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O35457

- CCRL2_MOUSE

UniProt

O35457 - CCRL2_MOUSE

Protein

C-C chemokine receptor-like 2

Gene

Ccrl2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Receptor for CCL19 and chemerin/RARRES2. Does not appear to be a signaling receptor, but may have a role in modulating chemokine-triggered immune responses by capturing and internalizing CCL19 or by presenting RARRES2 ligand to CMKLR1, a functional signaling receptor. Plays a critical role for the development of Th2 responses By similarity.By similarity

    GO - Molecular functioni

    1. C-C chemokine receptor activity Source: MGI
    2. chemokine receptor binding Source: UniProtKB

    GO - Biological processi

    1. chemokine-mediated signaling pathway Source: GOC
    2. chemotaxis Source: InterPro
    3. inflammatory response Source: UniProtKB

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-C chemokine receptor-like 2
    Alternative name(s):
    Chemokine receptor CCR11
    G-protein coupled beta chemokine receptor
    Lipopolysaccharide-inducible C-C chemokine receptor
    Short name:
    L-CCR
    Gene namesi
    Name:Ccrl2
    Synonyms:Ccr11, Lccr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1920904. Ccrl2.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Deficient-mice have normal numbers of mast cells in all tissues analyzed. Wild-type and deficient mice develop marked local inflammation when sensitized with a high dose of DNP-specific IgE, however deficient mice have significantly reduced IgE-dependent passive cutaneous anaphylaxis (PCA) reactions when lower sensitizing dose is used. Deficient-mice show normal recruitment of circulating DC into the lung, but a defective trafficking of antigen-loaded lung DC to mediastinal lymph nodes. This defect was associated to a reduction in lymph node cellularity and reduced priming of T-helper cell 2 response.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 360360C-C chemokine receptor-like 2PRO_0000236800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi3 – 31N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi108 ↔ 185PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiO35457.

    PTM databases

    PhosphoSiteiO35457.

    Expressioni

    Tissue specificityi

    Expressed in macrophages, astrocytes, in glial cells. Constitutively expressed by mast cells. Detected in bronchial epithelium in OVA-induced airway inflammation. Up-regulated during dendritic cell (DC) maturation.5 Publications

    Inductioni

    By bacterial lipopolysaccharide in astrocytes.1 Publication

    Gene expression databases

    BgeeiO35457.
    CleanExiMM_CCRL2.
    GenevestigatoriO35457.

    Structurei

    3D structure databases

    ProteinModelPortaliO35457.
    SMRiO35457. Positions 47-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4242ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini64 – 7310CytoplasmicSequence Analysis
    Topological domaini95 – 10915ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini131 – 14111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini163 – 20240ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini224 – 24320CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini265 – 28521ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini308 – 36053CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei43 – 6321Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei74 – 9421Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei110 – 13021Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei142 – 16221Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei203 – 22321Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei244 – 26421Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei286 – 30722Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    Lacks the conserved DRYLAIV motif in the second intracellular loop that is required for signaling of functional chemokine receptors.By similarity

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG149863.
    GeneTreeiENSGT00700000104407.
    HOGENOMiHOG000234122.
    HOVERGENiHBG106917.
    InParanoidiO35457.
    KOiK08373.
    OMAiFLLMWAP.
    OrthoDBiEOG77HDFH.
    PhylomeDBiO35457.
    TreeFamiTF330966.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24227. PTHR24227. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00657. CCCHEMOKINER.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O35457-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNYTVAPDD EYDVLILDDY LDNSGPDQVP APEFLSPQQV LQFCCAVFAV    50
    GLLDNVLAVF ILVKYKGLKN LGNIYFLNLA LSNLCFLLPL PFWAHTAAHG 100
    ESPGNGTCKV LVGLHSSGLY SEVFSNILLL VQGYRVFSQG RLASIFTTVS 150
    CGIVACILAW AMATALSLPE SVFYEPRMER QKHKCAFGKP HFLPIEAPLW 200
    KYVLTSKMII LVLAFPLLVF IICCRQLRRR QSFRERQYDL HKPALVITGV 250
    FLLMWAPYNT VLFLSAFQEH LSLQDEKSSY HLDASVQVTQ LVATTHCCVN 300
    PLLYLLLDRK AFMRYLRSLF PRCNDIPYQS SGGYQQAPPR EGHGRPIELY 350
    SNLHQRQDII 360
    Length:360
    Mass (Da):40,745
    Last modified:May 30, 2006 - v2
    Checksum:iE0DBF990A8595E3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti37 – 371P → S in BAE26775. (PubMed:16141072)Curated
    Sequence conflicti39 – 391Q → R in CAC79612. (PubMed:12555200)Curated
    Sequence conflicti157 – 1571I → V in AAB86479. 1 PublicationCurated
    Sequence conflicti215 – 2151F → L in CAC79612. (PubMed:12555200)Curated
    Sequence conflicti292 – 2921V → A in CAC79612. (PubMed:12555200)Curated
    Sequence conflicti334 – 3341Y → S in AAB86479. 1 PublicationCurated
    Sequence conflicti341 – 3411E → K in AAB86479. 1 PublicationCurated
    Sequence conflicti359 – 3591I → K in CAJ18456. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009384 mRNA. Translation: BAA25879.1.
    AJ318863 mRNA. Translation: CAC79612.1.
    AF316576 mRNA. Translation: AAG30950.1.
    AF030185 mRNA. Translation: AAB86479.1.
    AK007808 mRNA. Translation: BAB25273.1.
    AK145946 mRNA. Translation: BAE26775.1.
    AK151856 mRNA. Translation: BAE30745.1.
    CT010248 mRNA. Translation: CAJ18456.1.
    BC038631 mRNA. Translation: AAH38631.1.
    CCDSiCCDS23582.1.
    RefSeqiNP_059494.2. NM_017466.4.
    XP_006512248.1. XM_006512185.1.
    XP_006512249.1. XM_006512186.1.
    UniGeneiMm.7336.

    Genome annotation databases

    EnsembliENSMUST00000111888; ENSMUSP00000107519; ENSMUSG00000043953.
    GeneIDi54199.
    KEGGimmu:54199.
    UCSCiuc009rvk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009384 mRNA. Translation: BAA25879.1 .
    AJ318863 mRNA. Translation: CAC79612.1 .
    AF316576 mRNA. Translation: AAG30950.1 .
    AF030185 mRNA. Translation: AAB86479.1 .
    AK007808 mRNA. Translation: BAB25273.1 .
    AK145946 mRNA. Translation: BAE26775.1 .
    AK151856 mRNA. Translation: BAE30745.1 .
    CT010248 mRNA. Translation: CAJ18456.1 .
    BC038631 mRNA. Translation: AAH38631.1 .
    CCDSi CCDS23582.1.
    RefSeqi NP_059494.2. NM_017466.4.
    XP_006512248.1. XM_006512185.1.
    XP_006512249.1. XM_006512186.1.
    UniGenei Mm.7336.

    3D structure databases

    ProteinModelPortali O35457.
    SMRi O35457. Positions 47-320.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    GuidetoPHARMACOLOGYi 78.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei O35457.

    Proteomic databases

    PRIDEi O35457.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111888 ; ENSMUSP00000107519 ; ENSMUSG00000043953 .
    GeneIDi 54199.
    KEGGi mmu:54199.
    UCSCi uc009rvk.1. mouse.

    Organism-specific databases

    CTDi 9034.
    MGIi MGI:1920904. Ccrl2.

    Phylogenomic databases

    eggNOGi NOG149863.
    GeneTreei ENSGT00700000104407.
    HOGENOMi HOG000234122.
    HOVERGENi HBG106917.
    InParanoidi O35457.
    KOi K08373.
    OMAi FLLMWAP.
    OrthoDBi EOG77HDFH.
    PhylomeDBi O35457.
    TreeFami TF330966.

    Miscellaneous databases

    NextBioi 311054.
    PROi O35457.
    SOURCEi Search...

    Gene expression databases

    Bgeei O35457.
    CleanExi MM_CCRL2.
    Genevestigatori O35457.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    PANTHERi PTHR24227. PTHR24227. 1 hit.
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00657. CCCHEMOKINER.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel lipopolysaccharide inducible C-C chemokine receptor related gene in murine macrophages."
      Shimada T., Matsumoto M., Tatsumi Y., Kanamaru A., Akira S.
      FEBS Lett. 425:490-494(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "LPS-induced expression of a novel chemokine receptor (L-CCR) in mouse glial cells in vitro and in vivo."
      Zuurman M.W., Heeroma J., Brouwer N., Boddeke H.W., Biber K.P.H.
      Glia 41:327-336(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
      Strain: CD-1.
    3. "RANTES and eotaxin stimulate chemotaxis, chemokine/cytokine synthesis, and receptor modulation in murine astroctyes."
      Luo Y., Berman M.A., Fischer F.R., Abromson-Leeman S.R., Kuziel W.A., Gerard C., Dorf M.E.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/Sv and C57BL/10.
    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].
      Strain: C57BL/6J.
      Tissue: Placenta.
    5. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    7. "Expression of L-CCR in HEK 293 cells reveals functional responses to CCL2, CCL5, CCL7, and CCL8."
      Biber K., Zuurman M.W., Homan H., Boddeke H.W.G.M.
      J. Leukoc. Biol. 74:243-251(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Induction of glial L-CCR mRNA expression in spinal cord and brain in experimental autoimmune encephalomyelitis."
      Brouwer N., Zuurman M.W., Wei T., Ransohoff R.M., Boddeke H.W., Biber K.
      Glia 46:84-94(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Localization and enhanced mRNA expression of the orphan chemokine receptor L-CCR in the lung in a murine model of ovalbumin-induced airway inflammation."
      Oostendorp J., Hylkema M.N., Luinge M., Geerlings M., Meurs H., Timens W., Zaagsma J., Postma D.S., Boddeke H.W., Biber K.
      J. Histochem. Cytochem. 52:401-410(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Mast cell-expressed orphan receptor CCRL2 binds chemerin and is required for optimal induction of IgE-mediated passive cutaneous anaphylaxis."
      Zabel B.A., Nakae S., Zuniga L., Kim J.Y., Ohyama T., Alt C., Pan J., Suto H., Soler D., Allen S.J., Handel T.M., Song C.H., Galli S.J., Butcher E.C.
      J. Exp. Med. 205:2207-2220(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING, DISRUPTION PHENOTYPE, FUNCTION, LACK OF RESPOND TO CCL2; CCL5; CCL7 AND CCL8.
    11. Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, FUNCTION.

    Entry informationi

    Entry nameiCCRL2_MOUSE
    AccessioniPrimary (citable) accession number: O35457
    Secondary accession number(s): O70171
    , Q3UKM6, Q4FK04, Q91YD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It was initially reported that CCRL2 responds functionally to CCL2, CCL5, CCL7, and CCL8 via intracellular calcium mobilization and transwell chemotaxis although no evidence for a direct ligand-receptor interaction was provided in this report (PubMed:14999816). These results are now controversial and other studies failed to confirm CCRL2 recognition and transwell chemotaxis of these chemokines or a series of other CC- and CXC-chemokines using CCRL2-transfected cells (PubMed:18794339).2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3