Protein detail
MRC1
Macrophage mannose receptor 1 (MMR) (C-type lectin domain family 13 member D) (C-type lectin domain family 13 member D-like) (Human mannose receptor) (hMR) (Macrophage mannose receptor 1-like protein 1) (CD antigen CD206)
Protein symbol MRC1 | UniProt ID | EVMP score 0.25 |
Frequency 5 | Transmembrane count 1 | Protein classification CD markersFDA approved drug targetsPlasma proteinsPredicted membrane proteins |
Basic Information
Protein Names
Macrophage mannose receptor 1 (MMR) (C-type lectin domain family 13 member D) (C-type lectin domain family 13 member D-like) (Human mannose receptor) (hMR) (Macrophage mannose receptor 1-like protein 1) (CD antigen CD206)
Protein Class
CD markersFDA approved drug targetsPlasma proteinsPredicted membrane proteins
Protein Function
- FDA approved drug targets:Small molecule drugs
- CD markers
Transmembrane
1390..1410; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
bA541I19.1CD206CLEC13DCLEC13DLMRC1L1
Gene Description
Mannose receptor C-type 1
Chromosome
10
Position
17809348-17911164
Frequency
5
EVMP Score
0.25
Fluorescence & Localization
Tissue SpecificesophagusCell SpecificB-cellsSingle-Nuclei Brain SpecificleukocyteBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway
Protein Function
- FDA approved drug targets:Small molecule drugs
- CD markers
Molecular Function
Biological Process
Reactome
- R-hsa-1280218 adaptive immune system
- R-hsa-1236975 antigen processing cross presentation
- R-hsa-9824439 bacterial infection pathways
- R-hsa-983169 class i mhc mediated antigen processing presentation
- R-hsa-1236978 cross presentation of soluble exogenous antigens endosomes
- R-hsa-9918485 dengue virus attachment and entry
- R-hsa-9839923 dengue virus infection
- R-hsa-9635486 infection with mycobacterium tuberculosis
- R-hsa-5663205 infectious disease
- R-hsa-9637628 modulation by mtb of host immune system
- R-hsa-9824446 viral infection pathways
Mediation Categories
Adhesion and uptake mediationClinical-translation mediationImmune mediationMetabolism mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
53 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor | receptor | CellPhoneDB | No | Yes | No | Yes | No |
| receptor | receptor | GO_Intercell | No | Yes | No | Yes | No |
| receptor | receptor | HPMR | No | Yes | No | Yes | No |
| receptor | receptor | CellChatDB | No | Yes | No | Yes | No |
| receptor | receptor | Surfaceome | No | Yes | No | Yes | No |
| scavenger | receptor | Almen2009 | No | Yes | No | Yes | No |
| mannose | receptor | Almen2009 | No | Yes | No | Yes | No |
| other_receptor_family | receptor | HPMR | No | Yes | No | Yes | No |
| scavenger | receptor | HPMR | No | Yes | No | Yes | No |
| mannose_scavenger | receptor | HPMR | No | Yes | No | Yes | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
Sequence, Structure & Domains
Sequences
Length
1,456
Mass
166,012
Sequence
MRLPLLLVFASVIPGAVLLLDTRQFLIYNEDHKRCVDAVSPSAVQTAACNQDAESQKFRWVSESQIMSVAFKLCLGVPSKTDWVAITLYACDSKSEFQKWECKNDTLLGIKGEDLFFNYGNRQEKNIMLYKGSGLWSRWKIYGTTDNLCSRGYEAMYTLLGNANGATCAFPFKFENKWYADCTSAGRSDGWLWCGTTTDYDTDKLFGYCPLKFEGSESLWNKDPLTSVSYQINSKSALTWHQARKSCQQQNAELLSITEIHEQTYLTGLTSSLTSGLWIGLNSLSFNSGWQWSDRSPFRYLNWLPGSPSAEPGKSCVSLNPGKNAKWENLECVQKLGYICKKGNTTLNSFVIPSESDVPTHCPSQWWPYAGHCYKIHRDEKKIQRDALTTCRKEGGDLTSIHTIEELDFIISQLGYEPNDELWIGLNDIKIQMYFEWSDGTPVTFTKWLRGEPSHENNRQEDCVVMKGKDGYWADRGCEWPLGYICKMKSRSQGPEIVEVEKGCRKGWKKHHFYCYMIGHTLSTFAEANQTCNNENAYLTTIEDRYEQAFLTSFVGLRPEKYFWTGLSDIQTKGTFQWTIEEEVRFTHWNSDMPGRKPGCVAMRTGIAGGLWDVLKCDEKAKFVCKHWAEGVTHPPKPTTTPEPKCPEDWGASSRTSLCFKLYAKGKHEKKTWFESRDFCRALGGDLASINNKEEQQTIWRLITASGSYHKLFWLGLTYGSPSEGFTWSDGSPVSYENWAYGEPNNYQNVEYCGELKGDPTMSWNDINCEHLNNWICQIQKGQTPKPEPTPAPQDNPPVTEDGWVIYKDYQYYFSKEKETMDNARAFCKRNFGDLVSIQSESEKKFLWKYVNRNDAQSAYFIGLLISLDKKFAWMDGSKVDYVSWATGEPNFANEDENCVTMYSNSGFWNDINCGYPNAFICQRHNSSINATTVMPTMPSVPSGCKEGWNFYSNKCFKIFGFMEEERKNWQEARKACIGFGGNLVSIQNEKEQAFLTYHMKDSTFSAWTGLNDVNSEHTFLWTDGRGVHYTNWGKGYPGGRRSSLSYEDADCVVIIGGASNEAGKWMDDTCDSKRGYICQTRSDPSLTNPPATIQTDGFVKYGKSSYSLMRQKFQWHEAETYCKLHNSLIASILDPYSNAFAWLQMETSNERVWIALNSNLTDNQYTWTDKWRVRYTNWAADEPKLKSACVYLDLDGYWKTAHCNESFYFLCKRSDEIPATEPPQLPGRCPESDHTAWIPFHGHCYYIESSYTRNWGQASLECLRMGSSLVSIESAAESSFLSYRVEPLKSKTNFWIGLFRNVEGTWLWINNSPVSFVNWNTGDPSGERNDCVALHASSGFWSNIHCSSYKGYICKRPKIIDAKPTHELLTTKADTRKMDPSKPSSNVAGVVIIVILLILTGAGLAAYFFYKKRRVHLPQEGAFENTLYFNSQSSPGTSDMKDLVGNIEQNEHSVI
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P22897-1; Sequence=Displayed; Name=2; IsoId=P22897-2; Sequence=VSP_041340, VSP_041341
Alternative Sequence
470..498; DGYWADRGCEWPLGYICKMKSRSQGPEIV -> AGVQWHNLGSMQPLPREFKRFSCLSLPSS (in isoform 2); 499..1456; Missing (in isoform 2)
3D Structural Models
Turn
30..33; 69..72; 104..106; 122..124; 148..151; 161..165; 224..226; 249..251; 270..272; 468..471; 648..650; 722..724
Helix
54..56; 96..98; 135..137; 200..203; 216..219; 240..248; 260..269; 321..323; 384..393; 404..412; 456..458; 525..534; 545..554; 606..608; 667..669; 673..682; 693..706; 747..749
Beta Strand
27..29; 34..40; 43..48; 58..60; 62..64; 66..68; 73..76; 78..85; 87..89; 100..103; 107..110; 116..118; 128..131; 138..141; 144..146; 170..174; 177..181; 193..199; 206..208; 220..222; 229..238; 277..282; 286..288; 290..292; 316..319; 327..330; 336..342; 367..369; 372..382; 396..398; 421..427; 429..431; 438..440; 463..467; 472..476; 478..480; 482..489; 509..511; 514..518; 555..559; 561..572; 575..577; 599..604; 612..615; 624..628; 655..657; 659..663; 685..687; 712..719; 726..728; 753..757; 764..767; 773..779
3D Structure
X-ray crystallography (24)
Domain & Motif Annotations
Domain (CC)
The C-type lectin domains, also called carbohydrate-recognition domains or CRDs, 1-3 have at most very weak affinity for carbohydrates. C-type lectin domain 4 shows the highest affinity binding and has multispecificity for a variety of monosaccharides. At least 3 C-type lectin domains (4, 5, and 7) are required for high affinity binding and endocytosis of multivalent glycoconjugates.
Domain (FT)
22..142; Ricin B-type lectin; 163..211; Fibronectin type-II; 225..341; C-type lectin 1; 369..487; C-type lectin 2; 511..626; C-type lectin 3; 655..778; C-type lectin 4; 807..923; C-type lectin 5; 952..1080; C-type lectin 6; 1102..1213; C-type lectin 7; 1241..1356; C-type lectin 8
Clinical Relevance
Disease Involvement
FDA approved drug targets
Related Diseases
Biomarker
Investigative; Approved
Drug Targets
FDA approved drug targets