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P22897 (MRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Macrophage mannose receptor 1

Short name=MMR
Alternative name(s):
C-type lectin domain family 13 member D
C-type lectin domain family 13 member D-like
Macrophage mannose receptor 1-like protein 1
CD_antigen=CD206
Gene names
Name:MRC1
Synonyms:CLEC13D, CLEC13DL, MRC1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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

Endosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein Ref.10.

Polymorphism

Genetic variations in MRC1 may influence susceptibility or resistance to leprosy in some populations. Particularly, Gly-396 seems to be a risk factor for leprosy when associated with Ala-399 and Phe-407.

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.

Sequence caution

The sequence CAH70733.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH70872.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAH71176.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI15339.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22897-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P22897-2)

The sequence of this isoform differs from the canonical sequence as follows:
     470-498: DGYWADRGCEWPLGYICKMKSRSQGPEIV → AGVQWHNLGSMQPLPREFKRFSCLSLPSS
     499-1456: Missing.
Note: No experimental confirmation available.

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 – 141021Helical; 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.8
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

Alternative sequence470 – 49829DGYWA…GPEIV → AGVQWHNLGSMQPLPREFKR FSCLSLPSS in isoform 2.
VSP_041340
Alternative sequence499 – 1456958Missing in isoform 2.
VSP_041341
Natural variant1671T → I. Ref.10
Corresponds to variant rs2296414 [ dbSNP | Ensembl ].
VAR_019700
Natural variant3961G → S Probably protective against leprosy when associated with A-399 and F-407. Ref.6 Ref.10
Corresponds to variant rs1926736 [ dbSNP | Ensembl ].
VAR_065250
Natural variant3991T → A. Ref.6 Ref.10
Corresponds to variant rs35950447 [ dbSNP | Ensembl ].
VAR_065251
Natural variant4071L → F. Ref.6 Ref.10
Corresponds to variant rs2437257 [ dbSNP | Ensembl ].
VAR_065252

Experimental info

Sequence conflict13341A → T in X55635. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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 

« Hide

Isoform 2 [UniParc].

Checksum: 1305DE544A35A7F4
Show »

FASTA49856,554

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS SER-396; ALA-399 AND PHE-407.
[7]"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] [Europe PMC] [Abstract]
Cited for: STUDIES ON THE BINDING OF INDIVIDUAL LECTIN DOMAINS.
[8]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1205.
Tissue: Milk.
[9]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 642-788.
[10]"Genetic and functional analysis of common MRC1 exon 7 polymorphisms in leprosy susceptibility."
Alter A., de Leseleuc L., Van Thuc N., Thai V.H., Huong N.T., Ba N.N., Cardoso C.C., Grant A.V., Abel L., Moraes M.O., Alcais A., Schurr E.
Hum. Genet. 127:337-348(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, POSSIBLE ASSOCIATION OF VARIANT SER-396 WITH RESISTANCE TO LEPROSY, VARIANTS ILE-167; ALA-399 AND PHE-407, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
EF444997 Genomic DNA. Translation: ACA06020.1.
AL928729, AC069023 Genomic DNA. Translation: CAH70733.1. Sequence problems.
AL139238, AL928580, BX255924 Genomic DNA. Translation: CAH70872.1. Sequence problems.
AL928580, AL139238, BX255924 Genomic DNA. Translation: CAH71176.1. Sequence problems.
BX255924, AL139238, AL928580 Genomic DNA. Translation: CAI15339.1. Sequence problems.
BC142642 mRNA. Translation: AAI42643.1.
CCDSCCDS7123.1. [P22897-1]
PIRA36563.
RefSeqNP_002429.1. NM_002438.3. [P22897-1]
UniGeneHs.743903.
Hs.75182.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGGX-ray2.30A/B644-787[»]
1EGIX-ray2.30A/B644-787[»]
ProteinModelPortalP22897.
SMRP22897. Positions 21-154, 161-348, 362-487, 504-629, 644-786, 803-1079, 1095-1215, 1230-1357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110500. 2 interactions.
DIPDIP-101N.
IntActP22897. 2 interactions.
MINTMINT-2801902.
STRING9606.ENSP00000239761.

Chemistry

ChEMBLCHEMBL2176854.

Protein family/group databases

MEROPSI63.001.

PTM databases

PhosphoSiteP22897.

Polymorphism databases

DMDM126730.

Proteomic databases

PaxDbP22897.
PRIDEP22897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000239761; ENSP00000239761; ENSG00000120586. [P22897-1]
ENST00000569591; ENSP00000455897; ENSG00000260314. [P22897-1]
GeneID4360.
KEGGhsa:4360.
UCSCuc001ipk.4. human. [P22897-1]

Organism-specific databases

CTD4360.
GeneCardsGC10P018098.
H-InvDBHIX0035369.
HGNCHGNC:7228. MRC1.
HPAHPA004114.
HPA045134.
MIM153618. gene.
neXtProtNX_P22897.
PharmGKBPA134941260.
PA30933.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288621.
HOGENOMHOG000113647.
HOVERGENHBG107130.
InParanoidQ5VSK2.
KOK06560.
OMARNERNIM.
OrthoDBEOG7FFMQR.
PhylomeDBP22897.
TreeFamTF316663.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP22897.
CleanExHS_MRC1.
GenevestigatorP22897.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
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

EvolutionaryTraceP22897.
GenomeRNAi4360.
NextBio17159.
PROP22897.
SOURCESearch...

Entry information

Entry nameMRC1_HUMAN
AccessionPrimary (citable) accession number: P22897
Secondary accession number(s): A5PKW3, Q5VSJ2, Q5VSK2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries