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O35114 (SCRB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Scarb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a lysosomal receptor for glucosylceramidase (GBA) targeting. Ref.5 Ref.7

Subunit structure

Interacts with GBA. Ref.5 Ref.7

Subcellular location

Lysosome membrane; Multi-pass membrane protein Ref.1 Ref.7.

Tissue specificity

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

Post-translational modification

Acylated by palmitic acid group(s) By similarity.

Heavily glycosylated.

Sequence similarities

Belongs to the CD36 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 478477Lysosome membrane protein 2
PRO_0000144156

Regions

Topological domain2 – 43Cytoplasmic Potential
Transmembrane5 – 2723Helical; Potential
Topological domain28 – 433406Lumenal Potential
Transmembrane434 – 45926Helical; Potential
Topological domain460 – 47819Cytoplasmic Potential
Region155 – 19137Important for interaction with GBA

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Ref.6
Glycosylation1221N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2241N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation3041N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Disulfide bond274 ↔ 329 By similarity
Disulfide bond312 ↔ 318 By similarity

Experimental info

Mutagenesis451N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis681N → Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes. Ref.7
Mutagenesis1051N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis1221N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis1551L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1561I → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1591M → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1601L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1621A → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1631Y → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1661K → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1841I → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1871L → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis1911F → D: Abolishes interaction with GBA. No effect on normal location in lysosomes. Ref.7
Mutagenesis2061N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis2241N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis2491N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis3041N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis3251N → Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes. Ref.7
Mutagenesis4001D → K: Slightly increased GBA binding. No effect on normal location in lysosomes. Ref.7
Mutagenesis4121N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7
Mutagenesis4301N → Q: Loss of glycosylation site. No effect on normal location in lysosomes. Ref.7

Sequences

Sequence LengthMass (Da)Tools
O35114 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 55724B77855470DF

FASTA47854,044
        10         20         30         40         50         60 
MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF NSWEKPPLPV 

        70         80         90        100        110        120 
YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANI QFGENGTTIS AVTNKAYVFE 

       130        140        150        160        170        180 
RNQSVGDPNV DLIRTINIPL LTVVDLAQLT LLRELIEAML KAYQQKLFVI HTVHELLWGY 

       190        200        210        220        230        240 
KDEILSLVHI FKPDVSPNFG LFYERNGTND GEYVFLTGED NYLNFSKIVE WNGKTSLDWW 

       250        260        270        280        290        300 
TTDTCNMING TDGDSFHPLI SKDEVLYLFP SDLCRSVHIT FSSFENVEGL PAFRYKVPAE 

       310        320        330        340        350        360 
ILANTSENAG FCIPEGNCMD SGVLNISICK NGAPIIMSFP HFYQADEKFV SAIKGMHPNK 

       370        380        390        400        410        420 
EEHESFVDIN PLTGIILRGA KRFQINTYVR KLDDFVETGD IRTMVFPVMY LNESVLIDKE 

       430        440        450        460        470 
TANQLKSVIN TTLVVTNIPY IIMALGVFFG LVFTWLACRG QGSMDEGTAD ERAPLIRT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36."
Neculai D., Schwake M., Ravichandran M., Zunke F., Collins R.F., Peters J., Neculai M., Plumb J., Loppnau P., Pizarro J.C., Seitova A., Trimble W.S., Saftig P., Grinstein S., Dhe-Paganon S.
Nature 504:172-176(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS19431.1.
PIRJC5670.
RefSeqNP_031670.1. NM_007644.3.
UniGeneMm.297964.

3D structure databases

ProteinModelPortalO35114.
SMRO35114. Positions 38-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35114. 6 interactions.
MINTMINT-4133971.

PTM databases

PhosphoSiteO35114.

Proteomic databases

MaxQBO35114.
PaxDbO35114.
PRIDEO35114.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031377; ENSMUSP00000031377; ENSMUSG00000029426.
GeneID12492.
KEGGmmu:12492.
UCSCuc008ydm.1. mouse.

Organism-specific databases

CTD950.
MGIMGI:1196458. Scarb2.

Phylogenomic databases

eggNOGNOG257244.
GeneTreeENSGT00530000062927.
HOGENOMHOG000252951.
HOVERGENHBG106707.
InParanoidO35114.
KOK12384.
OMALNESVHI.
OrthoDBEOG79SDWX.
PhylomeDBO35114.
TreeFamTF317925.

Gene expression databases

ArrayExpressO35114.
BgeeO35114.
CleanExMM_SCARB2.
GenevestigatorO35114.

Family and domain databases

InterProIPR002159. CD36.
IPR005429. LimpII.
[Graphical view]
PANTHERPTHR11923. PTHR11923. 1 hit.
PfamPF01130. CD36. 1 hit.
[Graphical view]
PRINTSPR01609. CD36FAMILY.
PR01611. LIMPII.
ProtoNetSearch...

Other

NextBio281416.
PROO35114.
SOURCESearch...

Entry information

Entry nameSCRB2_MOUSE
AccessionPrimary (citable) accession number: O35114
Secondary accession number(s): Q3UNF8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot