MARCO_MOUSE
ID MARCO_MOUSE Reviewed; 518 AA.
AC Q60754;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Macrophage receptor MARCO;
DE AltName: Full=Macrophage receptor with collagenous structure;
GN Name=Marco;
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND TOPOLOGY.
RX PubMed=7867067; DOI=10.1016/0092-8674(95)90514-6;
RA Elomaa O., Kangas M., Sahlberg C., Tuukkanen J., Sormunen R., Liakka A.,
RA Thesleff I., Kraal G., Tryggvason K.;
RT "Cloning of a novel bacteria-binding receptor structurally related to
RT scavenger receptors and expressed in a subset of macrophages.";
RL Cell 80:603-609(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10331948; DOI=10.1006/geno.1999.5811;
RA Kangas M., Brannstrom A., Elomaa O., Matsuda Y., Eddy R., Shows T.B.,
RA Tryggvason K.;
RT "Structure and chromosomal localization of the human and murine genes for
RT the macrophage MARCO receptor.";
RL Genomics 58:82-89(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 421-518, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=17405873; DOI=10.1074/jbc.m701750200;
RA Ojala J.R., Pikkarainen T., Tuuttila A., Sandalova T., Tryggvason K.;
RT "Crystal structure of the cysteine-rich domain of scavenger receptor MARCO
RT reveals the presence of a basic and an acidic cluster that both contribute
RT to ligand recognition.";
RL J. Biol. Chem. 282:16654-16666(2007).
CC -!- FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive
CC and Gram-negative bacteria (PubMed:7867067). Also plays a role in
CC binding of unopsonized particles by alveolar macrophages (By
CC similarity). Binds to the secretoglobin SCGB3A2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UEW3, ECO:0000250|UniProtKB:Q9WUB9,
CC ECO:0000269|PubMed:7867067}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:7867067). Trimers may
CC assemble in larger oligomers thus resulting in the creation of a large
CC surface capable of interacting with very large ligands
CC (PubMed:17405873). {ECO:0000269|PubMed:17405873,
CC ECO:0000269|PubMed:7867067}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7867067};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in subpopulations of macrophages in the
CC spleen and the medullary cord of lymph nodes (at protein level).
CC {ECO:0000269|PubMed:7867067}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:7867067}.
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DR EMBL; U18424; AAA68638.1; -; mRNA.
DR EMBL; AF128423; AAD51136.1; -; Genomic_DNA.
DR EMBL; AF127927; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF127928; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128169; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128170; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128171; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF127601; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF127602; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128419; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128420; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128421; AAD51136.1; JOINED; Genomic_DNA.
DR EMBL; AF128422; AAD51136.1; JOINED; Genomic_DNA.
DR CCDS; CCDS15234.1; -.
DR PIR; A55840; A55840.
DR RefSeq; NP_034896.1; NM_010766.2.
DR PDB; 2OY3; X-ray; 1.78 A; A=421-518.
DR PDB; 2OYA; X-ray; 1.77 A; A/B=421-518.
DR PDBsum; 2OY3; -.
DR PDBsum; 2OYA; -.
DR AlphaFoldDB; Q60754; -.
DR SMR; Q60754; -.
DR STRING; 10090.ENSMUSP00000027639; -.
DR GlyGen; Q60754; 2 sites.
DR PhosphoSitePlus; Q60754; -.
DR CPTAC; non-CPTAC-3472; -.
DR MaxQB; Q60754; -.
DR PaxDb; Q60754; -.
DR PRIDE; Q60754; -.
DR ProteomicsDB; 292168; -.
DR Antibodypedia; 41307; 256 antibodies from 27 providers.
DR DNASU; 17167; -.
DR Ensembl; ENSMUST00000027639; ENSMUSP00000027639; ENSMUSG00000026390.
DR GeneID; 17167; -.
DR KEGG; mmu:17167; -.
DR UCSC; uc007cjl.1; mouse.
DR CTD; 8685; -.
DR MGI; MGI:1309998; Marco.
DR VEuPathDB; HostDB:ENSMUSG00000026390; -.
DR eggNOG; ENOG502QWN1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_039737_0_0_1; -.
DR InParanoid; Q60754; -.
DR OMA; GMFGIKG; -.
DR OrthoDB; 727886at2759; -.
DR PhylomeDB; Q60754; -.
DR TreeFam; TF330855; -.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR BioGRID-ORCS; 17167; 3 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q60754; -.
DR PRO; PR:Q60754; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q60754; protein.
DR Bgee; ENSMUSG00000026390; Expressed in stroma of bone marrow and 55 other tissues.
DR ExpressionAtlas; Q60754; baseline and differential.
DR Genevisible; Q60754; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0097242; P:amyloid-beta clearance; IEA:Ensembl.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00530; SRCR; 1.
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; Cell membrane; Collagen; Disulfide bond; Glycoprotein;
KW Immunity; Innate immunity; Membrane; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..518
FT /note="Macrophage receptor MARCO"
FT /id="PRO_0000181632"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7867067"
FT TRANSMEM 49..69
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..518
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7867067"
FT DOMAIN 149..418
FT /note="Collagen-like"
FT DOMAIN 423..518
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 147..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 446..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 459..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 487..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT STRAND 422..438
FT /evidence="ECO:0007829|PDB:2OYA"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:2OYA"
FT HELIX 452..461
FT /evidence="ECO:0007829|PDB:2OYA"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:2OYA"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2OYA"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:2OYA"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:2OYA"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:2OYA"
SQ SEQUENCE 518 AA; 52730 MW; B09E7601ECA23637 CRC64;
MGSKELLKEE DFLGSTEDRA DFDQAMFPVM ETFEINDPVP KKRNGGTFCM AVMAIHLILL
TAGTALLLIQ VLNLQEQLQM LEMCCGNGSL AIEDKPFFSL QWAPKTHLVP RAQGLQALQA
QLSWVHTSQE QLRQQFNNLT QNPELFQIKG ERGSPGPKGA PGAPGIPGLP GPAAEKGEKG
AAGRDGTPGV QGPQGPPGSK GEAGLQGLTG APGKQGATGA PGPRGEKGSK GDIGLTGPKG
EHGTKGDKGD LGLPGNKGDM GMKGDTGPMG SPGAQGGKGD AGKPGLPGLA GSPGVKGDQG
KPGVQGVPGP QGAPGLSGAK GEPGRTGLPG PAGPPGIAGN PGIAGVKGSK GDTGIQGQKG
TKGESGVPGL VGRKGDTGSP GLAGPKGEPG RVGQKGDPGM KGSSGQQGQK GEKGQKGESF
QRVRIMGGTN RGRAEVYYNN EWGTICDDDW DNNDATVFCR MLGYSRGRAL SSYGGGSGNI
WLDNVNCRGT ENSLWDCSKN SWGNHNCVHN EDAGVECS
