ID   MARCO_MESAU             Reviewed;         483 AA.
AC   Q9WUB9;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Macrophage receptor MARCO;
DE   AltName: Full=Macrophage receptor with collagenous structure;
GN   Name=MARCO;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10224290; DOI=10.1084/jem.189.9.1497;
RA   Palecanda A., Paulauskis J.D., Al-Mutairi E., Imrich A., Qin G., Suzuki H.,
RA   Kodama T., Tryggvason K., Koziel H., Kobzik L.;
RT   "Role of the scavenger receptor MARCO in alveolar macrophage binding of
RT   unopsonized environmental particles.";
RL   J. Exp. Med. 189:1497-1506(1999).
CC   -!- FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive
CC       and Gram-negative bacteria (PubMed:10224290). Also plays a role in
CC       binding of unopsonized particles by alveolar macrophages
CC       (PubMed:10224290). Binds to the secretoglobin SCGB3A2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UEW3, ECO:0000269|PubMed:10224290}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. Trimers may assemble in larger
CC       oligomers thus resulting in the creation of a large surface capable of
CC       interacting with very large ligands. {ECO:0000250|UniProtKB:Q60754}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10224290};
CC       Single-pass type II membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in alveolar macrophages, macrophages of
CC       lymph node sinues, and Kupffer cells in liver (at protein level).
CC       {ECO:0000269|PubMed:10224290}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q60754}.
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DR   EMBL; AF125191; AAD20360.1; -; mRNA.
DR   RefSeq; NP_001268535.1; NM_001281606.1.
DR   AlphaFoldDB; Q9WUB9; -.
DR   SMR; Q9WUB9; -.
DR   STRING; 10036.XP_005070362.1; -.
DR   PRIDE; Q9WUB9; -.
DR   GeneID; 101834359; -.
DR   CTD; 8685; -.
DR   eggNOG; ENOG502QWN1; Eukaryota.
DR   OrthoDB; 727886at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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; 3.
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   Cell membrane; Collagen; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Membrane; Receptor; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..483
FT                   /note="Macrophage receptor MARCO"
FT                   /id="PRO_0000181631"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q60754"
FT   TRANSMEM        49..69
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        70..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q60754"
FT   DOMAIN          148..383
FT                   /note="Collagen-like"
FT   DOMAIN          389..483
FT                   /note="SRCR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   REGION          146..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        412..472
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        425..482
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT   DISULFID        452..462
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
SQ   SEQUENCE   483 AA;  49622 MW;  C38F18C46505FB1E CRC64;
     MGNKKALKEE AFLGSAEEGA DFDQAMFPVM ETFEINDPMP KKRNWGSFCT AVMAIHLILL
     TAGTTLLTLK VLSLQKWILE KYLDNETLAA EDRSFFSLQL ASPETHLVPR TPGLQALQVQ
     LTQVRTSQEQ LLQQVDNLTR NPELFRIKGE RGSPGIPGLQ GPPGIKGEAG LQGPMGAPRE
     PGATGAPGPQ GEKGSKGDKG LIGPKGEHGT KGDKGDLGLP GSKGDMGMKG VTGVMGPPGA
     QGNKGDPGKP GLPGLAGSPG VKGDQGQPGL QGVPGTPGAA GPSGAKGEPG HPGPPGPTGP
     QGISGSPGAA GLKGSKGDTG IQGQKGTKGE SGVPGLAGRK GDTGNPGLAG PKGEPGRPGL
     KGDPGMKGSS GQQGQKGEKG EKGQSFKEVR IVGGTNRGRA EIFYNNAWGT ICDDNWDNND
     ATVFCRMLGY SSGKGFTFGG GSGNIWLDDV NCQGTEDSLW NCRKNNWGSH NCNHNEDAGV
     ECR