBG054466.
    InParanoidi P14206.
    KOi K02998.
    OMAi TEWDVVV.
    OrthoDBi EOG73NG4F.
    PhylomeDBi P14206.
    TreeFami TF300100.

    Miscellaneous databases

    ChiTaRSi RPSA. mouse.
    NextBioi 290650.
    PROi P14206.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14206.
    CleanExi MM_RPSA.
    Genevestigatori P14206.

    Family and domain databases

    HAMAPi MF_03015. Ribosomal_S2_euk.
    MF_03016. Ribosomal_S2_laminin_receptor.
    InterProi IPR027504. 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 ]
    PANTHERi PTHR11489. PTHR11489. 1 hit.
    Pfami PF00318. Ribosomal_S2. 1 hit.
    [Graphical view ]
    PRINTSi PR00395. RIBOSOMALS2.
    SUPFAMi SSF52313. SSF52313. 1 hit.
    TIGRFAMsi TIGR01012. Sa_S2_E_A. 1 hit.
    PROSITEi PS00962. RIBOSOMAL_S2_1. 1 hit.
    PS00963. RIBOSOMAL_S2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 139 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