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Reviewed, UniProtKB/Swiss-Prot P22897 (MRC1_HUMAN)

Last modified May 26, 2009. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Macrophage mannose receptor 1
      Short name=MMR
Alternative name(s):
    C-type lectin domain family 13 member D
    CD_antigen=CD206
Gene names
Name: MRC1
Synonyms: CLEC13D
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Miscellaneous

CRDs 1-3 have at most very weak affinity for carbohydrate. CRD 4 shows the highest affinity binding and has multispecificity for a variety of monosaccharides. At least 3 CRDs (4, 5, and 7) are required for high affinity binding and endocytosis of multivalent glycoconjugates.

Sequence similarities

Contains 8 C-type lectin domains.

Contains 1 fibronectin type-II domain.

Contains 1 ricin B-type lectin domain.

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Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
   LigandCalcium
Lectin
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processreceptor-mediated endocytosis Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: HPA

integral to plasma membrane Ref.3

Traceable author statement. Source: ProtInc

nucleus

Inferred from direct assay. Source: HPA

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mannose binding Ref.1

Traceable author statement. Source: ProtInc

receptor activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 14561438Macrophage mannose receptor 1
PRO_0000017548

Regions

Topological domain19 – 13891371Extracellular Potential
Transmembrane1390 – 141021 Potential
Topological domain1411 – 145646Cytoplasmic Potential
Domain22 – 142121Ricin B-type lectin
Domain163 – 21149Fibronectin type-II
Domain225 – 341117C-type lectin 1
Domain369 – 487119C-type lectin 2
Domain511 – 626116C-type lectin 3
Domain655 – 778124C-type lectin 4
Domain807 – 923117C-type lectin 5
Domain952 – 1080129C-type lectin 6
Domain1102 – 1213112C-type lectin 7
Domain1241 – 1356116C-type lectin 8

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation5291N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation9301N-linked (GlcNAc...) Potential
Glycosylation11601N-linked (GlcNAc...) Potential
Glycosylation12051N-linked (GlcNAc...) Ref.5
Glycosylation13111N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 49 By similarity
Disulfide bond74 ↔ 91 By similarity
Disulfide bond168 ↔ 194 By similarity
Disulfide bond182 ↔ 209 By similarity
Disulfide bond247 ↔ 340 By similarity
Disulfide bond316 ↔ 332 By similarity
Disulfide bond391 ↔ 486 By similarity
Disulfide bond463 ↔ 478 By similarity
Disulfide bond532 ↔ 625 By similarity
Disulfide bond600 ↔ 617 By similarity
Disulfide bond646 ↔ 659
Disulfide bond680 ↔ 777
Disulfide bond753 ↔ 769
Disulfide bond828 ↔ 922 By similarity
Disulfide bond899 ↔ 914 By similarity
Disulfide bond977 ↔ 1079 By similarity
Disulfide bond1052 ↔ 1071 By similarity
Disulfide bond1123 ↔ 1212 By similarity
Disulfide bond1190 ↔ 1204 By similarity
Disulfide bond1263 ↔ 1355 By similarity
Disulfide bond1332 ↔ 1347 By similarity

Natural variations

Natural variant1671T → I: dbSNP rs2296414.
VAR_019700

Experimental info

Sequence conflict13341A → T in X55635. Ref.2

Secondary structure

1 ........................ 1456
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P22897-1 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 264E5AF3C576A5E3

FASTA1,456166,012
        10         20         30         40         50         60 
MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN QDAESQKFRW 

        70         80         90        100        110        120 
VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG 

       130        140        150        160        170        180 
NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA 

       190        200        210        220        230        240 
DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW 

       250        260        270        280        290        300 
HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY 

       310        320        330        340        350        360 
LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT 

       370        380        390        400        410        420 
HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS IHTIEELDFI ISQLGYEPND 

       430        440        450        460        470        480 
ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKD GYWADRGCEW 

       490        500        510        520        530        540 
PLGYICKMKS RSQGPEIVEV EKGCRKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT 

       550        560        570        580        590        600 
TIEDRYEQAF LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC 

       610        620        630        640        650        660 
VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW GASSRTSLCF 

       670        680        690        700        710        720 
KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW RLITASGSYH KLFWLGLTYG 

       730        740        750        760        770        780 
SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP TMSWNDINCE HLNNWICQIQ 

       790        800        810        820        830        840 
KGQTPKPEPT PAPQDNPPVT EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS 

       850        860        870        880        890        900 
ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV 

       910        920        930        940        950        960 
TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTMPS VPSGCKEGWN FYSNKCFKIF 

       970        980        990       1000       1010       1020 
GFMEEERKNW QEARKACIGF GGNLVSIQNE KEQAFLTYHM KDSTFSAWTG LNDVNSEHTF 

      1030       1040       1050       1060       1070       1080 
LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA DCVVIIGGAS NEAGKWMDDT CDSKRGYICQ 

      1090       1100       1110       1120       1130       1140 
TRSDPSLTNP PATIQTDGFV KYGKSSYSLM RQKFQWHEAE TYCKLHNSLI ASILDPYSNA 

      1150       1160       1170       1180       1190       1200 
FAWLQMETSN ERVWIALNSN LTDNQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK 

      1210       1220       1230       1240       1250       1260 
TAHCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES SYTRNWGQAS 

      1270       1280       1290       1300       1310       1320 
LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF RNVEGTWLWI NNSPVSFVNW 

      1330       1340       1350       1360       1370       1380 
NTGDPSGERN DCVALHASSG FWSNIHCSSY KGYICKRPKI IDAKPTHELL TTKADTRKMD 

      1390       1400       1410       1420       1430       1440 
PSKPSSNVAG VVIIVILLIL TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD 

      1450 
MKDLVGNIEQ NEHSVI

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References

« Hide 'large scale' references
[1]"Primary structure of the mannose receptor contains multiple motifs resembling carbohydrate-recognition domains."
Taylor M.E., Conary J.T., Lennartz M.R., Stahl P.D., Drickamer K.
J. Biol. Chem. 265:12156-12162(1990) [PubMed: 2373685] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Placenta.
[2]"Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells."
Ezekowitz R.A., Sastry K., Bailly P., Warner A.
J. Exp. Med. 172:1785-1794(1990) [PubMed: 2258707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Organization of the gene encoding the human macrophage mannose receptor (MRC1)."
Kim S.J., Ruiz N., Bezouska K., Drickamer K.
Genomics 14:721-727(1992) [PubMed: 1294118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor."
Taylor M.E., Bezouska K., Drickamer K.
J. Biol. Chem. 267:1719-1726(1992) [PubMed: 1730714] [Abstract]
Cited for: STUDIES ON THE BINDING OF INDIVIDUAL LECTIN DOMAINS.
[5]"Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
Proteomics 8:3833-3847(2008) [PubMed: 18780401] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1205, MASS SPECTROMETRY.
Tissue: Milk.
[6]"Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor."
Feinberg H., Park-Snyder S., Kolatkar A.R., Heise C.T., Taylor M.E., Weis W.I.
J. Biol. Chem. 275:21539-21548(2000) [PubMed: 10779515] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 642-788.
+Additional computationally mapped references.

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Web resources

Functional Glycomics Gateway - Glycan Binding

Macrophage mannose receptor

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Cross-references

Sequence databases

J05550 mRNA. Translation: AAA59868.1.
X55635 mRNA. No translation available.
M93221 expand/collapse EMBL AC list , M93192, M93193, M93194, M93195, M93196, M93197, M93198, M93199, M93200, M93201, M93202, M93203, M93204, M93205, M93206, M93207, M93208, M93209, M93210, M93211, M93212, M93213, M93214, M93215, M93216, M93217, M93218, M93219, M93220 Genomic DNA. Translation: AAA60389.1.
IPIIPI00027848.
PIRA36563.
RefSeqNP_002429.1.
UniGeneHs.461247
Hs.75182

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EGGX-ray2.30A/B644-787[»]
1EGIX-ray2.30A/B644-787[»]
SMRP22897. Positions 21-154.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:101N.

PTM databases

PhosphoSiteP22897.

Proteomic databases

PRIDEP22897.

Genome annotation databases

EnsemblENSG00000120586. Homo sapiens. [Contig view]
GeneID4360.
KEGGhsa:4360.

Organism-specific databases

GeneCardsGC10P018138.
H-InvDBHIX0026040.
HIX0035369.
HGNCHGNC:7228. MRC1.
HPAHPA004114.
MIM153618. gene.
PharmGKBPA30933.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP22897.
HOVERGENP22897.
OMAP22897. LPCPDGW.

Gene expression databases

BgeeP22897.
CleanExHS_MRC1.

Family and domain databases

InterProIPR002353. AntifreezeII.
IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR000562. FN_type2_col_bd.
IPR000772. Ricin_B_lectin.
[Graphical view]
Gene3DG3DSA:3.10.100.10. C-type_lectin-like. 8 hits.
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSPR00356. ANTIFREEZEII.
PR00013. FNTYPEII.
ProDomPD000995. FN_Type_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
PROSITEPS00615. C_TYPE_LECTIN_1. 6 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio17159.
SOURCESearch...

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Entry information

Entry nameMRC1_HUMAN
AccessionPrimary (citable) accession number: P22897
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: May 26, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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PDB cross-references

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents