Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30204 (MSRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage scavenger receptor types I and II
Alternative name(s):
Macrophage acetylated LDL receptor I and II
Scavenger receptor type A
Short name=SR-A
CD_antigen=CD204
Gene names
Name:Msr1
Synonyms:Scvr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL).

Subunit structure

Homotrimer.

Subcellular location

Membrane; Single-pass type II membrane protein.

Sequence similarities

Contains 1 collagen-like domain.

Contains 1 SRCR domain.

Sequence caution

The sequence AAA39747.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAA39748.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentLDL
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Collagen
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol transport

Inferred from mutant phenotype PubMed 12376530. Source: BHF-UCL

lipoprotein transport

Inferred from mutant phenotype PubMed 17148552. Source: MGI

plasma lipoprotein particle clearance

Inferred from mutant phenotype PubMed 12376530. Source: BHF-UCL

positive regulation of cholesterol storage

Inferred from mutant phenotype PubMed 12376530. Source: BHF-UCL

positive regulation of macrophage derived foam cell differentiation

Inferred from genetic interaction PubMed 12376530. Source: BHF-UCL

   Cellular_componentcollagen trimer

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionlow-density lipoprotein particle binding

Inferred from mutant phenotype PubMed 12376530. Source: BHF-UCL

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform I (identifier: P30204-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform II (identifier: P30204-2)

The sequence of this isoform differs from the canonical sequence as follows:
     352-354: TPL → RSV
     355-458: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Macrophage scavenger receptor types I and II
PRO_0000181628

Regions

Topological domain1 – 5555Cytoplasmic Potential
Transmembrane56 – 7823Helical; Signal-anchor for type II membrane protein; Potential
Topological domain79 – 458380Extracellular Potential
Domain277 – 35074Collagen-like
Domain357 – 457101SRCR
Region79 – 11436Spacer Probable
Coiled coil209 – 25951 Potential

Amino acid modifications

Modified residue321Phosphoserine Ref.9
Modified residue361Phosphoserine Ref.9
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Disulfide bond382 ↔ 446 By similarity
Disulfide bond395 ↔ 456 By similarity
Disulfide bond426 ↔ 436 By similarity

Natural variations

Alternative sequence352 – 3543TPL → RSV in isoform II.
VSP_006231
Alternative sequence355 – 458104Missing in isoform II.
VSP_006232

Experimental info

Sequence conflict161Q → R in AAA39747. Ref.1
Sequence conflict161Q → R in AAA39748. Ref.1
Sequence conflict161Q → R in BAA02650. Ref.2
Sequence conflict161Q → R in AAF14001. Ref.3
Sequence conflict161Q → R in BAC40779. Ref.4
Sequence conflict161Q → R in AAH03814. Ref.6
Sequence conflict471L → V in AAA39747. Ref.1
Sequence conflict471L → V in AAA39748. Ref.1
Sequence conflict471L → V in BAA02650. Ref.2
Sequence conflict471L → V in BAC40779. Ref.4
Sequence conflict471L → V in AAH03814. Ref.6
Sequence conflict931L → R in AAA39747. Ref.1
Sequence conflict931L → R in AAA39748. Ref.1
Sequence conflict931L → R in BAA02650. Ref.2
Sequence conflict931L → R in AAF14001. Ref.3
Sequence conflict931L → R in BAC40779. Ref.4
Sequence conflict931L → R in AAH03814. Ref.6
Sequence conflict1101K → N in AAA39747. Ref.1
Sequence conflict1101K → N in AAA39748. Ref.1
Sequence conflict1101K → N in BAA02650. Ref.2
Sequence conflict1101K → N in BAC40779. Ref.4
Sequence conflict1101K → N in AAH03814. Ref.6
Sequence conflict1201E → A in AAA39747. Ref.1
Sequence conflict1201E → A in AAA39748. Ref.1
Sequence conflict1201E → A in BAA02650. Ref.2
Sequence conflict1201E → A in BAC40779. Ref.4
Sequence conflict1201E → A in AAH03814. Ref.6
Sequence conflict1301E → Q in AAA39747. Ref.1
Sequence conflict1301E → Q in AAA39748. Ref.1
Sequence conflict1301E → Q in BAA02650. Ref.2
Sequence conflict1301E → Q in BAC40779. Ref.4
Sequence conflict1301E → Q in AAH03814. Ref.6
Sequence conflict1431E → G in AAA39747. Ref.1
Sequence conflict1431E → G in AAA39748. Ref.1
Sequence conflict1431E → G in BAA02650. Ref.2
Sequence conflict1431E → G in AAF14001. Ref.3
Sequence conflict1431E → G in BAC40779. Ref.4
Sequence conflict1431E → G in AAH03814. Ref.6
Sequence conflict1681S → L in AAA39747. Ref.1
Sequence conflict1681S → L in AAA39748. Ref.1
Sequence conflict1681S → L in BAA02650. Ref.2
Sequence conflict1681S → L in BAC40779. Ref.4
Sequence conflict1681S → L in AAH03814. Ref.6
Sequence conflict2021N → H in AAA39747. Ref.1
Sequence conflict2021N → H in AAA39748. Ref.1
Sequence conflict2021N → H in BAA02650. Ref.2
Sequence conflict2021N → H in BAC40779. Ref.4
Sequence conflict2021N → H in AAH03814. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform I [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: DA069B90A6B59EB5

FASTA45850,170
        10         20         30         40         50         60 
MTKEMTENQR LCPHEQEDAD CSSESVKFDA RSMTASLPHS TKNGPSLQEK LKSFKAALIA 

        70         80         90        100        110        120 
LYLLVFAVLI PVVGIVTAQL LNWEMKNCLV CSLNTSDTSQ GPMEKENTSK VEMRFTIIME 

       130        140        150        160        170        180 
HMKDMEERIE SISNSKADLI DTERFQNFSM ATDQRLNDIL LQLNSLISSV QEHGNSLDAI 

       190        200        210        220        230        240 
SKSLQSLNMT LLDVQLHTET LNVRVRESTA KQQEDISKLE ERVYKVSAEV QSVKEEQAHV 

       250        260        270        280        290        300 
EQEVKQEVRV LNNITNDLRL KDWEHSQTLK NITFIQGPPG PQGEKGDRGL TGQTGPPGAP 

       310        320        330        340        350        360 
GIRGIPGVKG DRGQIGFPGG RGNPGAPGKP GRSGSPGPKG QKGEKGSVGG STPLKTVRLV 

       370        380        390        400        410        420 
GGSGAHEGRV EIFHQGQWGT ICDDRWDIRA GQVVCRSLGY QEVLAVHKRA HFGQGTGPIW 

       430        440        450 
LNEVMCFGRE SSIENCKINQ WGVLSCSHSE DAGVTCTS 

« Hide

Isoform II [UniParc].

Checksum: 348E084D2D8B644B
Show »

FASTA35438,773

References

« Hide 'large scale' references
[1]"Structures and high and low affinity ligand binding properties of murine type I and type II macrophage scavenger receptors."
Ashkenas J., Penman M., Vasile E., Acton S., Freeman M.W., Krieger M.
J. Lipid Res. 34:983-1000(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II).
[2]"Charged collagen structure mediates the recognition of negatively charged macromolecules by macrophage scavenger receptors."
Doi T., Wada Y., Kodama T., Higashi K.I., Kurihara Y., Miyazaki T., Nakamura H., Uesugi S., Imanishi T., Kawabe Y., Itakura H., Yazaki Y., Matsumoto A.
J. Biol. Chem. 268:2126-2133(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
[3]"Identification of a functional domain in class A scavenger receptors that mediates metabolism of AcLDL."
Rateri D.L., Whitman S.C., Block A.E., Daugherty A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM I).
Strain: C57BL/6.
[4]"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] (ISOFORM II).
Strain: NOD.
Tissue: Thymus.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] (ISOFORM II).
[7]"An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors."
Freeman M., Ashkenas J., Rees D.J., Kingsley D.M., Copeland N.G., Jenkins N.A., Krieger M.
Proc. Natl. Acad. Sci. U.S.A. 87:8810-8814(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 349-458.
[8]"Structure of the murine macrophage scavenger receptor gene and evaluation of sequences that regulate expression in the macrophage cell line, P388D."
Aftring R.P., Freeman M.W.
J. Lipid Res. 36:1305-1314(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04274 mRNA. Translation: AAA39747.1. Different initiation.
L04275 mRNA. Translation: AAA39748.1. Different initiation.
D13382 mRNA. Translation: BAA02650.1.
AF203781 mRNA. Translation: AAF14001.1.
M59445 mRNA. Translation: AAA37464.1.
M59446 mRNA. Translation: AAA37465.1.
U13873 Genomic DNA. Translation: AAC13774.1.
AK089178 mRNA. Translation: BAC40779.1.
AC111028 Genomic DNA. No translation available.
BC003814 mRNA. Translation: AAH03814.1.
CCDSCCDS52542.1. [P30204-1]
CCDS52543.1. [P30204-2]
PIRB44407.
I73338.
RefSeqNP_001106797.1. NM_001113326.1. [P30204-1]
UniGeneMm.239291.

3D structure databases

ProteinModelPortalP30204.
SMRP30204. Positions 357-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP30204. 1 interaction.

Chemistry

BindingDBP30204.
ChEMBLCHEMBL4399.

PTM databases

PhosphoSiteP30204.

Proteomic databases

MaxQBP30204.
PaxDbP30204.
PRIDEP30204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026021; ENSMUSP00000026021; ENSMUSG00000025044. [P30204-1]
ENSMUST00000170091; ENSMUSP00000132535; ENSMUSG00000025044. [P30204-2]
GeneID20288.
KEGGmmu:20288.
UCSCuc012gcm.1. mouse. [P30204-1]

Organism-specific databases

CTD4481.
MGIMGI:98257. Msr1.

Phylogenomic databases

eggNOGNOG150350.
GeneTreeENSGT00640000091447.
HOGENOMHOG000085659.
HOVERGENHBG002473.
InParanoidP30204.
KOK06558.
OMAKWEMKNC.
OrthoDBEOG7V1FQV.
TreeFamTF330855.

Enzyme and pathway databases

ReactomeREACT_196573. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_213817. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP30204.
BgeeP30204.
CleanExMM_MSR1.
GenevestigatorP30204.

Family and domain databases

Gene3D3.10.250.10. 1 hit.
InterProIPR008160. Collagen.
IPR003543. Macro_scav_rcpt.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamPF01391. Collagen. 2 hits.
PF03523. Macscav_rec. 1 hit.
PF00530. SRCR. 1 hit.
[Graphical view]
PRINTSPR01408. MACSCAVRCPTR.
PR00258. SPERACTRCPTR.
SMARTSM00202. SR. 1 hit.
[Graphical view]
SUPFAMSSF56487. SSF56487. 1 hit.
PROSITEPS00420. SRCR_1. 1 hit.
PS50287. SRCR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMSR1. mouse.
NextBio297995.
PROP30204.
SOURCESearch...

Entry information

Entry nameMSRE_MOUSE
AccessionPrimary (citable) accession number: P30204
Secondary accession number(s): E9QNQ5, Q923G0, Q9QZ56
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 140 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