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O35114

- SCRB2_MOUSE

UniProt

O35114 - SCRB2_MOUSE

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Protein
Lysosome membrane protein 2
Gene
Scarb2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 43Cytoplasmic Reviewed prediction
Transmembranei5 – 2723Helical; Reviewed prediction
Add
BLAST
Topological domaini28 – 433406Lumenal Reviewed prediction
Add
BLAST
Transmembranei434 – 45926Helical; Reviewed prediction
Add
BLAST
Topological domaini460 – 47819Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 – 11Removed By similarity
Chaini2 – 478477Lysosome membrane protein 2
PRO_0000144156Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the CD36 family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 101 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

Similar proteinsi