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Q61009 (SCRB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Scavenger receptor class B member 1

Short name=SRB1
Alternative name(s):
SR-BI
Gene names
Name:Scarb1
Synonyms:Srb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity By similarity. Plays an important role in the uptake of HDL cholesteryl ester By similarity.

Subunit structure

The C-terminal region binds to PDZK1 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Membranecaveola; Multi-pass membrane protein By similarity. Note: Predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae By similarity.

Tissue specificity

Expressed primarily in liver and non-placental steroidogenic tissues.

Post-translational modification

N-glycosylated By similarity.

The six cysteines of the extracellular domain are all involved in intramolecular disulfide bonds.

Sequence similarities

Belongs to the CD36 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

blood vessel endothelial cell migration

Inferred from mutant phenotype PubMed 16339487. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: InterPro

cholesterol catabolic process

Inferred from direct assay PubMed 11278646. Source: MGI

cholesterol efflux

Inferred from direct assay PubMed 14718538. Source: BHF-UCL

cholesterol homeostasis

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

cholesterol import

Inferred from direct assay PubMed 14718538. Source: BHF-UCL

cholesterol transport

Inferred from direct assay PubMed 14729860PubMed 8753864. Source: MGI

detection of lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

endothelial cell proliferation

Inferred from mutant phenotype PubMed 16339487. Source: MGI

high-density lipoprotein particle clearance

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

high-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 15210842. Source: BHF-UCL

lipopolysaccharide transport

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL

phospholipid transport

Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL

positive regulation of cholesterol storage

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of triglyceride biosynthetic process

Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL

receptor-mediated endocytosis

Inferred from sequence or structural similarity PubMed 9211901. Source: GOC

recognition of apoptotic cell

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

regulation of phosphatidylcholine catabolic process

Inferred from mutant phenotype PubMed 18175806. Source: BHF-UCL

reverse cholesterol transport

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

triglyceride homeostasis

Inferred from mutant phenotype PubMed 19136670. Source: BHF-UCL

   Cellular_componentcaveola

Inferred from direct assay PubMed 9148942. Source: MGI

cell surface

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 9148942. Source: MGI

integral component of plasma membrane

Inferred from direct assay PubMed 9148942. Source: MGI

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

microvillus membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

   Molecular_functionapolipoprotein binding

Inferred from physical interaction PubMed 9254056. Source: BHF-UCL

high-density lipoprotein particle binding

Inferred from direct assay PubMed 15210959. Source: BHF-UCL

high-density lipoprotein particle receptor activity

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

lipopolysaccharide binding

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide receptor activity

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle binding

Inferred from sequence or structural similarity PubMed 9211901. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Scavenger receptor class B member 1
PRO_0000144161

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Potential
Topological domain33 – 440408Extracellular Potential
Transmembrane441 – 46121Helical; Potential
Topological domain462 – 50948Cytoplasmic Potential

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Disulfide bond251 ↔ 384 Probable

Experimental info

Sequence conflict3961S → F in BAB27068. Ref.2
Sequence conflict468 – 50942EKCFL…QEAKL → GPEDTISPPNLIAWSDQPPS PYTPLLEDSLSGQPTSAMA in BAB27068. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61009 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5CFCDD62DD6ECB1C

FASTA50956,754
        10         20         30         40         50         60 
MGGSSRARWV ALGLGALGLL FAALGVVMIL MVPSLIKQQV LKNVRIDPSS LSFGMWKEIP 

        70         80         90        100        110        120 
VPFYLSVYFF EVVNPNEVLN GQKPVVRERG PYVYREFRQK VNITFNDNDT VSFVENRSLH 

       130        140        150        160        170        180 
FQPDKSHGSE SDYIVLPNIL VLGGSILMES KPVSLKLMMT LALVTMGQRA FMNRTVGEIL 

       190        200        210        220        230        240 
WGYDDPFVHF LNTYLPDMLP IKGKFGLFVG MNNSNSGVFT VFTGVQNFSR IHLVDKWNGL 

       250        260        270        280        290        300 
SKIDYWHSEQ CNMINGTSGQ MWAPFMTPES SLEFFSPEAC RSMKLTYNES RVFEGIPTYR 

       310        320        330        340        350        360 
FTAPDTLFAN GSVYPPNEGF CPCRESGIQN VSTCRFGAPL FLSHPHFYNA DPVLSEAVLG 

       370        380        390        400        410        420 
LNPNPKEHSL FLDIHPVTGI PMNCSVKMQL SLYIKSVKGI GQTGKIEPVV LPLLWFEQSG 

       430        440        450        460        470        480 
AMGGKPLSTF YTQLVLMPQV LHYAQYVLLG LGGLLLLVPI ICQLRSQEKC FLFWSGSKKG 

       490        500 
SQDKEAIQAY SESLMSPAAK GTVLQEAKL 

« Hide

References

« Hide 'large scale' references
[1]"Identification of scavenger receptor SR-BI as a high density lipoprotein receptor."
Acton S., Rigotti A., Landschulz K.T., Xu S., Hobbs H.H., Krieger M.
Science 271:518-520(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Testis.
[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].
[4]"Extracellular disulfide bonds support scavenger receptor class B type I-mediated cholesterol transport."
Papale G.A., Hanson P.J., Sahoo D.
Biochemistry 50:6245-6254(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37799 mRNA. Translation: AAC52378.1.
AK010622 mRNA. Translation: BAB27068.1.
AK028191 mRNA. Translation: BAC25802.1.
AK033114 mRNA. Translation: BAC28157.1.
BC004656 mRNA. Translation: AAH04656.1.
CCDSCCDS19683.1.
RefSeqNP_001192011.1. NM_001205082.1.
NP_058021.1. NM_016741.2.
UniGeneMm.282242.
Mm.474018.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R69X-ray1.50A/B505-509[»]
ProteinModelPortalQ61009.
SMRQ61009. Positions 52-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-242627.

Chemistry

ChEMBLCHEMBL1741203.

PTM databases

PhosphoSiteQ61009.

Proteomic databases

MaxQBQ61009.
PaxDbQ61009.
PRIDEQ61009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000086075; ENSMUSP00000083242; ENSMUSG00000037936.
GeneID20778.
KEGGmmu:20778.
UCSCuc008zrd.2. mouse.

Organism-specific databases

CTD949.
MGIMGI:893578. Scarb1.

Phylogenomic databases

eggNOGNOG257244.
GeneTreeENSGT00530000062927.
HOGENOMHOG000252951.
HOVERGENHBG106577.
InParanoidQ61009.
KOK13885.
OMADNDTVSF.
OrthoDBEOG79SDWX.
PhylomeDBQ61009.
TreeFamTF317925.

Gene expression databases

ArrayExpressQ61009.
BgeeQ61009.
CleanExMM_SCARB1.
GenevestigatorQ61009.

Family and domain databases

InterProIPR002159. CD36.
IPR005428. CD36_antigen.
[Graphical view]
PANTHERPTHR11923. PTHR11923. 1 hit.
PfamPF01130. CD36. 1 hit.
[Graphical view]
PRINTSPR01610. CD36ANTIGEN.
PR01609. CD36FAMILY.
ProtoNetSearch...

Other

ChiTaRSSCARB1. mouse.
NextBio299499.
PROQ61009.
SOURCESearch...

Entry information

Entry nameSCRB1_MOUSE
AccessionPrimary (citable) accession number: Q61009
Secondary accession number(s): Q9CWJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 102 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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