Q61830 · MRC1_MOUSE

  • Protein
    Macrophage mannose receptor 1
  • Gene
    Mrc1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell surface
Cellular Componentendosome membrane
Cellular Componentplasma membrane
Molecular Functioncargo receptor activity
Molecular FunctionD-mannose binding
Molecular Functionsignaling receptor activity
Molecular Functiontransmembrane signaling receptor activity
Biological Processcellular response to interleukin-4
Biological Processcellular response to lipopolysaccharide
Biological Processcellular response to type II interferon
Biological Processreceptor-mediated endocytosis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Macrophage mannose receptor 1
  • Short names
    MMR
  • CD Antigen Name
    • CD206

Gene names

    • Name
      Mrc1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q61830
  • Secondary accessions
    • Q8C502

Proteomes

Organism-specific databases

Subcellular Location

Endosome membrane
; Single-pass type I membrane protein
Cell membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-1388Extracellular
Transmembrane1389-1409Helical
Topological domain1410-1456Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000001754920-1456Macrophage mannose receptor 1
Disulfide bond35↔49
Disulfide bond74↔91
Disulfide bond102↔149
Glycosylation104N-linked (GlcNAc...) asparagine
Disulfide bond168↔194
Disulfide bond182↔209
Disulfide bond247↔340
Disulfide bond316↔332
Glycosylation344N-linked (GlcNAc...) asparagine
Disulfide bond391↔486
Disulfide bond463↔478
Glycosylation529N-linked (GlcNAc...) asparagine
Disulfide bond532↔625
Disulfide bond600↔617
Disulfide bond680↔777
Disulfide bond753↔769
Disulfide bond828↔922
Disulfide bond899↔914
Glycosylation926N-linked (GlcNAc...) asparagine
Glycosylation930N-linked (GlcNAc...) asparagine
Disulfide bond976↔1078
Disulfide bond1051↔1070
Disulfide bond1122↔1211
Glycosylation1159N-linked (GlcNAc...) asparagine
Disulfide bond1189↔1203
Glycosylation1204N-linked (GlcNAc...) asparagine
Disulfide bond1262↔1354
Disulfide bond1331↔1346

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in macrophages.

Induction

Down-regulated by interferon gamma.

Gene expression databases

Interaction

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
XENO Q61830S P0DTC22EBI-642509, EBI-25474821

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-142Ricin B-type lectin
Domain163-211Fibronectin type-II
Domain225-341C-type lectin 1
Domain369-487C-type lectin 2
Domain511-626C-type lectin 3
Domain655-778C-type lectin 4
Domain807-923C-type lectin 5
Domain951-1079C-type lectin 6
Domain1101-1212C-type lectin 7
Domain1240-1355C-type lectin 8

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,456
  • Mass (Da)
    164,981
  • Last updated
    2011-07-27 v2
  • Checksum
    FD568C1B812214D2
MRLLLLLAFISVIPVSVQLLDARQFLIYNEDHKRCVDALSAISVQTATCNPEAESQKFRWVSDSQIMSVAFKLCLGVPSKTDWASVTLYACDSKSEYQKWECKNDTLFGIKGTELYFNYGNRQEKNIKLYKGSGLWSRWKVYGTTDDLCSRGYEAMYSLLGNANGAVCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDKDKLFGFCPLHFEGSERLWNKDPLTGILYQINSKSALTWHQARASCKQQNADLLSVTEIHEQMYLTGLTSSLSSGLWIGLNSLSVRSGWQWAGGSPFRYLNWLPGSPSSEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNNTLNPFIIPSASDVPTGCPNQWWPYAGHCYRIHREEKKIQKYALQACRKEGGDLASIHSIEEFDFIFSQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLPGEPSHENNRQEDCVVMKGKDGYWADRACEQPLGYICKMVSQSHAVVPEGADKGCRKGWKRHGFYCYLIGSTLSTFTDANHTCTNEKAYLTTVEDRYEQAFLTSLVGLRPEKYFWTGLSDVQNKGTFRWTVDEQVQFTHWNADMPGRKAGCVAMKTGVAGGLWDVLSCEEKAKFVCKHWAEGVTRPPEPTTTPEPKCPENWGTTSKTSMCFKLYAKGKHEKKTWFESRDFCKAIGGELASIKSKDEQQVIWRLITSSGSYHELFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPGMSWNDINCEHLNNWICQIQKGKTLLPEPTPAPQDNPPVTADGWVIYKDYQYYFSKEKETMDNARAFCKKNFGDLATIKSESEKKFLWKYINKNGGQSPYFIGMLISMDKKFIWMDGSKVDFVAWATGEPNFANDDENCVTMYTNSGFWNDINCGYPNNFICQRHNSSINATAMPTTPTTPGGCKEGWHLYKNKCFKIFGFANEEKKSWQDARQACKGLKGNLVSIENAQEQAFVTYHMRDSTFNAWTGLNDINAEHMFLWTAGQGVHYTNWGKGYPGGRRSSLSYEDADCVVVIGGNSREAGTWMDDTCDSKQGYICQTQTDPSLPVSPTTTPKDGFVTYGKSSYSLMKLKLPWHEAETYCKDHTSLLASILDPYSNAFAWMKMHPFNVPIWIALNSNLTNNEYTWTDRWRVRYTNWGADEPKLKSACVYMDVDGYWRTSYCNESFYFLCKKSDEIPATEPPQLPGKCPESEQTAWIPFYGHCYYFESSFTRSWGQASLECLRMGASLVSIETAAESSFLSYRVEPLKSKTNFWIGMFRNVEGKWLWLNDNPVSFVNWKTGDPSGERNDCVVLASSSGLWNNIHCSSYKGFICKMPKIIDPVTTHSSITTKADQRKMDPQPKGSSKAAGVVTVVLLIVIGAGVAAYFFYKKRHALHIPQEATFENTLYFNSNLSPGTSDTKDLMGNIEQNEHAII

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict826in Ref. 1; CAA78028

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z11974
EMBL· GenBank· DDBJ
CAA78028.1
EMBL· GenBank· DDBJ
mRNA
AL845290
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL845434
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AK079897
EMBL· GenBank· DDBJ
BAC37778.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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