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P22897

- MRC1_HUMAN

UniProt

P22897 - MRC1_HUMAN

Protein

Macrophage mannose receptor 1

Gene

MRC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    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

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

    GO - Cellular componenti

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

    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 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 14561438Macrophage mannose receptor 1PRO_0000017548Add
    BLAST

    Amino acid modifications

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

    1
    1456
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22897.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 13891371ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1411 – 145646CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1390 – 141021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 8 C-type lectin domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1334 – 13341A → T in X55635. (PubMed:2258707)Curated

    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. 1 Publication
    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. 1 PublicationVSP_041340Add
    BLAST
    Alternative sequencei499 – 1456958Missing in isoform 2. 1 PublicationVSP_041341Add
    BLAST

    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

    EnsembliENST00000569591; 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 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

    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: October 1, 2014
    This is version 170 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