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P25106

- ACKR3_HUMAN

UniProt

P25106 - ACKR3_HUMAN

Protein

Atypical chemokine receptor 3

Gene

ACKR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.12 Publications

    GO - Molecular functioni

    1. coreceptor activity Source: InterPro
    2. C-X-C chemokine binding Source: UniProtKB
    3. C-X-C chemokine receptor activity Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. scavenger receptor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: InterPro
    2. cell adhesion Source: UniProtKB-KW
    3. chemokine-mediated signaling pathway Source: BHF-UCL
    4. chemotaxis Source: InterPro
    5. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
    6. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    7. receptor internalization Source: UniProtKB
    8. vasculogenesis Source: InterPro
    9. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.
    SignaLinkiP25106.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atypical chemokine receptor 3
    Alternative name(s):
    C-X-C chemokine receptor type 7
    Short name:
    CXC-R7
    Short name:
    CXCR-7
    Chemokine orphan receptor 1
    G-protein coupled receptor 159
    G-protein coupled receptor RDC1 homolog
    Short name:
    RDC-1
    Gene namesi
    Name:ACKR3
    Synonyms:CMKOR1, CXCR7, GPR159, RDC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:23692. ACKR3.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cytoplasmperinuclear region. Early endosome. Recycling endosome By similarity
    Note: Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits in a beta-arrestin-dependent manner. Once internalized, the ligand dissociates from the receptor, and is targeted to degradation while the receptor is recycled back to the cell membrane.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. coated pit Source: UniProtKB
    3. early endosome Source: UniProtKB-SubCell
    4. endosome Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: UniProtKB
    8. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi145 – 1451S → A: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with V-147. 1 Publication
    Mutagenesisi147 – 1471T → V: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with A-145. 1 Publication

    Organism-specific databases

    PharmGKBiPA162383053.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Atypical chemokine receptor 3PRO_0000070101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi22 – 221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi117 ↔ 196PROSITE-ProRule annotation

    Post-translational modificationi

    The Ser/Thr residues in the C-terminal cytoplasmic tail may be phosphorylated.
    Ubiquitinated at the Lys residues in its C-terminal cytoplasmic tail and is essential for correct trafficking from and to the cell membrane. Deubiquitinated by CXCL12-stimulation in a reversible manner.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP25106.
    PaxDbiP25106.
    PeptideAtlasiP25106.
    PRIDEiP25106.

    PTM databases

    PhosphoSiteiP25106.

    Expressioni

    Tissue specificityi

    Expressed in monocytes, basophils, B-cells, umbilical vein endothelial cells (HUVEC) and B-lymphoblastoid cells. Lower expression detected in CD4+ T-lymphocytes and natural killer cells. In the brain, detected in endothelial cells and capillaries, and in mature neurons of the frontal cortex and hippocampus. Expressed in tubular formation in the kidney. Highly expressed in astroglial tumor endothelial, microglial and glioma cells. Expressed at low levels in normal CD34+ progenitor cells, but at very high levels in several myeloid malignant cell lines. Expressed in breast carcinomas but not in normal breast tissue (at protein level).6 Publications

    Inductioni

    Up-regulated during cell differentiation in glioma cells.1 Publication

    Gene expression databases

    BgeeiP25106.
    CleanExiHS_CXCR7.
    GenevestigatoriP25106.

    Organism-specific databases

    HPAiHPA049718.

    Interactioni

    Subunit structurei

    Homodimer. Can form heterodimers with CXCR4; heterodimerization may regulate CXCR4 signaling activity. Interacts with ARRB1 and ARRB2.4 Publications

    Protein-protein interaction databases

    BioGridi121321. 2 interactions.
    IntActiP25106. 5 interactions.
    STRINGi9606.ENSP00000272928.

    Structurei

    3D structure databases

    ProteinModelPortaliP25106.
    SMRiP25106. Positions 45-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4040ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini62 – 8120CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini103 – 11816ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini140 – 16223CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini184 – 21330ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini235 – 25218CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini274 – 29623ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini320 – 36243CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei41 – 6121Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei82 – 10221Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei119 – 13921Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei163 – 18321Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei214 – 23421Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei253 – 27321Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei297 – 31923Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni324 – 36239C-terminal cytoplasmic tailAdd
    BLAST

    Domaini

    The C-terminal cytoplasmic tail, plays a key role in: correct trafficking to the cell membrane, recruitment of beta-arrestin, ubiquitination, and in chemokine scavenging and signaling functions. The Ser/Thr residues and the Lys residues in the C-terminal cytoplasmic tail are essential for beta-arrestin recruitment and ubiquitination respectively.

    Sequence similaritiesi

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

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG306050.
    HOGENOMiHOG000261660.
    HOVERGENiHBG106832.
    InParanoidiP25106.
    KOiK04304.
    OMAiYIPFTCQ.
    OrthoDBiEOG73FQMT.
    PhylomeDBiP25106.
    TreeFamiTF333489.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR001416. Chemokine_CXCR7.
    IPR000355. Chemokine_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PANTHERiPTHR24227. PTHR24227. 1 hit.
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00237. GPCRRHODOPSN.
    PR00646. RDC1ORPHANR.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25106-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLHLFDYSE PGNFSDISWP CNSSDCIVVD TVMCPNMPNK SVLLYTLSFI    50
    YIFIFVIGMI ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVLTIPVW 100
    VVSLVQHNQW PMGELTCKVT HLIFSINLFG SIFFLTCMSV DRYLSITYFT 150
    NTPSSRKKMV RRVVCILVWL LAFCVSLPDT YYLKTVTSAS NNETYCRSFY 200
    PEHSIKEWLI GMELVSVVLG FAVPFSIIAV FYFLLARAIS ASSDQEKHSS 250
    RKIIFSYVVV FLVCWLPYHV AVLLDIFSIL HYIPFTCRLE HALFTALHVT 300
    QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS 350
    ETEYSALEQS TK 362
    Length:362
    Mass (Da):41,493
    Last modified:October 3, 2006 - v3
    Checksum:iA863EC1AFB5B158B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91S → A in AAA62370. (PubMed:1675791)Curated
    Sequence conflicti130 – 1301G → S in AAA62370. (PubMed:1675791)Curated
    Sequence conflicti130 – 1301G → S in AAB16913. 1 PublicationCurated
    Sequence conflicti130 – 1301G → S in AAB94130. 1 PublicationCurated
    Sequence conflicti131 – 1311S → G in AAA62370. (PubMed:1675791)Curated
    Sequence conflicti228 – 2281I → V in AAH36661. (PubMed:15489334)Curated
    Sequence conflicti360 – 3612ST → NA in AAA62370. (PubMed:1675791)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti219 – 2191L → W.
    Corresponds to variant rs10183641 [ dbSNP | Ensembl ].
    VAR_027477

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64749 mRNA. Translation: AAA62370.1.
    U73141 Genomic DNA. Translation: AAB18130.1.
    U67784 mRNA. Translation: AAB16913.1.
    AF030297 mRNA. Translation: AAB94130.1.
    DQ822477 mRNA. Translation: ABH01258.1.
    AK291659 mRNA. Translation: BAF84348.1.
    AC079611 Genomic DNA. Translation: AAX93086.1.
    CH471063 Genomic DNA. Translation: EAW71092.1.
    BC036661 mRNA. Translation: AAH36661.1.
    CCDSiCCDS2516.1.
    PIRiA39714.
    RefSeqiNP_064707.1. NM_020311.2.
    XP_005246154.1. XM_005246097.1.
    XP_005246155.1. XM_005246098.1.
    XP_006712703.1. XM_006712640.1.
    UniGeneiHs.471751.

    Genome annotation databases

    EnsembliENST00000272928; ENSP00000272928; ENSG00000144476.
    GeneIDi57007.
    KEGGihsa:57007.
    UCSCiuc002vwd.3. human.

    Polymorphism databases

    DMDMi115502380.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    CXC chemokine receptors entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64749 mRNA. Translation: AAA62370.1 .
    U73141 Genomic DNA. Translation: AAB18130.1 .
    U67784 mRNA. Translation: AAB16913.1 .
    AF030297 mRNA. Translation: AAB94130.1 .
    DQ822477 mRNA. Translation: ABH01258.1 .
    AK291659 mRNA. Translation: BAF84348.1 .
    AC079611 Genomic DNA. Translation: AAX93086.1 .
    CH471063 Genomic DNA. Translation: EAW71092.1 .
    BC036661 mRNA. Translation: AAH36661.1 .
    CCDSi CCDS2516.1.
    PIRi A39714.
    RefSeqi NP_064707.1. NM_020311.2.
    XP_005246154.1. XM_005246097.1.
    XP_005246155.1. XM_005246098.1.
    XP_006712703.1. XM_006712640.1.
    UniGenei Hs.471751.

    3D structure databases

    ProteinModelPortali P25106.
    SMRi P25106. Positions 45-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121321. 2 interactions.
    IntActi P25106. 5 interactions.
    STRINGi 9606.ENSP00000272928.

    Chemistry

    ChEMBLi CHEMBL2010631.
    GuidetoPHARMACOLOGYi 80.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P25106.

    Polymorphism databases

    DMDMi 115502380.

    Proteomic databases

    MaxQBi P25106.
    PaxDbi P25106.
    PeptideAtlasi P25106.
    PRIDEi P25106.

    Protocols and materials databases

    DNASUi 57007.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272928 ; ENSP00000272928 ; ENSG00000144476 .
    GeneIDi 57007.
    KEGGi hsa:57007.
    UCSCi uc002vwd.3. human.

    Organism-specific databases

    CTDi 57007.
    GeneCardsi GC02P237477.
    HGNCi HGNC:23692. ACKR3.
    HPAi HPA049718.
    MIMi 610376. gene.
    neXtProti NX_P25106.
    PharmGKBi PA162383053.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306050.
    HOGENOMi HOG000261660.
    HOVERGENi HBG106832.
    InParanoidi P25106.
    KOi K04304.
    OMAi YIPFTCQ.
    OrthoDBi EOG73FQMT.
    PhylomeDBi P25106.
    TreeFami TF333489.

    Enzyme and pathway databases

    Reactomei REACT_15344. Chemokine receptors bind chemokines.
    REACT_19231. G alpha (i) signalling events.
    SignaLinki P25106.

    Miscellaneous databases

    ChiTaRSi CXCR7. human.
    GeneWikii CXCR7.
    GenomeRNAii 57007.
    NextBioi 62747.
    PROi P25106.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25106.
    CleanExi HS_CXCR7.
    Genevestigatori P25106.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR001416. Chemokine_CXCR7.
    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 PR00237. GPCRRHODOPSN.
    PR00646. RDC1ORPHANR.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the human vasoactive intestinal peptide receptor."
      Sreedharan S.P., Robichon A., Peterson K.E., Goetzl E.J.
      Proc. Natl. Acad. Sci. U.S.A. 88:4986-4990(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "Coding and 3'-noncoding sequence of human RDC1, an orphan G protein-coupled receptor."
      Oates E.L., Roos B.A., Howard G.A.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Human RDC1 gene."
      Bi A., Yu L., Zhang Q., Tu Q., Xing Y., Zheng L.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Isolation of cDNA coding for Homo sapiens chemokine orphan receptor 1 (CMKOR1)."
      Martin A.L., Kaighin V.A., Aronstam R.S.
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    6. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Testis.
    9. Cited for: DOUBTS ON THE ORIGINAL FUNCTION.
    10. "The chemokine SDF-1/CXCL12 binds to and signals through the orphan receptor RDC1 in T lymphocytes."
      Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J., Moepps B., Arenzana-Seisdedos F., Thelen M., Bachelerie F.
      J. Biol. Chem. 280:35760-35766(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "A novel chemokine receptor for SDF-1 and I-TAC involved in cell survival, cell adhesion, and tumor development."
      Burns J.M., Summers B.C., Wang Y., Melikian A., Berahovich R., Miao Z., Penfold M.E., Sunshine M.J., Littman D.R., Kuo C.J., Wei K., McMaster B.E., Wright K., Howard M.C., Schall T.J.
      J. Exp. Med. 203:2201-2213(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Expression and regulation of the orphan receptor RDC1 and its putative ligand in human dendritic and B cells."
      Infantino S., Moepps B., Thelen M.
      J. Immunol. 176:2197-2207(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. "Disrupted cardiac development but normal hematopoiesis in mice deficient in the second CXCL12/SDF-1 receptor, CXCR7."
      Sierro F., Biben C., Martinez-Munoz L., Mellado M., Ransohoff R.M., Li M., Woehl B., Leung H., Groom J., Batten M., Harvey R.P., Martinez-A C., Mackay C.R., Mackay F.
      Proc. Natl. Acad. Sci. U.S.A. 104:14759-14764(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HETERODIMERIZATION.
    14. "A crosstalk between intracellular CXCR7 and CXCR4 involved in rapid CXCL12-triggered integrin activation but not in chemokine-triggered motility of human T lymphocytes and CD34+ cells."
      Hartmann T.N., Grabovsky V., Pasvolsky R., Shulman Z., Buss E.C., Spiegel A., Nagler A., Lapidot T., Thelen M., Alon R.
      J. Leukoc. Biol. 84:1130-1140(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "CXCR7 heterodimerizes with CXCR4 and regulates CXCL12-mediated G protein signaling."
      Levoye A., Balabanian K., Baleux F., Bachelerie F., Lagane B.
      Blood 113:6085-6093(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    16. "Elucidation of CXCR7-mediated signaling events and inhibition of CXCR4-mediated tumor cell transendothelial migration by CXCR7 ligands."
      Zabel B.A., Wang Y., Lewen S., Berahovich R.D., Penfold M.E., Zhang P., Powers J., Summers B.C., Miao Z., Zhao B., Jalili A., Janowska-Wieczorek A., Jaen J.C., Schall T.J.
      J. Immunol. 183:3204-3211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    17. Cited for: FUNCTION, SUBUNIT.
    18. "The chemokine receptor CXCR7 is highly expressed in human glioma cells and mediates antiapoptotic effects."
      Hattermann K., Held-Feindt J., Lucius R., Muerkoster S.S., Penfold M.E., Schall T.J., Mentlein R.
      Cancer Res. 70:3299-3308(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    19. "Chemokine decoy receptors: structure-function and biological properties."
      Bonecchi R., Savino B., Borroni E.M., Mantovani A., Locati M.
      Curr. Top. Microbiol. Immunol. 341:15-36(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    20. "CXCR7: a new SDF-1-binding receptor in contrast to normal CD34(+) progenitors is functional and is expressed at higher level in human malignant hematopoietic cells."
      Tarnowski M., Liu R., Wysoczynski M., Ratajczak J., Kucia M., Ratajczak M.Z.
      Eur. J. Haematol. 85:472-483(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    21. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-145 AND THR-147.
    22. "Beta-arrestin- but not G protein-mediated signaling by the 'decoy' receptor CXCR7."
      Rajagopal S., Kim J., Ahn S., Craig S., Lam C.M., Gerard N.P., Gerard C., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:628-632(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "CXCR7 protein expression in human adult brain and differentiated neurons."
      Shimizu S., Brown M., Sengupta R., Penfold M.E., Meucci O.
      PLoS ONE 6:E20680-E20680(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    24. "The biochemistry and biology of the atypical chemokine receptors."
      Graham G.J., Locati M., Mantovani A., Rot A., Thelen M.
      Immunol. Lett. 145:30-38(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    25. "Carboxy-terminus of CXCR7 regulates receptor localization and function."
      Ray P., Mihalko L.A., Coggins N.L., Moudgil P., Ehrlich A., Luker K.E., Luker G.D.
      Int. J. Biochem. Cell Biol. 44:669-678(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, C-TERMINAL CYTOPLASMIC TAIL, INTERACTION WITH ARRB2.
    26. Cited for: UBIQUITINATION, C-TERMINAL CYTOPLASMIC TAIL, SUBCELLULAR LOCATION, INTERACTION WITH ARRB1 AND ARRB2.
    27. Cited for: REVIEW.
    28. Cited for: REVIEW.

    Entry informationi

    Entry nameiACKR3_HUMAN
    AccessioniPrimary (citable) accession number: P25106
    Secondary accession number(s): A8K6J4
    , Q53RV4, Q8NE10, Q92938, Q92986
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 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

    Caution

    Was originally thought to be the receptor for VIP.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 2
      Human chromosome 2: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3