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Q60754

- MARCO_MOUSE

UniProt

Q60754 - MARCO_MOUSE

Protein

Macrophage receptor MARCO

Gene

Marco

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Pattern recognition receptor (PRR). Binds Gram-positive and Gram-negative bacteria.

    GO - Molecular functioni

    1. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. apoptotic cell clearance Source: MGI
    2. endocytosis Source: MGI
    3. innate immune response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage receptor MARCO
    Alternative name(s):
    Macrophage receptor with collagenous structure
    Gene namesi
    Name:Marco
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1309998. Marco.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518Macrophage receptor MARCOPRO_0000181632Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi446 ↔ 507PROSITE-ProRule annotation
    Disulfide bondi459 ↔ 517PROSITE-ProRule annotation
    Disulfide bondi487 ↔ 497PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ60754.
    PRIDEiQ60754.

    PTM databases

    PhosphoSiteiQ60754.

    Expressioni

    Tissue specificityi

    Expressed in subpopulations of macrophages in the spleen and the medullary cord of lymph nodes.

    Gene expression databases

    ArrayExpressiQ60754.
    BgeeiQ60754.
    CleanExiMM_MARCO.
    GenevestigatoriQ60754.

    Interactioni

    Subunit structurei

    Homotrimer. Trimers may assemble in larger oligomers thus resulting in the creation of a large surface capable of interacting with very large ligands.1 Publication

    Protein-protein interaction databases

    MINTiMINT-4997199.
    STRINGi10090.ENSMUSP00000027639.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi422 – 43817
    Beta strandi441 – 4466
    Helixi452 – 46110
    Beta strandi465 – 4706
    Beta strandi480 – 4823
    Helixi494 – 4963
    Helixi509 – 5113
    Beta strandi514 – 5185

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OY3X-ray1.78A421-518[»]
    2OYAX-ray1.77A/B421-518[»]
    ProteinModelPortaliQ60754.
    SMRiQ60754. Positions 421-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60754.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4848CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini70 – 518449ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 418270Collagen-likeAdd
    BLAST
    Domaini423 – 51896SRCRPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 collagen-like domain.Curated
    Contains 1 SRCR domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG297041.
    GeneTreeiENSGT00640000091447.
    HOGENOMiHOG000085659.
    HOVERGENiHBG004933.
    InParanoidiQ60754.
    KOiK13884.
    OMAiSHNCNHN.
    OrthoDBiEOG7HHWSF.
    PhylomeDBiQ60754.
    TreeFamiTF330855.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    InterProiIPR008160. Collagen.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01391. Collagen. 2 hits.
    PF00530. SRCR. 1 hit.
    [Graphical view]
    PRINTSiPR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 1 hit.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 1 hit.
    PROSITEiPS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSKELLKEE DFLGSTEDRA DFDQAMFPVM ETFEINDPVP KKRNGGTFCM    50
    AVMAIHLILL TAGTALLLIQ VLNLQEQLQM LEMCCGNGSL AIEDKPFFSL 100
    QWAPKTHLVP RAQGLQALQA QLSWVHTSQE QLRQQFNNLT QNPELFQIKG 150
    ERGSPGPKGA PGAPGIPGLP GPAAEKGEKG AAGRDGTPGV QGPQGPPGSK 200
    GEAGLQGLTG APGKQGATGA PGPRGEKGSK GDIGLTGPKG EHGTKGDKGD 250
    LGLPGNKGDM GMKGDTGPMG SPGAQGGKGD AGKPGLPGLA GSPGVKGDQG 300
    KPGVQGVPGP QGAPGLSGAK GEPGRTGLPG PAGPPGIAGN PGIAGVKGSK 350
    GDTGIQGQKG TKGESGVPGL VGRKGDTGSP GLAGPKGEPG RVGQKGDPGM 400
    KGSSGQQGQK GEKGQKGESF QRVRIMGGTN RGRAEVYYNN EWGTICDDDW 450
    DNNDATVFCR MLGYSRGRAL SSYGGGSGNI WLDNVNCRGT ENSLWDCSKN 500
    SWGNHNCVHN EDAGVECS 518
    Length:518
    Mass (Da):52,730
    Last modified:November 1, 1996 - v1
    Checksum:iB09E7601ECA23637
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18424 mRNA. Translation: AAA68638.1.
    AF128423
    , AF127927, AF127928, AF128169, AF128170, AF128171, AF127601, AF127602, AF128419, AF128420, AF128421, AF128422 Genomic DNA. Translation: AAD51136.1.
    CCDSiCCDS15234.1.
    PIRiA55840.
    RefSeqiNP_034896.1. NM_010766.2.
    UniGeneiMm.1856.

    Genome annotation databases

    EnsembliENSMUST00000027639; ENSMUSP00000027639; ENSMUSG00000026390.
    GeneIDi17167.
    KEGGimmu:17167.
    UCSCiuc007cjl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18424 mRNA. Translation: AAA68638.1 .
    AF128423
    , AF127927 , AF127928 , AF128169 , AF128170 , AF128171 , AF127601 , AF127602 , AF128419 , AF128420 , AF128421 , AF128422 Genomic DNA. Translation: AAD51136.1 .
    CCDSi CCDS15234.1.
    PIRi A55840.
    RefSeqi NP_034896.1. NM_010766.2.
    UniGenei Mm.1856.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OY3 X-ray 1.78 A 421-518 [» ]
    2OYA X-ray 1.77 A/B 421-518 [» ]
    ProteinModelPortali Q60754.
    SMRi Q60754. Positions 421-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-4997199.
    STRINGi 10090.ENSMUSP00000027639.

    PTM databases

    PhosphoSitei Q60754.

    Proteomic databases

    PaxDbi Q60754.
    PRIDEi Q60754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027639 ; ENSMUSP00000027639 ; ENSMUSG00000026390 .
    GeneIDi 17167.
    KEGGi mmu:17167.
    UCSCi uc007cjl.1. mouse.

    Organism-specific databases

    CTDi 8685.
    MGIi MGI:1309998. Marco.

    Phylogenomic databases

    eggNOGi NOG297041.
    GeneTreei ENSGT00640000091447.
    HOGENOMi HOG000085659.
    HOVERGENi HBG004933.
    InParanoidi Q60754.
    KOi K13884.
    OMAi SHNCNHN.
    OrthoDBi EOG7HHWSF.
    PhylomeDBi Q60754.
    TreeFami TF330855.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.

    Miscellaneous databases

    EvolutionaryTracei Q60754.
    NextBioi 291450.
    PROi Q60754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60754.
    Bgeei Q60754.
    CleanExi MM_MARCO.
    Genevestigatori Q60754.

    Family and domain databases

    Gene3Di 3.10.250.10. 1 hit.
    InterProi IPR008160. Collagen.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01391. Collagen. 2 hits.
    PF00530. SRCR. 1 hit.
    [Graphical view ]
    PRINTSi PR00258. SPERACTRCPTR.
    SMARTi SM00202. SR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 1 hit.
    PROSITEi PS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a novel bacteria-binding receptor structurally related to scavenger receptors and expressed in a subset of macrophages."
      Elomaa O., Kangas M., Sahlberg C., Tuukkanen J., Sormunen R., Liakka A., Thesleff I., Kraal G., Tryggvason K.
      Cell 80:603-609(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structure and chromosomal localization of the human and murine genes for the macrophage MARCO receptor."
      Kangas M., Brannstrom A., Elomaa O., Matsuda Y., Eddy R., Shows T.B., Tryggvason K.
      Genomics 58:82-89(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Crystal structure of the cysteine-rich domain of scavenger receptor MARCO reveals the presence of a basic and an acidic cluster that both contribute to ligand recognition."
      Ojala J.R., Pikkarainen T., Tuuttila A., Sandalova T., Tryggvason K.
      J. Biol. Chem. 282:16654-16666(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 421-518, SUBUNIT, DISULFIDE BONDS.

    Entry informationi

    Entry nameiMARCO_MOUSE
    AccessioniPrimary (citable) accession number: Q60754
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3