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P22897

- MRC1_HUMAN

UniProt

P22897 - MRC1_HUMAN

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Protein
Macrophage mannose receptor 1
Gene
MRC1, CLEC13D, CLEC13DL, MRC1L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 - Molecular functioni

  1. mannose binding Source: ProtInc
  2. protein binding Source: MTBBASE
  3. receptor activity Source: UniProtKB

GO - Biological processi

  1. receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Lectin

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

Protein family/group databases

MEROPSiI63.001.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:MRC1
Synonyms:CLEC13D, CLEC13DL, MRC1L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:7228. MRC1.

Subcellular locationi

Endosome membrane; Single-pass type I membrane protein. Cell membrane; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 13891371Extracellular Reviewed prediction
Add
BLAST
Transmembranei1390 – 141021Helical; Reviewed prediction
Add
BLAST
Topological domaini1411 – 145646Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endosome membrane Source: UniProtKB
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134941260.
PA30933.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 14561438Macrophage mannose receptor 1
PRO_0000017548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 49 By similarity
Disulfide bondi74 ↔ 91 By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi168 ↔ 194 By similarity
Disulfide bondi182 ↔ 209 By similarity
Disulfide bondi247 ↔ 340 By similarity
Disulfide bondi316 ↔ 332 By similarity
Glycosylationi344 – 3441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi391 ↔ 486 By similarity
Disulfide bondi463 ↔ 478 By similarity
Glycosylationi529 – 5291N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi532 ↔ 625 By similarity
Disulfide bondi600 ↔ 617 By similarity
Disulfide bondi646 ↔ 659
Disulfide bondi680 ↔ 777
Disulfide bondi753 ↔ 769
Disulfide bondi828 ↔ 922 By similarity
Disulfide bondi899 ↔ 914 By similarity
Glycosylationi926 – 9261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi930 – 9301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi977 ↔ 1079 By similarity
Disulfide bondi1052 ↔ 1071 By similarity
Disulfide bondi1123 ↔ 1212 By similarity
Glycosylationi1160 – 11601N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1190 ↔ 1204 By similarity
Glycosylationi1205 – 12051N-linked (GlcNAc...)1 Publication
Disulfide bondi1263 ↔ 1355 By similarity
Glycosylationi1311 – 13111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1332 ↔ 1347 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP22897.
PRIDEiP22897.

PTM databases

PhosphoSiteiP22897.

Expressioni

Gene expression databases

BgeeiP22897.
CleanExiHS_MRC1.
GenevestigatoriP22897.

Organism-specific databases

HPAiHPA004114.
HPA045134.

Interactioni

Protein-protein interaction databases

BioGridi110500. 2 interactions.
DIPiDIP-101N.
IntActiP22897. 2 interactions.
MINTiMINT-2801902.
STRINGi9606.ENSP00000239761.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi654 – 6574
Beta strandi659 – 6635
Helixi667 – 6693
Helixi673 – 6819
Turni682 – 6843
Beta strandi685 – 6873
Helixi693 – 70614
Beta strandi712 – 7187
Helixi746 – 7483
Beta strandi752 – 7576
Beta strandi764 – 7685
Beta strandi773 – 7786

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EGGX-ray2.30A/B644-787[»]
1EGIX-ray2.30A/B644-787[»]
ProteinModelPortaliP22897.
SMRiP22897. Positions 21-154, 161-348, 362-487, 504-629, 644-786, 803-1079, 1095-1215, 1230-1357.

Miscellaneous databases

EvolutionaryTraceiP22897.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 142121Ricin B-type lectin
Add
BLAST
Domaini163 – 21149Fibronectin type-II
Add
BLAST
Domaini225 – 341117C-type lectin 1
Add
BLAST
Domaini369 – 487119C-type lectin 2
Add
BLAST
Domaini511 – 626116C-type lectin 3
Add
BLAST
Domaini655 – 778124C-type lectin 4
Add
BLAST
Domaini807 – 923117C-type lectin 5
Add
BLAST
Domaini952 – 1080129C-type lectin 6
Add
BLAST
Domaini1102 – 1213112C-type lectin 7
Add
BLAST
Domaini1241 – 1356116C-type lectin 8
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG288621.
HOGENOMiHOG000113647.
HOVERGENiHBG107130.
InParanoidiQ5VSK2.
KOiK06560.
OMAiRNERNIM.
OrthoDBiEOG7FFMQR.
PhylomeDBiP22897.
TreeFamiTF316663.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. 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]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P22897-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVDAVS PSAVQTAACN     50
QDAESQKFRW VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW 100
ECKNDTLLGI KGEDLFFNYG NRQEKNIMLY KGSGLWSRWK IYGTTDNLCS 150
RGYEAMYTLL GNANGATCAF PFKFENKWYA DCTSAGRSDG WLWCGTTTDY 200
DTDKLFGYCP LKFEGSESLW NKDPLTSVSY QINSKSALTW HQARKSCQQQ 250
NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY 300
LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF 350
VIPSESDVPT HCPSQWWPYA GHCYKIHRDE KKIQRDALTT CRKEGGDLTS 400
IHTIEELDFI ISQLGYEPND ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR 450
GEPSHENNRQ EDCVVMKGKD GYWADRGCEW PLGYICKMKS RSQGPEIVEV 500
EKGCRKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT TIEDRYEQAF 550
LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC 600
VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW 650
GASSRTSLCF KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW 700
RLITASGSYH KLFWLGLTYG SPSEGFTWSD GSPVSYENWA YGEPNNYQNV 750
EYCGELKGDP TMSWNDINCE HLNNWICQIQ KGQTPKPEPT PAPQDNPPVT 800
EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS ESEKKFLWKY 850
VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV 900
TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTMPS VPSGCKEGWN 950
FYSNKCFKIF GFMEEERKNW QEARKACIGF GGNLVSIQNE KEQAFLTYHM 1000
KDSTFSAWTG LNDVNSEHTF LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA 1050
DCVVIIGGAS NEAGKWMDDT CDSKRGYICQ TRSDPSLTNP PATIQTDGFV 1100
KYGKSSYSLM RQKFQWHEAE TYCKLHNSLI ASILDPYSNA FAWLQMETSN 1150
ERVWIALNSN LTDNQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK 1200
TAHCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES 1250
SYTRNWGQAS LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF 1300
RNVEGTWLWI NNSPVSFVNW NTGDPSGERN DCVALHASSG FWSNIHCSSY 1350
KGYICKRPKI IDAKPTHELL TTKADTRKMD PSKPSSNVAG VVIIVILLIL 1400
TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD MKDLVGNIEQ 1450
NEHSVI 1456
Length:1,456
Mass (Da):166,012
Last modified:August 1, 1991 - v1
Checksum:i264E5AF3C576A5E3
GO
Isoform 2 (identifier: P22897-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     470-498: DGYWADRGCEWPLGYICKMKSRSQGPEIV → AGVQWHNLGSMQPLPREFKRFSCLSLPSS
     499-1456: Missing.

Note: No experimental confirmation available.

Show »
Length:498
Mass (Da):56,554
Checksum:i1305DE544A35A7F4
GO

Sequence cautioni

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.

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti167 – 1671T → I.1 Publication
Corresponds to variant rs2296414 [ dbSNP | Ensembl ].
VAR_019700
Natural varianti396 – 3961G → S Probably protective against leprosy when associated with A-399 and F-407. 2 Publications
Corresponds to variant rs1926736 [ dbSNP | Ensembl ].
VAR_065250
Natural varianti399 – 3991T → A.2 Publications
Corresponds to variant rs35950447 [ dbSNP | Ensembl ].
VAR_065251
Natural varianti407 – 4071L → F.2 Publications
Corresponds to variant rs2437257 [ dbSNP | Ensembl ].
VAR_065252

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei470 – 49829DGYWA…GPEIV → AGVQWHNLGSMQPLPREFKR FSCLSLPSS in isoform 2.
VSP_041340Add
BLAST
Alternative sequencei499 – 1456958Missing in isoform 2.
VSP_041341Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1334 – 13341A → T in X55635. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05550 mRNA. Translation: AAA59868.1.
X55635 mRNA. No translation available.
M93221
, 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.
CCDSiCCDS7123.1. [P22897-1]
PIRiA36563.
RefSeqiNP_002429.1. NM_002438.3. [P22897-1]
UniGeneiHs.743903.
Hs.75182.

Genome annotation databases

EnsembliENST00000239761; ENSP00000239761; ENSG00000120586. [P22897-1]
ENST00000569591; ENSP00000455897; ENSG00000260314. [P22897-1]
GeneIDi4360.
KEGGihsa:4360.
UCSCiuc001ipk.4. human. [P22897-1]

Polymorphism databases

DMDMi126730.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Macrophage mannose receptor

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05550 mRNA. Translation: AAA59868.1 .
X55635 mRNA. No translation available.
M93221
, 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 .
CCDSi CCDS7123.1. [P22897-1 ]
PIRi A36563.
RefSeqi NP_002429.1. NM_002438.3. [P22897-1 ]
UniGenei Hs.743903.
Hs.75182.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EGG X-ray 2.30 A/B 644-787 [» ]
1EGI X-ray 2.30 A/B 644-787 [» ]
ProteinModelPortali P22897.
SMRi P22897. Positions 21-154, 161-348, 362-487, 504-629, 644-786, 803-1079, 1095-1215, 1230-1357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110500. 2 interactions.
DIPi DIP-101N.
IntActi P22897. 2 interactions.
MINTi MINT-2801902.
STRINGi 9606.ENSP00000239761.

Chemistry

ChEMBLi CHEMBL2176854.

Protein family/group databases

MEROPSi I63.001.

PTM databases

PhosphoSitei P22897.

Polymorphism databases

DMDMi 126730.

Proteomic databases

PaxDbi P22897.
PRIDEi P22897.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000239761 ; ENSP00000239761 ; ENSG00000120586 . [P22897-1 ]
ENST00000569591 ; ENSP00000455897 ; ENSG00000260314 . [P22897-1 ]
GeneIDi 4360.
KEGGi hsa:4360.
UCSCi uc001ipk.4. human. [P22897-1 ]

Organism-specific databases

CTDi 4360.
GeneCardsi GC10P018098.
H-InvDB HIX0035369.
HGNCi HGNC:7228. MRC1.
HPAi HPA004114.
HPA045134.
MIMi 153618. gene.
neXtProti NX_P22897.
PharmGKBi PA134941260.
PA30933.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG288621.
HOGENOMi HOG000113647.
HOVERGENi HBG107130.
InParanoidi Q5VSK2.
KOi K06560.
OMAi RNERNIM.
OrthoDBi EOG7FFMQR.
PhylomeDBi P22897.
TreeFami TF316663.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

Miscellaneous databases

EvolutionaryTracei P22897.
GenomeRNAii 4360.
NextBioi 17159.
PROi P22897.
SOURCEi Search...

Gene expression databases

Bgeei P22897.
CleanExi HS_MRC1.
Genevestigatori P22897.

Family and domain databases

Gene3Di 2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProi IPR001304. 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 ]
Pfami PF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEi PS00615. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMRC1_HUMAN
AccessioniPrimary (citable) accession number: P22897
Secondary accession number(s): A5PKW3, Q5VSJ2, Q5VSK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 3, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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