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O35114

- SCRB2_MOUSE

UniProt

O35114 - SCRB2_MOUSE

Protein

Lysosome membrane protein 2

Gene

Scarb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Acts as a lysosomal receptor for glucosylceramidase (GBA) targeting.2 Publications

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. receptor activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: InterPro
    2. protein targeting to lysosome Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosome membrane protein 2
    Alternative name(s):
    85 kDa lysosomal membrane sialoglycoprotein
    Short name:
    LGP85
    Lysosome membrane protein II
    Short name:
    LIMP II
    Scavenger receptor class B member 2
    Gene namesi
    Name:Scarb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1196458. Scarb2.

    Subcellular locationi

    Lysosome membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. lysosomal lumen Source: BHF-UCL
    3. lysosomal membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Lysosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi68 – 681N → Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes. 1 Publication
    Mutagenesisi105 – 1051N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi122 – 1221N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi155 – 1551L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi156 – 1561I → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi159 – 1591M → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi160 – 1601L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi162 – 1621A → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi163 – 1631Y → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi166 – 1661K → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi184 – 1841I → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi187 – 1871L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi191 – 1911F → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi206 – 2061N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi224 – 2241N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi249 – 2491N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi304 – 3041N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi325 – 3251N → Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes. 1 Publication
    Mutagenesisi400 – 4001D → K: Slightly increased GBA binding. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi412 – 4121N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication
    Mutagenesisi430 – 4301N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 478477Lysosome membrane protein 2PRO_0000144156Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)1 Publication
    Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi224 – 2241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi274 ↔ 329By similarity
    Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi312 ↔ 318By similarity
    Glycosylationi325 – 3251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Acylated by palmitic acid group(s).By similarity
    Heavily glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiO35114.
    PaxDbiO35114.
    PRIDEiO35114.

    PTM databases

    PhosphoSiteiO35114.

    Expressioni

    Tissue specificityi

    Detected in the extracts of brain, heart, lung, liver and kidney.

    Gene expression databases

    ArrayExpressiO35114.
    BgeeiO35114.
    CleanExiMM_SCARB2.
    GenevestigatoriO35114.

    Interactioni

    Subunit structurei

    Interacts with GBA.2 Publications

    Protein-protein interaction databases

    IntActiO35114. 6 interactions.
    MINTiMINT-4133971.

    Structurei

    3D structure databases

    ProteinModelPortaliO35114.
    SMRiO35114. Positions 38-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 43CytoplasmicSequence Analysis
    Topological domaini28 – 433406LumenalSequence AnalysisAdd
    BLAST
    Topological domaini460 – 47819CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723HelicalSequence AnalysisAdd
    BLAST
    Transmembranei434 – 45926HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 19137Important for interaction with GBAAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CD36 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG257244.
    GeneTreeiENSGT00530000062927.
    HOGENOMiHOG000252951.
    HOVERGENiHBG106707.
    InParanoidiO35114.
    KOiK12384.
    OMAiLNESVHI.
    OrthoDBiEOG79SDWX.
    PhylomeDBiO35114.
    TreeFamiTF317925.

    Family and domain databases

    InterProiIPR002159. CD36.
    IPR005429. LimpII.
    [Graphical view]
    PANTHERiPTHR11923. PTHR11923. 1 hit.
    PfamiPF01130. CD36. 1 hit.
    [Graphical view]
    PRINTSiPR01609. CD36FAMILY.
    PR01611. LIMPII.

    Sequencei

    Sequence statusi: Complete.

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

    O35114-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF    50
    NSWEKPPLPV YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANI 100
    QFGENGTTIS AVTNKAYVFE RNQSVGDPNV DLIRTINIPL LTVVDLAQLT 150
    LLRELIEAML KAYQQKLFVI HTVHELLWGY KDEILSLVHI FKPDVSPNFG 200
    LFYERNGTND GEYVFLTGED NYLNFSKIVE WNGKTSLDWW TTDTCNMING 250
    TDGDSFHPLI SKDEVLYLFP SDLCRSVHIT FSSFENVEGL PAFRYKVPAE 300
    ILANTSENAG FCIPEGNCMD SGVLNISICK NGAPIIMSFP HFYQADEKFV 350
    SAIKGMHPNK EEHESFVDIN PLTGIILRGA KRFQINTYVR KLDDFVETGD 400
    IRTMVFPVMY LNESVLIDKE TANQLKSVIN TTLVVTNIPY IIMALGVFFG 450
    LVFTWLACRG QGSMDEGTAD ERAPLIRT 478
    Length:478
    Mass (Da):54,044
    Last modified:January 23, 2007 - v3
    Checksum:i55724B77855470DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008553 mRNA. Translation: BAA23372.1.
    AK011123 mRNA. Translation: BAB27416.1.
    AK083038 mRNA. Translation: BAC38740.1.
    AK144235 mRNA. Translation: BAE25789.1.
    BC029073 mRNA. Translation: AAH29073.1.
    CCDSiCCDS19431.1.
    PIRiJC5670.
    RefSeqiNP_031670.1. NM_007644.3.
    UniGeneiMm.297964.

    Genome annotation databases

    EnsembliENSMUST00000031377; ENSMUSP00000031377; ENSMUSG00000029426.
    GeneIDi12492.
    KEGGimmu:12492.
    UCSCiuc008ydm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008553 mRNA. Translation: BAA23372.1 .
    AK011123 mRNA. Translation: BAB27416.1 .
    AK083038 mRNA. Translation: BAC38740.1 .
    AK144235 mRNA. Translation: BAE25789.1 .
    BC029073 mRNA. Translation: AAH29073.1 .
    CCDSi CCDS19431.1.
    PIRi JC5670.
    RefSeqi NP_031670.1. NM_007644.3.
    UniGenei Mm.297964.

    3D structure databases

    ProteinModelPortali O35114.
    SMRi O35114. Positions 38-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O35114. 6 interactions.
    MINTi MINT-4133971.

    PTM databases

    PhosphoSitei O35114.

    Proteomic databases

    MaxQBi O35114.
    PaxDbi O35114.
    PRIDEi O35114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031377 ; ENSMUSP00000031377 ; ENSMUSG00000029426 .
    GeneIDi 12492.
    KEGGi mmu:12492.
    UCSCi uc008ydm.1. mouse.

    Organism-specific databases

    CTDi 950.
    MGIi MGI:1196458. Scarb2.

    Phylogenomic databases

    eggNOGi NOG257244.
    GeneTreei ENSGT00530000062927.
    HOGENOMi HOG000252951.
    HOVERGENi HBG106707.
    InParanoidi O35114.
    KOi K12384.
    OMAi LNESVHI.
    OrthoDBi EOG79SDWX.
    PhylomeDBi O35114.
    TreeFami TF317925.

    Miscellaneous databases

    NextBioi 281416.
    PROi O35114.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O35114.
    Bgeei O35114.
    CleanExi MM_SCARB2.
    Genevestigatori O35114.

    Family and domain databases

    InterProi IPR002159. CD36.
    IPR005429. LimpII.
    [Graphical view ]
    PANTHERi PTHR11923. PTHR11923. 1 hit.
    Pfami PF01130. CD36. 1 hit.
    [Graphical view ]
    PRINTSi PR01609. CD36FAMILY.
    PR01611. LIMPII.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of a major lysosomal membrane glycoprotein, LGP85/LIMP II in mouse liver."
      Tabuchi N., Akasaki K., Sasaki T., Kanda N., Tsuji H.
      J. Biochem. 122:756-763(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION.
      Tissue: Liver.
    2. "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.
      Tissue: Liver and Spinal cord.
    3. "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: FVB/N.
      Tissue: Mammary tumor.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 276-294 AND 361-378, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase."
      Reczek D., Schwake M., Schroder J., Hughes H., Blanz J., Jin X., Brondyk W., Van Patten S., Edmunds T., Saftig P.
      Cell 131:770-783(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GBA.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
    7. Cited for: FUNCTION, INTERACTION WITH GBA, SUBCELLULAR LOCATION, REGION, MUTAGENESIS OF ASN-45; ASN-68; ASN-105; ASN-122; LEU-155; ILE-156; MET-159; LEU-160; ALA-162; TYR-163; LYS-166; ILE-184; LEU-187; PHE-191; ASN-206; ASN-224; ASN-249; ASN-304; ASN-325; ASP-400; ASN-412 AND ASN-430.

    Entry informationi

    Entry nameiSCRB2_MOUSE
    AccessioniPrimary (citable) accession number: O35114
    Secondary accession number(s): Q3UNF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 102 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3