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P30204

- MSRE_MOUSE

UniProt

P30204 - MSRE_MOUSE

Protein

Macrophage scavenger receptor types I and II

Gene

Msr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL).

    GO - Molecular functioni

    1. low-density lipoprotein particle binding Source: BHF-UCL
    2. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. cholesterol transport Source: BHF-UCL
    2. lipoprotein transport Source: MGI
    3. plasma lipoprotein particle clearance Source: BHF-UCL
    4. positive regulation of cholesterol storage Source: BHF-UCL
    5. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Enzyme and pathway databases

    ReactomeiREACT_196581. Scavenging by Class A Receptors.
    REACT_209041. Scavenging by Class A Receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Macrophage scavenger receptor types I and II
    Alternative name(s):
    Macrophage acetylated LDL receptor I and II
    Scavenger receptor type A
    Short name:
    SR-A
    CD_antigen: CD204
    Gene namesi
    Name:Msr1
    Synonyms:Scvr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:98257. Msr1.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. cytoplasmic vesicle Source: Ensembl
    3. cytosol Source: Ensembl
    4. integral component of membrane Source: UniProtKB-KW
    5. low-density lipoprotein particle Source: UniProtKB-KW
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    LDL, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 458458Macrophage scavenger receptor types I and IIPRO_0000181628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphoserine1 Publication
    Modified residuei36 – 361Phosphoserine1 Publication
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi271 – 2711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi382 ↔ 446PROSITE-ProRule annotation
    Disulfide bondi395 ↔ 456PROSITE-ProRule annotation
    Disulfide bondi426 ↔ 436PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP30204.
    PaxDbiP30204.
    PRIDEiP30204.

    PTM databases

    PhosphoSiteiP30204.

    Expressioni

    Gene expression databases

    ArrayExpressiP30204.
    BgeeiP30204.
    CleanExiMM_MSR1.
    GenevestigatoriP30204.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    IntActiP30204. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP30204.
    SMRiP30204. Positions 357-458.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5555CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini79 – 458380ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei56 – 7823Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini277 – 35074Collagen-likeAdd
    BLAST
    Domaini357 – 457101SRCRPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 11436SpacerCuratedAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili209 – 25951Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil, Collagen, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG150350.
    GeneTreeiENSGT00640000091447.
    HOGENOMiHOG000085659.
    HOVERGENiHBG002473.
    InParanoidiP30204.
    KOiK06558.
    OMAiKWEMKNC.
    OrthoDBiEOG7V1FQV.
    TreeFamiTF330855.

    Family and domain databases

    Gene3Di3.10.250.10. 1 hit.
    InterProiIPR008160. Collagen.
    IPR003543. Macro_scav_rcpt.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01391. Collagen. 2 hits.
    PF03523. Macscav_rec. 1 hit.
    PF00530. SRCR. 1 hit.
    [Graphical view]
    PRINTSiPR01408. MACSCAVRCPTR.
    PR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 1 hit.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 1 hit.
    PROSITEiPS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform I (identifier: P30204-1) [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

    MTKEMTENQR LCPHEQEDAD CSSESVKFDA RSMTASLPHS TKNGPSLQEK    50
    LKSFKAALIA LYLLVFAVLI PVVGIVTAQL LNWEMKNCLV CSLNTSDTSQ 100
    GPMEKENTSK VEMRFTIIME HMKDMEERIE SISNSKADLI DTERFQNFSM 150
    ATDQRLNDIL LQLNSLISSV QEHGNSLDAI SKSLQSLNMT LLDVQLHTET 200
    LNVRVRESTA KQQEDISKLE ERVYKVSAEV QSVKEEQAHV EQEVKQEVRV 250
    LNNITNDLRL KDWEHSQTLK NITFIQGPPG PQGEKGDRGL TGQTGPPGAP 300
    GIRGIPGVKG DRGQIGFPGG RGNPGAPGKP GRSGSPGPKG QKGEKGSVGG 350
    STPLKTVRLV GGSGAHEGRV EIFHQGQWGT ICDDRWDIRA GQVVCRSLGY 400
    QEVLAVHKRA HFGQGTGPIW LNEVMCFGRE SSIENCKINQ WGVLSCSHSE 450
    DAGVTCTS 458
    Length:458
    Mass (Da):50,170
    Last modified:July 27, 2011 - v3
    Checksum:iDA069B90A6B59EB5
    GO
    Isoform II (identifier: P30204-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         352-354: TPL → RSV
         355-458: Missing.

    Show »
    Length:354
    Mass (Da):38,773
    Checksum:i348E084D2D8B644B
    GO

    Sequence cautioni

    The sequence AAA39747.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAA39748.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161Q → R in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti16 – 161Q → R in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti16 – 161Q → R in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti16 – 161Q → R in AAF14001. 1 PublicationCurated
    Sequence conflicti16 – 161Q → R in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti16 – 161Q → R in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti47 – 471L → V in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti47 – 471L → V in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti47 – 471L → V in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti47 – 471L → V in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti47 – 471L → V in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti93 – 931L → R in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti93 – 931L → R in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti93 – 931L → R in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti93 – 931L → R in AAF14001. 1 PublicationCurated
    Sequence conflicti93 – 931L → R in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti93 – 931L → R in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti110 – 1101K → N in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti110 – 1101K → N in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti110 – 1101K → N in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti110 – 1101K → N in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti110 – 1101K → N in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti120 – 1201E → A in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti120 – 1201E → A in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti120 – 1201E → A in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti120 – 1201E → A in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti120 – 1201E → A in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti130 – 1301E → Q in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti130 – 1301E → Q in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti130 – 1301E → Q in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti130 – 1301E → Q in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti130 – 1301E → Q in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti143 – 1431E → G in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti143 – 1431E → G in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti143 – 1431E → G in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti143 – 1431E → G in AAF14001. 1 PublicationCurated
    Sequence conflicti143 – 1431E → G in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti143 – 1431E → G in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti168 – 1681S → L in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti168 – 1681S → L in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti168 – 1681S → L in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti168 – 1681S → L in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti168 – 1681S → L in AAH03814. (PubMed:15489334)Curated
    Sequence conflicti202 – 2021N → H in AAA39747. (PubMed:8394868)Curated
    Sequence conflicti202 – 2021N → H in AAA39748. (PubMed:8394868)Curated
    Sequence conflicti202 – 2021N → H in BAA02650. (PubMed:8380589)Curated
    Sequence conflicti202 – 2021N → H in BAC40779. (PubMed:16141072)Curated
    Sequence conflicti202 – 2021N → H in AAH03814. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei352 – 3543TPL → RSV in isoform II. 4 PublicationsVSP_006231
    Alternative sequencei355 – 458104Missing in isoform II. 4 PublicationsVSP_006232Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04274 mRNA. Translation: AAA39747.1. Different initiation.
    L04275 mRNA. Translation: AAA39748.1. Different initiation.
    D13382 mRNA. Translation: BAA02650.1.
    AF203781 mRNA. Translation: AAF14001.1.
    M59445 mRNA. Translation: AAA37464.1.
    M59446 mRNA. Translation: AAA37465.1.
    U13873 Genomic DNA. Translation: AAC13774.1.
    AK089178 mRNA. Translation: BAC40779.1.
    AC111028 Genomic DNA. No translation available.
    BC003814 mRNA. Translation: AAH03814.1.
    CCDSiCCDS52542.1. [P30204-1]
    CCDS52543.1. [P30204-2]
    PIRiB44407.
    I73338.
    RefSeqiNP_001106797.1. NM_001113326.1. [P30204-1]
    UniGeneiMm.239291.

    Genome annotation databases

    EnsembliENSMUST00000026021; ENSMUSP00000026021; ENSMUSG00000025044. [P30204-1]
    ENSMUST00000170091; ENSMUSP00000132535; ENSMUSG00000025044. [P30204-2]
    GeneIDi20288.
    KEGGimmu:20288.
    UCSCiuc012gcm.1. mouse. [P30204-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04274 mRNA. Translation: AAA39747.1 . Different initiation.
    L04275 mRNA. Translation: AAA39748.1 . Different initiation.
    D13382 mRNA. Translation: BAA02650.1 .
    AF203781 mRNA. Translation: AAF14001.1 .
    M59445 mRNA. Translation: AAA37464.1 .
    M59446 mRNA. Translation: AAA37465.1 .
    U13873 Genomic DNA. Translation: AAC13774.1 .
    AK089178 mRNA. Translation: BAC40779.1 .
    AC111028 Genomic DNA. No translation available.
    BC003814 mRNA. Translation: AAH03814.1 .
    CCDSi CCDS52542.1. [P30204-1 ]
    CCDS52543.1. [P30204-2 ]
    PIRi B44407.
    I73338.
    RefSeqi NP_001106797.1. NM_001113326.1. [P30204-1 ]
    UniGenei Mm.239291.

    3D structure databases

    ProteinModelPortali P30204.
    SMRi P30204. Positions 357-458.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P30204. 1 interaction.

    Chemistry

    BindingDBi P30204.
    ChEMBLi CHEMBL4399.

    PTM databases

    PhosphoSitei P30204.

    Proteomic databases

    MaxQBi P30204.
    PaxDbi P30204.
    PRIDEi P30204.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026021 ; ENSMUSP00000026021 ; ENSMUSG00000025044 . [P30204-1 ]
    ENSMUST00000170091 ; ENSMUSP00000132535 ; ENSMUSG00000025044 . [P30204-2 ]
    GeneIDi 20288.
    KEGGi mmu:20288.
    UCSCi uc012gcm.1. mouse. [P30204-1 ]

    Organism-specific databases

    CTDi 4481.
    MGIi MGI:98257. Msr1.

    Phylogenomic databases

    eggNOGi NOG150350.
    GeneTreei ENSGT00640000091447.
    HOGENOMi HOG000085659.
    HOVERGENi HBG002473.
    InParanoidi P30204.
    KOi K06558.
    OMAi KWEMKNC.
    OrthoDBi EOG7V1FQV.
    TreeFami TF330855.

    Enzyme and pathway databases

    Reactomei REACT_196581. Scavenging by Class A Receptors.
    REACT_209041. Scavenging by Class A Receptors.

    Miscellaneous databases

    ChiTaRSi MSR1. mouse.
    NextBioi 297995.
    PROi P30204.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30204.
    Bgeei P30204.
    CleanExi MM_MSR1.
    Genevestigatori P30204.

    Family and domain databases

    Gene3Di 3.10.250.10. 1 hit.
    InterProi IPR008160. Collagen.
    IPR003543. Macro_scav_rcpt.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01391. Collagen. 2 hits.
    PF03523. Macscav_rec. 1 hit.
    PF00530. SRCR. 1 hit.
    [Graphical view ]
    PRINTSi PR01408. MACSCAVRCPTR.
    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. "Structures and high and low affinity ligand binding properties of murine type I and type II macrophage scavenger receptors."
      Ashkenas J., Penman M., Vasile E., Acton S., Freeman M.W., Krieger M.
      J. Lipid Res. 34:983-1000(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I AND II).
    2. "Charged collagen structure mediates the recognition of negatively charged macromolecules by macrophage scavenger receptors."
      Doi T., Wada Y., Kodama T., Higashi K.I., Kurihara Y., Miyazaki T., Nakamura H., Uesugi S., Imanishi T., Kawabe Y., Itakura H., Yazaki Y., Matsumoto A.
      J. Biol. Chem. 268:2126-2133(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
    3. "Identification of a functional domain in class A scavenger receptors that mediates metabolism of AcLDL."
      Rateri D.L., Whitman S.C., Block A.E., Daugherty A.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM I).
      Strain: C57BL/6.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
      Strain: NOD.
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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 II).
    7. "An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors."
      Freeman M., Ashkenas J., Rees D.J., Kingsley D.M., Copeland N.G., Jenkins N.A., Krieger M.
      Proc. Natl. Acad. Sci. U.S.A. 87:8810-8814(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 349-458.
    8. "Structure of the murine macrophage scavenger receptor gene and evaluation of sequences that regulate expression in the macrophage cell line, P388D."
      Aftring R.P., Freeman M.W.
      J. Lipid Res. 36:1305-1314(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
    9. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMSRE_MOUSE
    AccessioniPrimary (citable) accession number: P30204
    Secondary accession number(s): E9QNQ5, Q923G0, Q9QZ56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3