MRC1_HUMAN
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 03-AUG-2022, entry version 232.
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 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="http://atlasgeneticsoncology.org/Genes/MRC1ID44561ch10p12.html";
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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 GlyGen; P22897; 12 sites, 26 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; P22897; -.
DR PeptideAtlas; P22897; -.
DR PRIDE; P22897; -.
DR ProteomicsDB; 54048; -. [P22897-1]
DR ProteomicsDB; 54049; -. [P22897-2]
DR Antibodypedia; 72990; 803 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 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; VPTDGFI; -.
DR OrthoDB; 29241at2759; -.
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 989 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 185 other tissues.
DR Genevisible; P22897; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
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:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 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 Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 8.
DR SUPFAM; SSF57440; SSF57440; 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.
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 (probably protective against leprosy when
FT associated with A-399 and F-407; 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
