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Protein

Atypical chemokine receptor 3

Gene

ACKR3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • coreceptor activity Source: InterPro
  • C-X-C chemokine binding Source: UniProtKB
  • C-X-C chemokine receptor activity Source: BHF-UCL
  • scavenger receptor activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: InterPro
  • cell adhesion Source: UniProtKB-KW
  • chemokine-mediated signaling pathway Source: BHF-UCL
  • chemotaxis Source: InterPro
  • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: BHF-UCL
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • vasculogenesis Source: InterPro
  • viral process Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:23692. ACKR3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4040ExtracellularSequence AnalysisAdd
BLAST
Transmembranei41 – 6121Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini62 – 8120CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei82 – 10221Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini103 – 11816ExtracellularSequence AnalysisAdd
BLAST
Transmembranei119 – 13921Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini140 – 16223CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei163 – 18321Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini184 – 21330ExtracellularSequence AnalysisAdd
BLAST
Transmembranei214 – 23421Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini235 – 25218CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei253 – 27321Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini274 – 29623ExtracellularSequence AnalysisAdd
BLAST
Transmembranei297 – 31923Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini320 – 36243CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • coated pit Source: UniProtKB
  • early endosome Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • recycling endosome Source: UniProtKB-SubCell
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiCXCR7.
DMDMi115502380.

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.
GenevisibleiP25106. HS.

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. 6 interactions.
IntActiP25106. 6 interactions.
STRINGi9606.ENSP00000272928.

Structurei

3D structure databases

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

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.
GeneTreeiENSGT00760000119055.
HOGENOMiHOG000261660.
HOVERGENiHBG106832.
InParanoidiP25106.
KOiK04304.
OMAiYIPFTCQ.
OrthoDBiEOG73FQMT.
PhylomeDBiP25106.
TreeFamiTF333489.

Family and domain databases

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

        10         20         30         40         50
MDLHLFDYSE PGNFSDISWP CNSSDCIVVD TVMCPNMPNK SVLLYTLSFI
60 70 80 90 100
YIFIFVIGMI ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVLTIPVW
110 120 130 140 150
VVSLVQHNQW PMGELTCKVT HLIFSINLFG SIFFLTCMSV DRYLSITYFT
160 170 180 190 200
NTPSSRKKMV RRVVCILVWL LAFCVSLPDT YYLKTVTSAS NNETYCRSFY
210 220 230 240 250
PEHSIKEWLI GMELVSVVLG FAVPFSIIAV FYFLLARAIS ASSDQEKHSS
260 270 280 290 300
RKIIFSYVVV FLVCWLPYHV AVLLDIFSIL HYIPFTCRLE HALFTALHVT
310 320 330 340 350
QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS
360
ETEYSALEQS TK
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 (Ref. 2) Curated
Sequence conflicti130 – 1301G → S in AAB94130 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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_005246098.2.
UniGeneiHs.471751.

Genome annotation databases

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

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:
EMBLi
GenBanki
DDBJi
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_005246098.2.
UniGeneiHs.471751.

3D structure databases

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

Protein-protein interaction databases

BioGridi121321. 6 interactions.
IntActiP25106. 6 interactions.
STRINGi9606.ENSP00000272928.

Chemistry

BindingDBiP25106.
ChEMBLiCHEMBL2010631.
GuidetoPHARMACOLOGYi80.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP25106.

Polymorphism and mutation databases

BioMutaiCXCR7.
DMDMi115502380.

Proteomic databases

MaxQBiP25106.
PaxDbiP25106.
PeptideAtlasiP25106.
PRIDEiP25106.

Protocols and materials databases

DNASUi57007.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi57007.
GeneCardsiGC02P237477.
HGNCiHGNC:23692. ACKR3.
HPAiHPA049718.
MIMi610376. gene.
neXtProtiNX_P25106.
PharmGKBiPA162383053.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG306050.
GeneTreeiENSGT00760000119055.
HOGENOMiHOG000261660.
HOVERGENiHBG106832.
InParanoidiP25106.
KOiK04304.
OMAiYIPFTCQ.
OrthoDBiEOG73FQMT.
PhylomeDBiP25106.
TreeFamiTF333489.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiACKR3. human.
GeneWikiiCXCR7.
GenomeRNAii57007.
NextBioi62747.
PROiP25106.
SOURCEiSearch...

Gene expression databases

BgeeiP25106.
CleanExiHS_CXCR7.
GenevisibleiP25106. HS.

Family and domain databases

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.