ID MRC1_HUMAN Reviewed; 1456 AA. AC P22897; A5PKW3; Q5VSJ2; Q5VSK2; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 27-MAR-2024, entry version 241. DE RecName: Full=Macrophage mannose receptor 1; DE Short=MMR; DE AltName: Full=C-type lectin domain family 13 member D; DE AltName: Full=C-type lectin domain family 13 member D-like; DE AltName: Full=Human mannose receptor; DE Short=hMR; DE AltName: Full=Macrophage mannose receptor 1-like protein 1; DE AltName: CD_antigen=CD206; DE Flags: Precursor; GN Name=MRC1; Synonyms=CLEC13D, CLEC13DL, MRC1L1; 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), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Placenta; RX PubMed=2373685; DOI=10.1016/s0021-9258(19)38325-5; RA Taylor M.E., Conary J.T., Lennartz M.R., Stahl P.D., Drickamer K.; RT "Primary structure of the mannose receptor contains multiple motifs RT resembling carbohydrate-recognition domains."; RL J. Biol. Chem. 265:12156-12162(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2258707; DOI=10.1084/jem.172.6.1785; RA Ezekowitz R.A., Sastry K., Bailly P., Warner A.; RT "Molecular characterization of the human macrophage mannose receptor: RT demonstration of multiple carbohydrate recognition-like domains and RT phagocytosis of yeasts in Cos-1 cells."; RL J. Exp. Med. 172:1785-1794(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1294118; DOI=10.1016/s0888-7543(05)80174-0; RA Kim S.J., Ruiz N., Bezouska K., Drickamer K.; RT "Organization of the gene encoding the human macrophage mannose receptor RT (MRC1)."; RL Genomics 14:721-727(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS SER-396; RP ALA-399 AND PHE-407. 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 STUDIES ON THE BINDING OF INDIVIDUAL LECTIN DOMAINS. RX PubMed=1730714; DOI=10.1016/s0021-9258(18)46005-x; RA Taylor M.E., Bezouska K., Drickamer K.; RT "Contribution to ligand binding by multiple carbohydrate-recognition RT domains in the macrophage mannose receptor."; RL J. Biol. Chem. 267:1719-1726(1992). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1205. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [9] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH DENGUE VIRUS ENVELOPE RP PROTEIN E. RX PubMed=18266465; DOI=10.1371/journal.ppat.0040017; RA Miller J.L., de Wet B.J., deWet B.J., Martinez-Pomares L., Radcliffe C.M., RA Dwek R.A., Rudd P.M., Gordon S.; RT "The mannose receptor mediates dengue virus infection of macrophages."; RL PLoS Pathog. 4:E17-E17(2008). RN [10] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS B VIRUS RP ENVELOPE PROTEIN. RX PubMed=19683778; DOI=10.1016/j.virol.2009.07.015; RA Op den Brouw M.L., Binda R.S., Geijtenbeek T.B., Janssen H.L., RA Woltman A.M.; RT "The mannose receptor acts as hepatitis B virus surface antigen receptor RT mediating interaction with intrahepatic dendritic cells."; RL Virology 393:84-90(2009). RN [11] 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). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 642-788. RX PubMed=10779515; DOI=10.1074/jbc.m002366200; RA Feinberg H., Park-Snyder S., Kolatkar A.R., Heise C.T., Taylor M.E., RA Weis W.I.; RT "Structure of a C-type carbohydrate recognition domain from the macrophage RT mannose receptor."; RL J. Biol. Chem. 275:21539-21548(2000). RN [13] RP POLYMORPHISM, POSSIBLE ASSOCIATION OF VARIANT SER-396 WITH RESISTANCE TO RP LEPROSY, VARIANTS ILE-167; ALA-399 AND PHE-407, AND SUBCELLULAR LOCATION. RX PubMed=20035344; DOI=10.1007/s00439-009-0775-x; RA Alter A., de Leseleuc L., Van Thuc N., Thai V.H., Huong N.T., Ba N.N., RA Cardoso C.C., Grant A.V., Abel L., Moraes M.O., Alcais A., Schurr E.; RT "Genetic and functional analysis of common MRC1 exon 7 polymorphisms in RT leprosy susceptibility."; RL Hum. Genet. 127:337-348(2010). CC -!- FUNCTION: Mediates the endocytosis of glycoproteins by macrophages. CC Binds both sulfated and non-sulfated polysaccharide chains. CC -!- FUNCTION: (Microbial infection) Acts as a phagocytic receptor for CC bacteria, fungi and other pathogens. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Dengue virus CC envelope protein E. {ECO:0000269|PubMed:18266465}. CC -!- FUNCTION: (Microbial infection) Interacts with Hepatitis B virus CC envelope protein. {ECO:0000269|PubMed:19683778}. CC -!- SUBUNIT: (Microbial infection) Interacts with Dengue virus. CC {ECO:0000269|PubMed:18266465}. CC -!- SUBUNIT: (Microbial infection) May act as a receptor for hepatitis B CC virus, enabling uptake of the virus in hepatic dendritic cells. CC {ECO:0000269|PubMed:19683778}. CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:20035344}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:20035344}. Cell CC membrane {ECO:0000269|PubMed:20035344}; Single-pass type I membrane CC protein {ECO:0000269|PubMed:20035344}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P22897-1; Sequence=Displayed; CC Name=2; CC IsoId=P22897-2; Sequence=VSP_041340, VSP_041341; CC -!- DOMAIN: The C-type lectin domains, also called carbohydrate-recognition CC domains or CRDs, 1-3 have at most very weak affinity for carbohydrates. CC C-type lectin domain 4 shows the highest affinity binding and has CC multispecificity for a variety of monosaccharides. At least 3 C-type CC lectin domains (4, 5, and 7) are required for high affinity binding and CC endocytosis of multivalent glycoconjugates. CC {ECO:0000269|PubMed:1730714}. CC -!- POLYMORPHISM: Genetic variations in MRC1 may influence susceptibility CC or resistance to leprosy in some populations. Particularly, Gly-396 CC seems to be a risk factor for leprosy when associated with Ala-399 and CC Phe-407. CC -!- SEQUENCE CAUTION: CC Sequence=CAH70733.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAH71176.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI15339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Macrophage mannose receptor; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_00127"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44561/MRC1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05550; AAA59868.1; -; mRNA. DR EMBL; X55635; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M93221; AAA60389.1; -; Genomic_DNA. DR EMBL; M93192; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93193; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93194; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93195; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93196; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93197; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93198; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93199; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93200; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93201; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93202; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93203; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93204; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93205; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93206; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93207; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93208; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93209; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93210; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93211; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93212; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93213; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93214; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93215; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93216; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93217; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93218; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93219; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; M93220; AAA60389.1; JOINED; Genomic_DNA. DR EMBL; EF444997; ACA06020.1; -; Genomic_DNA. DR EMBL; AL928729; CAH70733.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC069023; CAH70733.1; JOINED; Genomic_DNA. DR EMBL; AL928580; CAH71176.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL139238; CAH71176.1; JOINED; Genomic_DNA. DR EMBL; BX255924; CAH71176.1; JOINED; Genomic_DNA. DR EMBL; BX255924; CAI15339.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL139238; CAI15339.1; JOINED; Genomic_DNA. DR EMBL; AL928580; CAI15339.1; JOINED; Genomic_DNA. DR EMBL; BC142642; AAI42643.1; -; mRNA. DR CCDS; CCDS7123.2; -. [P22897-1] DR PIR; A36563; A36563. DR RefSeq; NP_002429.1; NM_002438.3. [P22897-1] DR PDB; 1EGG; X-ray; 2.30 A; A/B=644-787. DR PDB; 1EGI; X-ray; 2.30 A; A/B=644-787. DR PDB; 5XTS; X-ray; 2.00 A; A=22-629. DR PDB; 5XTW; X-ray; 3.20 A; A/B/C/D/E/F/G/H=22-490. DR PDB; 6INN; X-ray; 3.00 A; A/B/C/D=22-629. DR PDB; 6INO; X-ray; 3.05 A; A/B=22-490. DR PDB; 6INU; X-ray; 2.65 A; A/B=22-490. DR PDB; 6INV; X-ray; 3.30 A; A=22-490. DR PDB; 6IOE; X-ray; 2.90 A; A/B=22-490. DR PDB; 7JUB; X-ray; 1.20 A; A=646-779. DR PDB; 7JUC; X-ray; 1.40 A; A=646-779. DR PDB; 7JUD; X-ray; 1.40 A; A/B=646-779. DR PDB; 7JUE; X-ray; 1.40 A; A=646-779. DR PDB; 7JUF; X-ray; 1.40 A; A/B=646-779. DR PDB; 7JUG; X-ray; 1.40 A; A=646-779. DR PDB; 7JUH; X-ray; 1.40 A; A=646-779. DR PDB; 7L61; X-ray; 1.35 A; A=646-779. DR PDB; 7L62; X-ray; 1.55 A; A=646-779. DR PDB; 7L63; X-ray; 1.65 A; A=646-779. DR PDB; 7L64; X-ray; 1.35 A; A=646-779. DR PDB; 7L65; X-ray; 1.35 A; A=646-779. DR PDB; 7L66; X-ray; 1.75 A; A=646-779. DR PDB; 7L67; X-ray; 1.20 A; A=646-779. DR PDB; 7L68; X-ray; 1.40 A; A/B=646-779. DR PDBsum; 1EGG; -. DR PDBsum; 1EGI; -. DR PDBsum; 5XTS; -. DR PDBsum; 5XTW; -. DR PDBsum; 6INN; -. DR PDBsum; 6INO; -. DR PDBsum; 6INU; -. DR PDBsum; 6INV; -. DR PDBsum; 6IOE; -. DR PDBsum; 7JUB; -. DR PDBsum; 7JUC; -. DR PDBsum; 7JUD; -. DR PDBsum; 7JUE; -. DR PDBsum; 7JUF; -. DR PDBsum; 7JUG; -. DR PDBsum; 7JUH; -. DR PDBsum; 7L61; -. DR PDBsum; 7L62; -. DR PDBsum; 7L63; -. DR PDBsum; 7L64; -. DR PDBsum; 7L65; -. DR PDBsum; 7L66; -. DR PDBsum; 7L67; -. DR PDBsum; 7L68; -. DR AlphaFoldDB; P22897; -. DR SASBDB; P22897; -. DR SMR; P22897; -. DR BioGRID; 110500; 4. DR DIP; DIP-101N; -. DR IntAct; P22897; 4. DR STRING; 9606.ENSP00000455897; -. DR BindingDB; P22897; -. DR ChEMBL; CHEMBL2176854; -. DR DrugBank; DB09266; Technetium Tc-99m tilmanocept. DR UniLectin; P22897; -. DR GlyConnect; 1956; 26 N-Linked glycans (6 sites). DR GlyCosmos; P22897; 12 sites, 32 glycans. DR GlyGen; P22897; 12 sites, 30 N-linked glycans (6 sites), 2 O-linked glycans (4 sites). DR iPTMnet; P22897; -. DR PhosphoSitePlus; P22897; -. DR BioMuta; MRC1; -. DR DMDM; 126730; -. DR jPOST; P22897; -. DR MassIVE; P22897; -. DR PaxDb; 9606-ENSP00000455897; -. DR PeptideAtlas; P22897; -. DR ProteomicsDB; 54048; -. [P22897-1] DR ProteomicsDB; 54049; -. [P22897-2] DR ABCD; P22897; 1 sequenced antibody. DR Antibodypedia; 72990; 951 antibodies from 43 providers. DR DNASU; 4360; -. DR Ensembl; ENST00000569591.3; ENSP00000455897.1; ENSG00000260314.3. [P22897-1] DR GeneID; 4360; -. DR KEGG; hsa:4360; -. DR MANE-Select; ENST00000569591.3; ENSP00000455897.1; NM_002438.4; NP_002429.1. DR UCSC; uc031ptj.2; human. [P22897-1] DR AGR; HGNC:7228; -. DR CTD; 4360; -. DR DisGeNET; 4360; -. DR GeneCards; MRC1; -. DR HGNC; HGNC:7228; MRC1. DR HPA; ENSG00000260314; Tissue enhanced (lung). DR MIM; 153618; gene. DR neXtProt; NX_P22897; -. DR OpenTargets; ENSG00000260314; -. DR PharmGKB; PA30933; -. DR VEuPathDB; HostDB:ENSG00000260314; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT01050000244842; -. DR HOGENOM; CLU_002069_0_0_1; -. DR InParanoid; P22897; -. DR OMA; WIDKWRV; -. DR OrthoDB; 4271106at2759; -. DR PhylomeDB; P22897; -. DR TreeFam; TF316663; -. DR PathwayCommons; P22897; -. DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-HSA-9637628; Modulation by Mtb of host immune system. DR SignaLink; P22897; -. DR SIGNOR; P22897; -. DR BioGRID-ORCS; 4360; 7 hits in 1052 CRISPR screens. DR ChiTaRS; MRC1; human. DR EvolutionaryTrace; P22897; -. DR GenomeRNAi; 4360; -. DR Pharos; P22897; Tbio. DR PRO; PR:P22897; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P22897; Protein. DR Bgee; ENSG00000260314; Expressed in lower lobe of lung and 187 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB. DR GO; GO:0005537; F:mannose binding; TAS:ProtInc. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:Ensembl. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB. DR CDD; cd00037; CLECT; 7. DR CDD; cd00062; FN2; 1. DR CDD; cd00161; RICIN; 1. DR Gene3D; 2.80.10.50; -; 1. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8. DR InterPro; IPR001304; C-type_lectin-like. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR018378; C-type_lectin_CS. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR035992; Ricin_B-like_lectins. DR InterPro; IPR000772; Ricin_B_lectin. DR PANTHER; PTHR22803:SF104; MACROPHAGE MANNOSE RECEPTOR 1; 1. DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1. DR Pfam; PF00040; fn2; 1. DR Pfam; PF00059; Lectin_C; 8. DR Pfam; PF00652; Ricin_B_lectin; 1. DR PRINTS; PR00013; FNTYPEII. DR SMART; SM00034; CLECT; 8. DR SMART; SM00059; FN2; 1. DR SMART; SM00458; RICIN; 1. DR SUPFAM; SSF56436; C-type lectin-like; 8. DR SUPFAM; SSF57440; Kringle-like; 1. DR SUPFAM; SSF50370; Ricin B-like lectins; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 6. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 1. DR PROSITE; PS50231; RICIN_B_LECTIN; 1. DR Genevisible; P22897; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; KW Direct protein sequencing; Disulfide bond; Endocytosis; Endosome; KW Glycoprotein; Host cell receptor for virus entry; Host-virus interaction; KW Lectin; Membrane; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..1456 FT /note="Macrophage mannose receptor 1" FT /id="PRO_0000017548" FT TOPO_DOM 19..1389 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 1390..1410 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1411..1456 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 22..142 FT /note="Ricin B-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT DOMAIN 163..211 FT /note="Fibronectin type-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479" FT DOMAIN 225..341 FT /note="C-type lectin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 369..487 FT /note="C-type lectin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 511..626 FT /note="C-type lectin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 655..778 FT /note="C-type lectin 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 807..923 FT /note="C-type lectin 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 952..1080 FT /note="C-type lectin 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 1102..1213 FT /note="C-type lectin 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DOMAIN 1241..1356 FT /note="C-type lectin 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 344 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 529 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 926 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 930 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1160 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18780401" FT DISULFID 35..49 FT /evidence="ECO:0000250" FT DISULFID 74..91 FT /evidence="ECO:0000250" FT DISULFID 168..194 FT /evidence="ECO:0000250" FT DISULFID 182..209 FT /evidence="ECO:0000250" FT DISULFID 247..340 FT /evidence="ECO:0000250" FT DISULFID 316..332 FT /evidence="ECO:0000250" FT DISULFID 391..486 FT /evidence="ECO:0000250" FT DISULFID 463..478 FT /evidence="ECO:0000250" FT DISULFID 532..625 FT /evidence="ECO:0000250" FT DISULFID 600..617 FT /evidence="ECO:0000250" FT DISULFID 646..659 FT DISULFID 680..777 FT DISULFID 753..769 FT DISULFID 828..922 FT /evidence="ECO:0000250" FT DISULFID 899..914 FT /evidence="ECO:0000250" FT DISULFID 977..1079 FT /evidence="ECO:0000250" FT DISULFID 1052..1071 FT /evidence="ECO:0000250" FT DISULFID 1123..1212 FT /evidence="ECO:0000250" FT DISULFID 1190..1204 FT /evidence="ECO:0000250" FT DISULFID 1263..1355 FT /evidence="ECO:0000250" FT DISULFID 1332..1347 FT /evidence="ECO:0000250" FT VAR_SEQ 470..498 FT /note="DGYWADRGCEWPLGYICKMKSRSQGPEIV -> AGVQWHNLGSMQPLPREFK FT RFSCLSLPSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041340" FT VAR_SEQ 499..1456 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_041341" FT VARIANT 167 FT /note="T -> I (in dbSNP:rs2296414)" FT /evidence="ECO:0000269|PubMed:20035344" FT /id="VAR_019700" FT VARIANT 396 FT /note="G -> S (protective factor against leprosy; FT dbSNP:rs606231248)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_065250" FT VARIANT 399 FT /note="T -> A (in dbSNP:rs71497223)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:20035344" FT /id="VAR_065251" FT VARIANT 407 FT /note="L -> F (in dbSNP:rs71497225)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:20035344" FT /id="VAR_065252" FT CONFLICT 1334 FT /note="A -> T (in Ref. 2; X55635)" FT /evidence="ECO:0000305" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 30..33 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 43..48 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 69..72 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 73..76 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 116..118 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:6INU" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:6INV" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 148..151 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 161..165 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 177..181 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 229..238 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:6IOE" FT STRAND 316..319 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 336..342 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 372..382 FT /evidence="ECO:0007829|PDB:5XTS" FT HELIX 384..393 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:6INU" FT HELIX 404..412 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 421..427 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:6INV" FT HELIX 456..458 FT /evidence="ECO:0007829|PDB:6INU" FT STRAND 463..467 FT /evidence="ECO:0007829|PDB:5XTS" FT TURN 468..471 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 472..476 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 478..480 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 482..489 FT /evidence="ECO:0007829|PDB:5XTS" FT STRAND 509..511 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 514..518 FT /evidence="ECO:0007829|PDB:6INN" FT HELIX 525..534 FT /evidence="ECO:0007829|PDB:6INN" FT HELIX 545..554 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 555..559 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 561..572 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 575..577 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 599..604 FT /evidence="ECO:0007829|PDB:6INN" FT HELIX 606..608 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 612..615 FT /evidence="ECO:0007829|PDB:6INN" FT STRAND 624..628 FT /evidence="ECO:0007829|PDB:6INN" FT TURN 648..650 FT /evidence="ECO:0007829|PDB:7L67" FT STRAND 655..657 FT /evidence="ECO:0007829|PDB:7JUD" FT STRAND 659..663 FT /evidence="ECO:0007829|PDB:7JUB" FT HELIX 667..669 FT /evidence="ECO:0007829|PDB:7L67" FT HELIX 673..682 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:7JUD" FT HELIX 693..706 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 712..719 FT /evidence="ECO:0007829|PDB:7JUB" FT TURN 722..724 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 726..728 FT /evidence="ECO:0007829|PDB:7JUB" FT HELIX 747..749 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 753..757 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 764..767 FT /evidence="ECO:0007829|PDB:7JUB" FT STRAND 773..779 FT /evidence="ECO:0007829|PDB:7JUB" SQ SEQUENCE 1456 AA; 166012 MW; 264E5AF3C576A5E3 CRC64; MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN QDAESQKFRW VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS IHTIEELDFI ISQLGYEPND ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKD GYWADRGCEW PLGYICKMKS RSQGPEIVEV EKGCRKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT TIEDRYEQAF LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW GASSRTSLCF KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW RLITASGSYH KLFWLGLTYG SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP TMSWNDINCE HLNNWICQIQ KGQTPKPEPT PAPQDNPPVT EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTMPS VPSGCKEGWN FYSNKCFKIF GFMEEERKNW QEARKACIGF GGNLVSIQNE KEQAFLTYHM KDSTFSAWTG LNDVNSEHTF LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA DCVVIIGGAS NEAGKWMDDT CDSKRGYICQ TRSDPSLTNP PATIQTDGFV KYGKSSYSLM RQKFQWHEAE TYCKLHNSLI ASILDPYSNA FAWLQMETSN ERVWIALNSN LTDNQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK TAHCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES SYTRNWGQAS LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF RNVEGTWLWI NNSPVSFVNW NTGDPSGERN DCVALHASSG FWSNIHCSSY KGYICKRPKI IDAKPTHELL TTKADTRKMD PSKPSSNVAG VVIIVILLIL TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD MKDLVGNIEQ NEHSVI //