MARCO_HUMAN
ID MARCO_HUMAN Reviewed; 520 AA.
AC Q9UEW3; B4DW79; Q9Y5S3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Macrophage receptor MARCO;
DE AltName: Full=Macrophage receptor with collagenous structure;
DE AltName: Full=Scavenger receptor class A member 2;
GN Name=MARCO; Synonyms=SCARA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISULFIDE BONDS.
RX PubMed=9468508; DOI=10.1074/jbc.273.8.4530;
RA Elomaa O., Sankala M., Pikkarainen T., Bergmann U., Tuuttila A.,
RA Raatikainen-Ahokas A., Sariola H., Tryggvason K.;
RT "Structure of the human macrophage MARCO receptor and characterization of
RT its bacteria-binding region.";
RL J. Biol. Chem. 273:4530-4538(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP TISSUE 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).
RN [7]
RP FUNCTION.
RX PubMed=12847263; DOI=10.4049/jimmunol.171.2.924;
RA Bin L.H., Nielson L.D., Liu X., Mason R.J., Shu H.B.;
RT "Identification of uteroglobin-related protein 1 and macrophage scavenger
RT receptor with collagenous structure as a lung-specific ligand-receptor
RT pair.";
RL J. Immunol. 171:924-930(2003).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive
CC and Gram-negative bacteria (PubMed:9468508). Also plays a role in
CC binding of unopsonized particles by alveolar macrophages (By
CC similarity). Binds to the secretoglobin SCGB3A2 (PubMed:12847263).
CC {ECO:0000250|UniProtKB:Q9WUB9, ECO:0000269|PubMed:12847263,
CC ECO:0000269|PubMed:9468508}.
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:9468508};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UEW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UEW3-2; Sequence=VSP_056698;
CC -!- TISSUE SPECIFICITY: Expressed in alveolar macrophages (at protein
CC level). Detected in macrophages from various tissues including thymus,
CC kidney, Kupffer cells of liver, and spleen (PubMed:9468508).
CC {ECO:0000269|PubMed:10224290, ECO:0000269|PubMed:9468508}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q60754}.
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DR EMBL; AF035819; AAC08800.1; -; mRNA.
DR EMBL; AF128186; AAD41064.1; -; Genomic_DNA.
DR EMBL; AF128172; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128173; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128174; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128175; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128176; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128177; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128178; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128179; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128180; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128181; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128182; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128183; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128184; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AF128185; AAD41064.1; JOINED; Genomic_DNA.
DR EMBL; AK301407; BAG62941.1; -; mRNA.
DR EMBL; AC013457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016004; AAH16004.1; -; mRNA.
DR CCDS; CCDS2124.1; -. [Q9UEW3-1]
DR RefSeq; NP_006761.1; NM_006770.3. [Q9UEW3-1]
DR RefSeq; XP_011510384.1; XM_011512082.1. [Q9UEW3-1]
DR AlphaFoldDB; Q9UEW3; -.
DR SMR; Q9UEW3; -.
DR BioGRID; 114232; 11.
DR IntAct; Q9UEW3; 4.
DR MINT; Q9UEW3; -.
DR STRING; 9606.ENSP00000318916; -.
DR DrugBank; DB11132; Silicon dioxide.
DR DrugBank; DB09536; Titanium dioxide.
DR GlyConnect; 1957; 9 N-Linked glycans (1 site).
DR GlyGen; Q9UEW3; 2 sites, 9 N-linked glycans (1 site).
DR iPTMnet; Q9UEW3; -.
DR PhosphoSitePlus; Q9UEW3; -.
DR BioMuta; MARCO; -.
DR DMDM; 17380151; -.
DR EPD; Q9UEW3; -.
DR jPOST; Q9UEW3; -.
DR MassIVE; Q9UEW3; -.
DR PaxDb; Q9UEW3; -.
DR PeptideAtlas; Q9UEW3; -.
DR PRIDE; Q9UEW3; -.
DR ProteomicsDB; 5319; -.
DR ProteomicsDB; 84158; -. [Q9UEW3-1]
DR ABCD; Q9UEW3; 1 sequenced antibody.
DR Antibodypedia; 41307; 256 antibodies from 27 providers.
DR DNASU; 8685; -.
DR Ensembl; ENST00000327097.5; ENSP00000318916.4; ENSG00000019169.11. [Q9UEW3-1]
DR GeneID; 8685; -.
DR KEGG; hsa:8685; -.
DR MANE-Select; ENST00000327097.5; ENSP00000318916.4; NM_006770.4; NP_006761.1.
DR UCSC; uc002tln.2; human. [Q9UEW3-1]
DR CTD; 8685; -.
DR DisGeNET; 8685; -.
DR GeneCards; MARCO; -.
DR HGNC; HGNC:6895; MARCO.
DR HPA; ENSG00000019169; Tissue enhanced (liver, lung, lymphoid tissue).
DR MIM; 604870; gene.
DR neXtProt; NX_Q9UEW3; -.
DR OpenTargets; ENSG00000019169; -.
DR PharmGKB; PA30638; -.
DR VEuPathDB; HostDB:ENSG00000019169; -.
DR eggNOG; ENOG502QWN1; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_039737_0_0_1; -.
DR InParanoid; Q9UEW3; -.
DR OMA; GMFGIKG; -.
DR PhylomeDB; Q9UEW3; -.
DR TreeFam; TF330855; -.
DR PathwayCommons; Q9UEW3; -.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR SignaLink; Q9UEW3; -.
DR SIGNOR; Q9UEW3; -.
DR BioGRID-ORCS; 8685; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; MARCO; human.
DR GeneWiki; MARCO; -.
DR GenomeRNAi; 8685; -.
DR Pharos; Q9UEW3; Tbio.
DR PRO; PR:Q9UEW3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UEW3; protein.
DR Bgee; ENSG00000019169; Expressed in right lung and 121 other tissues.
DR ExpressionAtlas; Q9UEW3; baseline and differential.
DR Genevisible; Q9UEW3; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0038024; F:cargo receptor activity; ISS:ARUK-UCL.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ARUK-UCL.
DR GO; GO:0038187; F:pattern recognition receptor activity; TAS:ProtInc.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0097242; P:amyloid-beta clearance; ISS:ARUK-UCL.
DR GO; GO:0043277; P:apoptotic cell clearance; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:ARUK-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:ARUK-UCL.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:ARUK-UCL.
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 Alternative splicing; Cell membrane; Collagen; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Membrane; Receptor;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Macrophage receptor MARCO"
FT /id="PRO_0000181630"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q60754"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..520
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q60754"
FT DOMAIN 147..419
FT /note="Collagen-like"
FT DOMAIN 424..519
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 142..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 447..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:9468508"
FT DISULFID 460..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:9468508"
FT DISULFID 488..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196,
FT ECO:0000269|PubMed:9468508"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056698"
FT VARIANT 282
FT /note="F -> S (in dbSNP:rs6761637)"
FT /id="VAR_024650"
FT CONFLICT 13
FT /note="L -> F (in Ref. 2; AAD41064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 52658 MW; 8CFC5F6F99EEBA8D CRC64;
MRNKKILKED ELLSETQQAA FHQIAMEPFE INVPKPKRRN GVNFSLAVVV IYLILLTAGA
GLLVVQVLNL QARLRVLEMY FLNDTLAAED SPSFSLLQSA HPGEHLAQGA SRLQVLQAQL
TWVRVSHEHL LQRVDNFTQN PGMFRIKGEQ GAPGLQGHKG AMGMPGAPGP PGPPAEKGAK
GAMGRDGATG PSGPQGPPGV KGEAGLQGPQ GAPGKQGATG TPGPQGEKGS KGDGGLIGPK
GETGTKGEKG DLGLPGSKGD RGMKGDAGVM GPPGAQGSKG DFGRPGPPGL AGFPGAKGDQ
GQPGLQGVPG PPGAVGHPGA KGEPGSAGSP GRAGLPGSPG SPGATGLKGS KGDTGLQGQQ
GRKGESGVPG PAGVKGEQGS PGLAGPKGAP GQAGQKGDQG VKGSSGEQGV KGEKGERGEN
SVSVRIVGSS NRGRAEVYYS GTWGTICDDE WQNSDAIVFC RMLGYSKGRA LYKVGAGTGQ
IWLDNVQCRG TESTLWSCTK NSWGHHDCSH EEDAGVECSV
