P30204 (MSRE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Endocytosis
Cellular component	LDL Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Collagen Signal-anchor Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol 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 response to chemical stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmic vesicle Inferred from electronic annotation. Source: Compara cytosol Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW low-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	low-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 458	458	Macrophage scavenger receptor types I and II		PRO_0000181628
Regions
	Topological domain	1 – 55	55	Cytoplasmic Potential
	Transmembrane	56 – 78	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	79 – 458	380	Extracellular Potential
	Domain	277 – 350	74	Collagen-like
	Domain	357 – 457	101	SRCR
	Region	79 – 114	36	Spacer Probable
	Coiled coil	209 – 259	51	Potential
Amino acid modifications
	Modified residue	32	1	Phosphoserine Ref.9
	Modified residue	34	1	Phosphothreonine Ref.9
	Modified residue	36	1	Phosphoserine Ref.9
	Modified residue	40	1	Phosphoserine Ref.9
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	147	1	N-linked (GlcNAc...) Potential
	Glycosylation	188	1	N-linked (GlcNAc...) Potential
	Glycosylation	253	1	N-linked (GlcNAc...) Potential
	Glycosylation	271	1	N-linked (GlcNAc...) Potential
	Disulfide bond	382 ↔ 446		By similarity
	Disulfide bond	395 ↔ 456		By similarity
	Disulfide bond	426 ↔ 436		By similarity
Natural variations
	Alternative sequence	352 – 354	3	TPL → RSV in isoform II.		VSP_006231
	Alternative sequence	355 – 458	104	Missing in isoform II.		VSP_006232
Experimental info
	Sequence conflict	16	1	Q → R in AAA39747. Ref.1
	Sequence conflict	16	1	Q → R in AAA39748. Ref.1
	Sequence conflict	16	1	Q → R in BAA02650. Ref.2
	Sequence conflict	16	1	Q → R in AAF14001. Ref.3
	Sequence conflict	16	1	Q → R in BAC40779. Ref.4
	Sequence conflict	16	1	Q → R in AAH03814. Ref.6
	Sequence conflict	47	1	L → V in AAA39747. Ref.1
	Sequence conflict	47	1	L → V in AAA39748. Ref.1
	Sequence conflict	47	1	L → V in BAA02650. Ref.2
	Sequence conflict	47	1	L → V in BAC40779. Ref.4
	Sequence conflict	47	1	L → V in AAH03814. Ref.6
	Sequence conflict	93	1	L → R in AAA39747. Ref.1
	Sequence conflict	93	1	L → R in AAA39748. Ref.1
	Sequence conflict	93	1	L → R in BAA02650. Ref.2
	Sequence conflict	93	1	L → R in AAF14001. Ref.3
	Sequence conflict	93	1	L → R in BAC40779. Ref.4
	Sequence conflict	93	1	L → R in AAH03814. Ref.6
	Sequence conflict	110	1	K → N in AAA39747. Ref.1
	Sequence conflict	110	1	K → N in AAA39748. Ref.1
	Sequence conflict	110	1	K → N in BAA02650. Ref.2
	Sequence conflict	110	1	K → N in BAC40779. Ref.4
	Sequence conflict	110	1	K → N in AAH03814. Ref.6
	Sequence conflict	120	1	E → A in AAA39747. Ref.1
	Sequence conflict	120	1	E → A in AAA39748. Ref.1
	Sequence conflict	120	1	E → A in BAA02650. Ref.2
	Sequence conflict	120	1	E → A in BAC40779. Ref.4
	Sequence conflict	120	1	E → A in AAH03814. Ref.6
	Sequence conflict	130	1	E → Q in AAA39747. Ref.1
	Sequence conflict	130	1	E → Q in AAA39748. Ref.1
	Sequence conflict	130	1	E → Q in BAA02650. Ref.2
	Sequence conflict	130	1	E → Q in BAC40779. Ref.4
	Sequence conflict	130	1	E → Q in AAH03814. Ref.6
	Sequence conflict	143	1	E → G in AAA39747. Ref.1
	Sequence conflict	143	1	E → G in AAA39748. Ref.1
	Sequence conflict	143	1	E → G in BAA02650. Ref.2
	Sequence conflict	143	1	E → G in AAF14001. Ref.3
	Sequence conflict	143	1	E → G in BAC40779. Ref.4
	Sequence conflict	143	1	E → G in AAH03814. Ref.6
	Sequence conflict	168	1	S → L in AAA39747. Ref.1
	Sequence conflict	168	1	S → L in AAA39748. Ref.1
	Sequence conflict	168	1	S → L in BAA02650. Ref.2
	Sequence conflict	168	1	S → L in BAC40779. Ref.4
	Sequence conflict	168	1	S → L in AAH03814. Ref.6
	Sequence conflict	202	1	N → H in AAA39747. Ref.1
	Sequence conflict	202	1	N → H in AAA39748. Ref.1
	Sequence conflict	202	1	N → H in BAA02650. Ref.2
	Sequence conflict	202	1	N → H in BAC40779. Ref.4
	Sequence conflict	202	1	N → H in AAH03814. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform I [UniParc]. Last modified July 27, 2011. Version 3. Checksum: DA069B90A6B59EB5	FASTA	458	50,170
	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
	Isoform II [UniParc]. Checksum: 348E084D2D8B644B	FASTA	354	38,773
	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 GIRGIPGVKG DRGQIGFPGG RGNPGAPGKP GRSGSPGPKG QKGEKGSVGG SRSV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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; THR-34; SER-36 AND SER-40, MASS SPECTROMETRY. Tissue: Macrophage.
+	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.
IPI	IPI00124283. IPI00128178.
PIR	B44407. I73338.
RefSeq	NP_001106797.1. NM_001113326.1.
UniGene	Mm.239291.
3D structure databases
ProteinModelPortal	P30204.
SMR	P30204. Positions 277-355, 357-458.
ModBase	Search...
Protein-protein interaction databases
IntAct	P30204. 1 interaction.
PTM databases
PhosphoSite	P30204.
Proteomic databases
PaxDb	P30204.
PRIDE	P30204.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026021; ENSMUSP00000026021; ENSMUSG00000025044. ENSMUST00000170091; ENSMUSP00000132535; ENSMUSG00000025044.
GeneID	20288.
KEGG	mmu:20288.
Organism-specific databases
CTD	4481.
MGI	MGI:98257. Msr1.
Phylogenomic databases
eggNOG	NOG150350.
GeneTree	ENSGT00640000091447.
HOGENOM	HOG000085659.
HOVERGEN	HBG002473.
InParanoid	P30204.
KO	K06558.
OMA	LLKWEMK.
OrthoDB	EOG4RJG1J.
Gene expression databases
ArrayExpress	P30204.
Bgee	P30204.
CleanEx	MM_MSR1.
Genevestigator	P30204.
GermOnline	ENSMUSG00000025044. Mus musculus.
Family and domain databases
InterPro	IPR008160. Collagen. IPR003543. Macro_scav_rcpt. IPR001190. Srcr_rcpt. IPR017448. Srcr_rcpt-rel. [Graphical view]
Pfam	PF01391. Collagen. 2 hits. PF03523. Macscav_rec. 1 hit. PF00530. SRCR. 1 hit. [Graphical view]
PRINTS	PR01408. MACSCAVRCPTR. PR00258. SPERACTRCPTR.
SMART	SM00202. SR. 1 hit. [Graphical view]
SUPFAM	SSF56487. Srcr_receptor. 1 hit.
PROSITE	PS00420. SRCR_1. 1 hit. PS50287. SRCR_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P30204.
ChEMBL	CHEMBL4399.
ChiTaRS	MSR1. mouse.
NextBio	297995.
SOURCE	Search...

Entry information

Entry name

MSRE_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program