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P25106 (ACKR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ACKR3
Synonyms:CMKOR1, CXCR7, GPR159, RDC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21 Ref.22 Ref.25

Subunit structure

Homodimer. Can form heterodimers with CXCR4; heterodimerization may regulate CXCR4 signaling activity. Interacts with ARRB1 and ARRB2. Ref.13 Ref.15 Ref.17 Ref.25 Ref.26

Subcellular location

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. Ref.14 Ref.21 Ref.23 Ref.25 Ref.26

Tissue specificity

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). Ref.10 Ref.12 Ref.16 Ref.18 Ref.20 Ref.23

Induction

Up-regulated during cell differentiation in glioma cells. Ref.18

Domain

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.

Post-translational modification

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. Ref.26

Sequence similarities

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

Caution

Was originally (Ref.1) thought to be the receptor for VIP.

Ontologies

Keywords
   Biological processCell adhesion
Host-virus interaction
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
G-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: InterPro

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

chemokine-mediated signaling pathway

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

chemotaxis

Inferred from electronic annotation. Source: InterPro

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.25. Source: UniProtKB

receptor internalization

Inferred from mutant phenotype Ref.25Ref.26. Source: UniProtKB

vasculogenesis

Inferred from electronic annotation. Source: InterPro

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell surface

Inferred from direct assay Ref.26. Source: UniProtKB

coated pit

Inferred from direct assay Ref.26. Source: UniProtKB

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay Ref.25. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.25. Source: UniProtKB

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionC-X-C chemokine binding

Inferred from mutant phenotype Ref.25. Source: UniProtKB

C-X-C chemokine receptor activity

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

coreceptor activity

Inferred from electronic annotation. Source: InterPro

scavenger receptor activity

Inferred from mutant phenotype Ref.25. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Atypical chemokine receptor 3
PRO_0000070101

Regions

Topological domain1 – 4040Extracellular Potential
Transmembrane41 – 6121Helical; Name=1; Potential
Topological domain62 – 8120Cytoplasmic Potential
Transmembrane82 – 10221Helical; Name=2; Potential
Topological domain103 – 11816Extracellular Potential
Transmembrane119 – 13921Helical; Name=3; Potential
Topological domain140 – 16223Cytoplasmic Potential
Transmembrane163 – 18321Helical; Name=4; Potential
Topological domain184 – 21330Extracellular Potential
Transmembrane214 – 23421Helical; Name=5; Potential
Topological domain235 – 25218Cytoplasmic Potential
Transmembrane253 – 27321Helical; Name=6; Potential
Topological domain274 – 29623Extracellular Potential
Transmembrane297 – 31923Helical; Name=7; Potential
Topological domain320 – 36243Cytoplasmic Potential
Region324 – 36239C-terminal cytoplasmic tail

Amino acid modifications

Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation391N-linked (GlcNAc...) Potential
Disulfide bond117 ↔ 196 By similarity

Natural variations

Natural variant2191L → W.
Corresponds to variant rs10183641 [ dbSNP | Ensembl ].
VAR_027477

Experimental info

Mutagenesis1451S → 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. Ref.21
Mutagenesis1471T → 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. Ref.21
Sequence conflict91S → A in AAA62370. Ref.1
Sequence conflict1301G → S in AAA62370. Ref.1
Sequence conflict1301G → S in AAB16913. Ref.2
Sequence conflict1301G → S in AAB94130. Ref.3
Sequence conflict1311S → G in AAA62370. Ref.1
Sequence conflict2281I → V in AAH36661. Ref.8
Sequence conflict360 – 3612ST → NA in AAA62370. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P25106 [UniParc].

Last modified October 3, 2006. Version 3.
Checksum: A863EC1AFB5B158B

FASTA36241,493
        10         20         30         40         50         60 
MDLHLFDYSE PGNFSDISWP CNSSDCIVVD TVMCPNMPNK SVLLYTLSFI YIFIFVIGMI 

        70         80         90        100        110        120 
ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVLTIPVW VVSLVQHNQW PMGELTCKVT 

       130        140        150        160        170        180 
HLIFSINLFG SIFFLTCMSV DRYLSITYFT NTPSSRKKMV RRVVCILVWL LAFCVSLPDT 

       190        200        210        220        230        240 
YYLKTVTSAS NNETYCRSFY PEHSIKEWLI GMELVSVVLG FAVPFSIIAV FYFLLARAIS 

       250        260        270        280        290        300 
ASSDQEKHSS RKIIFSYVVV FLVCWLPYHV AVLLDIFSIL HYIPFTCRLE HALFTALHVT 

       310        320        330        340        350        360 
QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQS 


TK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"RDC1 may not be VIP receptor."
Nagata S., Ishihara T., Robberecht P., Libert F., Parmentier M., Christophe J., Vassart G.
Trends Pharmacol. Sci. 13:102-103(1992) [PubMed] [Europe PMC] [Abstract]
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]"AMD3100 is a CXCR7 ligand with allosteric agonist properties."
Kalatskaya I., Berchiche Y.A., Gravel S., Limberg B.J., Rosenbaum J.S., Heveker N.
Mol. Pharmacol. 75:1240-1247(2009) [PubMed] [Europe PMC] [Abstract]
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]"CXCR7 functions as a scavenger for CXCL12 and CXCL11."
Naumann U., Cameroni E., Pruenster M., Mahabaleshwar H., Raz E., Zerwes H.G., Rot A., Thelen M.
PLoS ONE 5:E9175-E9175(2010) [PubMed] [Europe PMC] [Abstract]
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]"Ubiquitination of CXCR7 controls receptor trafficking."
Canals M., Scholten D.J., de Munnik S., Han M.K., Smit M.J., Leurs R.
PLoS ONE 7:E34192-E34192(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, C-TERMINAL CYTOPLASMIC TAIL, SUBCELLULAR LOCATION, INTERACTION WITH ARRB1 AND ARRB2.
[27]"Atypical chemokine receptors: from silence to sound."
Cancellieri C., Vacchini A., Locati M., Bonecchi R., Borroni E.M.
Biochem. Soc. Trans. 41:231-236(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"CXCR7 impact on CXCL12 biology and disease."
Sanchez-Martin L., Sanchez-Mateos P., Cabanas C.
Trends Mol. Med. 19:12-22(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA39714.
RefSeqNP_064707.1. NM_020311.2.
XP_005246154.1. XM_005246097.1.
XP_005246155.1. XM_005246098.1.
UniGeneHs.471751.

3D structure databases

ProteinModelPortalP25106.
SMRP25106. Positions 10-358.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121321. 2 interactions.
IntActP25106. 5 interactions.
STRING9606.ENSP00000272928.

Chemistry

ChEMBLCHEMBL2010631.
GuidetoPHARMACOLOGY80.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP25106.

Polymorphism databases

DMDM115502380.

Proteomic databases

PaxDbP25106.
PeptideAtlasP25106.
PRIDEP25106.

Protocols and materials databases

DNASU57007.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272928; ENSP00000272928; ENSG00000144476.
GeneID57007.
KEGGhsa:57007.
UCSCuc002vwd.3. human.

Organism-specific databases

CTD57007.
GeneCardsGC02P237477.
HGNCHGNC:23692. ACKR3.
HPAHPA049718.
MIM610376. gene.
neXtProtNX_P25106.
PharmGKBPA162383053.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306050.
HOGENOMHOG000261660.
HOVERGENHBG106832.
InParanoidP25106.
KOK04304.
OMAYIPFTCQ.
OrthoDBEOG73FQMT.
PhylomeDBP25106.
TreeFamTF333489.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP25106.

Gene expression databases

BgeeP25106.
CleanExHS_CXCR7.
GenevestigatorP25106.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001416. Chemokine_CXCR7.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00646. RDC1ORPHANR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCXCR7. human.
GeneWikiCXCR7.
GenomeRNAi57007.
NextBio62747.
PROP25106.
SOURCESearch...

Entry information

Entry nameACKR3_HUMAN
AccessionPrimary (citable) accession number: P25106
Secondary accession number(s): A8K6J4 expand/collapse secondary AC list , Q53RV4, Q8NE10, Q92938, Q92986
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 3, 2006
Last modified: April 16, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries