MSRE_MOUSE
ID MSRE_MOUSE Reviewed; 458 AA.
AC P30204; E9QNQ5; Q923G0; Q9QZ56;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Macrophage scavenger receptor types I and II;
DE AltName: Full=Macrophage acetylated LDL receptor I and II;
DE AltName: Full=Scavenger receptor type A;
DE Short=SR-A;
DE AltName: CD_antigen=CD204;
GN Name=Msr1; Synonyms=Scvr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II), AND SUBUNIT.
RX PubMed=8394868;
RA Ashkenas J., Penman M., Vasile E., Acton S., Freeman M.W., Krieger M.;
RT "Structures and high and low affinity ligand binding properties of murine
RT type I and type II macrophage scavenger receptors.";
RL J. Lipid Res. 34:983-1000(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
RX PubMed=8380589; DOI=10.1016/s0021-9258(18)53971-5;
RA Doi T., Wada Y., Kodama T., Higashi K.I., Kurihara Y., Miyazaki T.,
RA Nakamura H., Uesugi S., Imanishi T., Kawabe Y., Itakura H., Yazaki Y.,
RA Matsumoto A.;
RT "Charged collagen structure mediates the recognition of negatively charged
RT macromolecules by macrophage scavenger receptors.";
RL J. Biol. Chem. 268:2126-2133(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM I).
RC STRAIN=C57BL/6J;
RA Rateri D.L., Whitman S.C., Block A.E., Daugherty A.;
RT "Identification of a functional domain in class A scavenger receptors that
RT mediates metabolism of AcLDL.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 349-458.
RX PubMed=1978939; DOI=10.1073/pnas.87.22.8810;
RA Freeman M., Ashkenas J., Rees D.J., Kingsley D.M., Copeland N.G.,
RA Jenkins N.A., Krieger M.;
RT "An ancient, highly conserved family of cysteine-rich protein domains
RT revealed by cloning type I and type II murine macrophage scavenger
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8810-8814(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RX PubMed=7666008;
RA Aftring R.P., Freeman M.W.;
RT "Structure of the murine macrophage scavenger receptor gene and evaluation
RT of sequences that regulate expression in the macrophage cell line, P388D.";
RL J. Lipid Res. 36:1305-1314(1995).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Membrane glycoproteins implicated in the pathologic
CC deposition of cholesterol in arterial walls during atherogenesis. Two
CC types of receptor subunits exist. These receptors mediate the
CC endocytosis of a diverse group of macromolecules, including modified
CC low density lipoproteins (LDL). {ECO:0000250|UniProtKB:P21757}.
CC -!- SUBUNIT: Homotrimer (PubMed:8394868). Interacts with MYO18A (By
CC similarity). {ECO:0000250|UniProtKB:P21757,
CC ECO:0000269|PubMed:8394868}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I;
CC IsoId=P30204-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P30204-2; Sequence=VSP_006231, VSP_006232;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39747.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA39748.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L04274; AAA39747.1; ALT_INIT; mRNA.
DR EMBL; L04275; AAA39748.1; ALT_INIT; mRNA.
DR EMBL; D13382; BAA02650.1; -; mRNA.
DR EMBL; AF203781; AAF14001.1; -; mRNA.
DR EMBL; M59445; AAA37464.1; -; mRNA.
DR EMBL; M59446; AAA37465.1; -; mRNA.
DR EMBL; U13873; AAC13774.1; -; Genomic_DNA.
DR EMBL; AK089178; BAC40779.1; -; mRNA.
DR EMBL; AC111028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003814; AAH03814.1; -; mRNA.
DR CCDS; CCDS52542.1; -. [P30204-1]
DR CCDS; CCDS52543.1; -. [P30204-2]
DR PIR; B44407; B44407.
DR PIR; I73338; I73338.
DR RefSeq; NP_001106797.1; NM_001113326.1. [P30204-1]
DR PDB; 6J02; X-ray; 1.80 A; A/B=350-458.
DR PDBsum; 6J02; -.
DR AlphaFoldDB; P30204; -.
DR SMR; P30204; -.
DR IntAct; P30204; 1.
DR STRING; 10090.ENSMUSP00000026021; -.
DR BindingDB; P30204; -.
DR ChEMBL; CHEMBL4399; -.
DR GlyGen; P30204; 6 sites.
DR iPTMnet; P30204; -.
DR PhosphoSitePlus; P30204; -.
DR jPOST; P30204; -.
DR MaxQB; P30204; -.
DR PaxDb; P30204; -.
DR PeptideAtlas; P30204; -.
DR PRIDE; P30204; -.
DR ProteomicsDB; 291527; -. [P30204-1]
DR ProteomicsDB; 291528; -. [P30204-2]
DR Antibodypedia; 601; 951 antibodies from 39 providers.
DR DNASU; 20288; -.
DR Ensembl; ENSMUST00000026021; ENSMUSP00000026021; ENSMUSG00000025044. [P30204-1]
DR Ensembl; ENSMUST00000170091; ENSMUSP00000132535; ENSMUSG00000025044. [P30204-2]
DR GeneID; 20288; -.
DR KEGG; mmu:20288; -.
DR UCSC; uc012gcm.1; mouse. [P30204-1]
DR CTD; 4481; -.
DR MGI; MGI:98257; Msr1.
DR VEuPathDB; HostDB:ENSMUSG00000025044; -.
DR eggNOG; ENOG502QUW0; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_2_0_1; -.
DR InParanoid; P30204; -.
DR OMA; RGPHEGR; -.
DR OrthoDB; 711951at2759; -.
DR PhylomeDB; P30204; -.
DR TreeFam; TF330855; -.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR BioGRID-ORCS; 20288; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Msr1; mouse.
DR PRO; PR:P30204; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P30204; protein.
DR Bgee; ENSMUSG00000025044; Expressed in stroma of bone marrow and 131 other tissues.
DR ExpressionAtlas; P30204; baseline and differential.
DR Genevisible; P30204; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IGI:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; IGI:ARUK-UCL.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IMP:BHF-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
DR GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0042953; P:lipoprotein transport; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0006911; P:phagocytosis, engulfment; IGI:ARUK-UCL.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IGI:BHF-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IGI:ARUK-UCL.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003543; SR-AI/II.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19331:SF440; PTHR19331:SF440; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF03523; Macscav_rec; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR01408; MACSCAVRCPTR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Collagen; Disulfide bond;
KW Endocytosis; Glycoprotein; LDL; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..458
FT /note="Macrophage scavenger receptor types I and II"
FT /id="PRO_0000181628"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..78
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 277..350
FT /note="Collagen-like"
FT DOMAIN 357..457
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 79..114
FT /note="Spacer"
FT /evidence="ECO:0000305"
FT REGION 272..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..259
FT /evidence="ECO:0000255"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 382..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 395..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 426..436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 352..354
FT /note="TPL -> RSV (in isoform II)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8380589,
FT ECO:0000303|PubMed:8394868"
FT /id="VSP_006231"
FT VAR_SEQ 355..458
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8380589,
FT ECO:0000303|PubMed:8394868"
FT /id="VSP_006232"
FT CONFLICT 16
FT /note="Q -> R (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 3; AAF14001, 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="L -> V (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="L -> R (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 3; AAF14001, 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="K -> N (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="E -> A (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="E -> Q (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> G (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 3; AAF14001, 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> L (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="N -> H (in Ref. 1; AAA39747/AAA39748, 2; BAA02650,
FT 4; BAC40779 and 6; AAH03814)"
FT /evidence="ECO:0000305"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:6J02"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:6J02"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:6J02"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6J02"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:6J02"
SQ SEQUENCE 458 AA; 50170 MW; DA069B90A6B59EB5 CRC64;
MTKEMTENQR LCPHEQEDAD CSSESVKFDA RSMTASLPHS TKNGPSLQEK LKSFKAALIA
LYLLVFAVLI PVVGIVTAQL LNWEMKNCLV CSLNTSDTSQ GPMEKENTSK VEMRFTIIME
HMKDMEERIE SISNSKADLI DTERFQNFSM ATDQRLNDIL LQLNSLISSV QEHGNSLDAI
SKSLQSLNMT LLDVQLHTET LNVRVRESTA KQQEDISKLE ERVYKVSAEV QSVKEEQAHV
EQEVKQEVRV LNNITNDLRL KDWEHSQTLK NITFIQGPPG PQGEKGDRGL TGQTGPPGAP
GIRGIPGVKG DRGQIGFPGG RGNPGAPGKP GRSGSPGPKG QKGEKGSVGG STPLKTVRLV
GGSGAHEGRV EIFHQGQWGT ICDDRWDIRA GQVVCRSLGY QEVLAVHKRA HFGQGTGPIW
LNEVMCFGRE SSIENCKINQ WGVLSCSHSE DAGVTCTS
