ID ACKR3_HUMAN Reviewed; 362 AA.
AC P25106; A8K6J4; Q53RV4; Q8NE10; Q92938; Q92986;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 10-MAY-2017, entry version 172.
DE RecName: Full=Atypical chemokine receptor 3;
DE AltName: Full=C-X-C chemokine receptor type 7;
DE Short=CXC-R7;
DE Short=CXCR-7;
DE AltName: Full=Chemokine orphan receptor 1;
DE AltName: Full=G-protein coupled receptor 159;
DE AltName: Full=G-protein coupled receptor RDC1 homolog;
DE Short=RDC-1;
GN Name=ACKR3; Synonyms=CMKOR1, CXCR7, GPR159, RDC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1675791; DOI=10.1073/pnas.88.11.4986;
RA Sreedharan S.P., Robichon A., Peterson K.E., Goetzl E.J.;
RT "Cloning and expression of the human vasoactive intestinal peptide
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4986-4990(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oates E.L., Roos B.A., Howard G.A.;
RT "Coding and 3'-noncoding sequence of human RDC1, an orphan G protein-
RT coupled receptor.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bi A., Yu L., Zhang Q., Tu Q., Xing Y., Zheng L.;
RT "Human RDC1 gene.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Martin A.L., Kaighin V.A., Aronstam R.S.;
RT "Isolation of cDNA coding for Homo sapiens chemokine orphan receptor 1
RT (CMKOR1).";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP DOUBTS ON THE ORIGINAL FUNCTION.
RX PubMed=1315461; DOI=10.1016/0165-6147(92)90037-7;
RA Nagata S., Ishihara T., Robberecht P., Libert F., Parmentier M.,
RA Christophe J., Vassart G.;
RT "RDC1 may not be VIP receptor.";
RL Trends Pharmacol. Sci. 13:102-103(1992).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16107333; DOI=10.1074/jbc.M508234200;
RA Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J.,
RA Moepps B., Arenzana-Seisdedos F., Thelen M., Bachelerie F.;
RT "The chemokine SDF-1/CXCL12 binds to and signals through the orphan
RT receptor RDC1 in T lymphocytes.";
RL J. Biol. Chem. 280:35760-35766(2005).
RN [11]
RP FUNCTION.
RX PubMed=16940167; DOI=10.1084/jem.20052144;
RA Burns J.M., Summers B.C., Wang Y., Melikian A., Berahovich R.,
RA Miao Z., Penfold M.E., Sunshine M.J., Littman D.R., Kuo C.J., Wei K.,
RA McMaster B.E., Wright K., Howard M.C., Schall T.J.;
RT "A novel chemokine receptor for SDF-1 and I-TAC involved in cell
RT survival, cell adhesion, and tumor development.";
RL J. Exp. Med. 203:2201-2213(2006).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=16455976; DOI=10.4049/jimmunol.176.4.2197;
RA Infantino S., Moepps B., Thelen M.;
RT "Expression and regulation of the orphan receptor RDC1 and its
RT putative ligand in human dendritic and B cells.";
RL J. Immunol. 176:2197-2207(2006).
RN [13]
RP FUNCTION, AND HETERODIMERIZATION.
RX PubMed=17804806; DOI=10.1073/pnas.0702229104;
RA Sierro F., Biben C., Martinez-Munoz L., Mellado M., Ransohoff R.M.,
RA Li M., Woehl B., Leung H., Groom J., Batten M., Harvey R.P.,
RA Martinez-A C., Mackay C.R., Mackay F.;
RT "Disrupted cardiac development but normal hematopoiesis in mice
RT deficient in the second CXCL12/SDF-1 receptor, CXCR7.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14759-14764(2007).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18653785; DOI=10.1189/jlb.0208088;
RA Hartmann T.N., Grabovsky V., Pasvolsky R., Shulman Z., Buss E.C.,
RA Spiegel A., Nagler A., Lapidot T., Thelen M., Alon R.;
RT "A crosstalk between intracellular CXCR7 and CXCR4 involved in rapid
RT CXCL12-triggered integrin activation but not in chemokine-triggered
RT motility of human T lymphocytes and CD34+ cells.";
RL J. Leukoc. Biol. 84:1130-1140(2008).
RN [15]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19380869; DOI=10.1182/blood-2008-12-196618;
RA Levoye A., Balabanian K., Baleux F., Bachelerie F., Lagane B.;
RT "CXCR7 heterodimerizes with CXCR4 and regulates CXCL12-mediated G
RT protein signaling.";
RL Blood 113:6085-6093(2009).
RN [16]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19641136; DOI=10.4049/jimmunol.0900269;
RA Zabel B.A., Wang Y., Lewen S., Berahovich R.D., Penfold M.E.,
RA Zhang P., Powers J., Summers B.C., Miao Z., Zhao B., Jalili A.,
RA Janowska-Wieczorek A., Jaen J.C., Schall T.J.;
RT "Elucidation of CXCR7-mediated signaling events and inhibition of
RT CXCR4-mediated tumor cell transendothelial migration by CXCR7
RT ligands.";
RL J. Immunol. 183:3204-3211(2009).
RN [17]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19255243; DOI=10.1124/mol.108.053389;
RA Kalatskaya I., Berchiche Y.A., Gravel S., Limberg B.J.,
RA Rosenbaum J.S., Heveker N.;
RT "AMD3100 is a CXCR7 ligand with allosteric agonist properties.";
RL Mol. Pharmacol. 75:1240-1247(2009).
RN [18]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20388803; DOI=10.1158/0008-5472.CAN-09-3642;
RA Hattermann K., Held-Feindt J., Lucius R., Muerkoster S.S.,
RA Penfold M.E., Schall T.J., Mentlein R.;
RT "The chemokine receptor CXCR7 is highly expressed in human glioma
RT cells and mediates antiapoptotic effects.";
RL Cancer Res. 70:3299-3308(2010).
RN [19]
RP REVIEW.
RX PubMed=20373092; DOI=10.1007/82_2010_19;
RA Bonecchi R., Savino B., Borroni E.M., Mantovani A., Locati M.;
RT "Chemokine decoy receptors: structure-function and biological
RT properties.";
RL Curr. Top. Microbiol. Immunol. 341:15-36(2010).
RN [20]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20887389; DOI=10.1111/j.1600-0609.2010.01531.x;
RA Tarnowski M., Liu R., Wysoczynski M., Ratajczak J., Kucia M.,
RA Ratajczak M.Z.;
RT "CXCR7: a new SDF-1-binding receptor in contrast to normal CD34(+)
RT progenitors is functional and is expressed at higher level in human
RT malignant hematopoietic cells.";
RL Eur. J. Haematol. 85:472-483(2010).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-145 AND
RP THR-147.
RX PubMed=20161793; DOI=10.1371/journal.pone.0009175;
RA Naumann U., Cameroni E., Pruenster M., Mahabaleshwar H., Raz E.,
RA Zerwes H.G., Rot A., Thelen M.;
RT "CXCR7 functions as a scavenger for CXCL12 and CXCL11.";
RL PLoS ONE 5:E9175-E9175(2010).
RN [22]
RP FUNCTION.
RX PubMed=20018651; DOI=10.1073/pnas.0912852107;
RA Rajagopal S., Kim J., Ahn S., Craig S., Lam C.M., Gerard N.P.,
RA Gerard C., Lefkowitz R.J.;
RT "Beta-arrestin- but not G protein-mediated signaling by the 'decoy'
RT receptor CXCR7.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:628-632(2010).
RN [23]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21655198; DOI=10.1371/journal.pone.0020680;
RA Shimizu S., Brown M., Sengupta R., Penfold M.E., Meucci O.;
RT "CXCR7 protein expression in human adult brain and differentiated
RT neurons.";
RL PLoS ONE 6:E20680-E20680(2011).
RN [24]
RP REVIEW.
RX PubMed=22698181; DOI=10.1016/j.imlet.2012.04.004;
RA Graham G.J., Locati M., Mantovani A., Rot A., Thelen M.;
RT "The biochemistry and biology of the atypical chemokine receptors.";
RL Immunol. Lett. 145:30-38(2012).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, C-TERMINAL CYTOPLASMIC TAIL, AND
RP INTERACTION WITH ARRB2.
RX PubMed=22300987; DOI=10.1016/j.biocel.2012.01.007;
RA Ray P., Mihalko L.A., Coggins N.L., Moudgil P., Ehrlich A.,
RA Luker K.E., Luker G.D.;
RT "Carboxy-terminus of CXCR7 regulates receptor localization and
RT function.";
RL Int. J. Biochem. Cell Biol. 44:669-678(2012).
RN [26]
RP UBIQUITINATION, C-TERMINAL CYTOPLASMIC TAIL, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ARRB1 AND ARRB2.
RX PubMed=22457824; DOI=10.1371/journal.pone.0034192;
RA Canals M., Scholten D.J., de Munnik S., Han M.K., Smit M.J., Leurs R.;
RT "Ubiquitination of CXCR7 controls receptor trafficking.";
RL PLoS ONE 7:E34192-E34192(2012).
RN [27]
RP REVIEW.
RX PubMed=23356288; DOI=10.1042/BST20120246;
RA Cancellieri C., Vacchini A., Locati M., Bonecchi R., Borroni E.M.;
RT "Atypical chemokine receptors: from silence to sound.";
RL Biochem. Soc. Trans. 41:231-236(2013).
RN [28]
RP REVIEW.
RX PubMed=23153575; DOI=10.1016/j.molmed.2012.10.004;
RA Sanchez-Martin L., Sanchez-Mateos P., Cabanas C.;
RT "CXCR7 impact on CXCL12 biology and disease.";
RL Trends Mol. Med. 19:12-22(2013).
CC -!- FUNCTION: Atypical chemokine receptor that controls chemokine
CC levels and localization via high-affinity chemokine binding that
CC is uncoupled from classic ligand-driven signal transduction
CC cascades, resulting instead in chemokine sequestration,
CC degradation, or transcytosis. Also known as interceptor
CC (internalizing receptor) or chemokine-scavenging receptor or
CC chemokine decoy receptor. Acts as a receptor for chemokines CXCL11
CC and CXCL12/SDF1. Chemokine binding does not activate G-protein-
CC mediated signal transduction but instead induces beta-arrestin
CC recruitment, leading to ligand internalization and activation of
CC MAPK signaling pathway. Required for regulation of CXCR4 protein
CC levels in migrating interneurons, thereby adapting their chemokine
CC responsiveness. In glioma cells, transduces signals via MEK/ERK
CC pathway, mediating resistance to apoptosis. Promotes cell growth
CC and survival. Not involved in cell migration, adhesion or
CC proliferation of normal hematopoietic progenitors but activated by
CC CXCL11 in malignant hemapoietic cells, leading to phosphorylation
CC of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration.
CC Plays a regulatory role in CXCR4-mediated activation of cell
CC surface integrins by CXCL12. Required for heart valve development.
CC Acts as coreceptor with CXCR4 for a restricted number of HIV
CC isolates. {ECO:0000269|PubMed:16107333,
CC ECO:0000269|PubMed:16940167, ECO:0000269|PubMed:17804806,
CC ECO:0000269|PubMed:18653785, ECO:0000269|PubMed:19255243,
CC ECO:0000269|PubMed:19380869, ECO:0000269|PubMed:19641136,
CC ECO:0000269|PubMed:20018651, ECO:0000269|PubMed:20161793,
CC ECO:0000269|PubMed:20388803, ECO:0000269|PubMed:20887389,
CC ECO:0000269|PubMed:22300987}.
CC -!- SUBUNIT: Homodimer. Can form heterodimers with CXCR4;
CC heterodimerization may regulate CXCR4 signaling activity.
CC Interacts with ARRB1 and ARRB2. {ECO:0000269|PubMed:19255243,
CC ECO:0000269|PubMed:19380869, ECO:0000269|PubMed:22300987,
CC ECO:0000269|PubMed:22457824}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasm, perinuclear region. Early endosome. Recycling endosome
CC {ECO:0000250}. Note=Predominantly localizes to endocytic vesicles,
CC and upon stimulation by the ligand is internalized via clathrin-
CC coated pits in a beta-arrestin-dependent manner. Once
CC internalized, the ligand dissociates from the receptor, and is
CC targeted to degradation while the receptor is recycled back to the
CC cell membrane.
CC -!- TISSUE SPECIFICITY: Expressed in monocytes, basophils, B-cells,
CC umbilical vein endothelial cells (HUVEC) and B-lymphoblastoid
CC cells. Lower expression detected in CD4+ T-lymphocytes and natural
CC killer cells. In the brain, detected in endothelial cells and
CC capillaries, and in mature neurons of the frontal cortex and
CC hippocampus. Expressed in tubular formation in the kidney. Highly
CC expressed in astroglial tumor endothelial, microglial and glioma
CC cells. Expressed at low levels in normal CD34+ progenitor cells,
CC but at very high levels in several myeloid malignant cell lines.
CC Expressed in breast carcinomas but not in normal breast tissue (at
CC protein level). {ECO:0000269|PubMed:16107333,
CC ECO:0000269|PubMed:16455976, ECO:0000269|PubMed:19641136,
CC ECO:0000269|PubMed:20388803, ECO:0000269|PubMed:20887389,
CC ECO:0000269|PubMed:21655198}.
CC -!- INDUCTION: Up-regulated during cell differentiation in glioma
CC cells. {ECO:0000269|PubMed:20388803}.
CC -!- DOMAIN: The C-terminal cytoplasmic tail, plays a key role in:
CC correct trafficking to the cell membrane, recruitment of beta-
CC arrestin, ubiquitination, and in chemokine scavenging and
CC signaling functions. The Ser/Thr residues and the Lys residues in
CC the C-terminal cytoplasmic tail are essential for beta-arrestin
CC recruitment and ubiquitination respectively.
CC -!- PTM: The Ser/Thr residues in the C-terminal cytoplasmic tail may
CC be phosphorylated.
CC -!- PTM: Ubiquitinated at the Lys residues in its C-terminal
CC cytoplasmic tail and is essential for correct trafficking from and
CC to the cell membrane. Deubiquitinated by CXCL12-stimulation in a
CC reversible manner. {ECO:0000269|PubMed:22457824}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
CC -!- CAUTION: Was originally thought to be the receptor for VIP.
CC {ECO:0000305|PubMed:1675791}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CMKOR1ID40108ch2q37.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXC chemokine receptors entry;
CC URL="https://en.wikipedia.org/wiki/CXC_chemokine_receptors";
CC -----------------------------------------------------------------------
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DR EMBL; M64749; AAA62370.1; -; mRNA.
DR EMBL; U73141; AAB18130.1; -; Genomic_DNA.
DR EMBL; U67784; AAB16913.1; -; mRNA.
DR EMBL; AF030297; AAB94130.1; -; mRNA.
DR EMBL; DQ822477; ABH01258.1; -; mRNA.
DR EMBL; AK291659; BAF84348.1; -; mRNA.
DR EMBL; AC079611; AAX93086.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71092.1; -; Genomic_DNA.
DR EMBL; BC036661; AAH36661.1; -; mRNA.
DR CCDS; CCDS2516.1; -.
DR PIR; A39714; A39714.
DR RefSeq; NP_064707.1; NM_020311.2.
DR RefSeq; XP_005246154.1; XM_005246097.2.
DR RefSeq; XP_005246155.1; XM_005246098.3.
DR RefSeq; XP_016860005.1; XM_017004516.1.
DR UniGene; Hs.471751; -.
DR ProteinModelPortal; P25106; -.
DR BioGrid; 121321; 11.
DR IntAct; P25106; 15.
DR STRING; 9606.ENSP00000272928; -.
DR BindingDB; P25106; -.
DR ChEMBL; CHEMBL2010631; -.
DR GuidetoPHARMACOLOGY; 80; -.
DR iPTMnet; P25106; -.
DR PhosphoSitePlus; P25106; -.
DR BioMuta; CXCR7; -.
DR DMDM; 115502380; -.
DR MaxQB; P25106; -.
DR PaxDb; P25106; -.
DR PeptideAtlas; P25106; -.
DR PRIDE; P25106; -.
DR DNASU; 57007; -.
DR Ensembl; ENST00000272928; ENSP00000272928; ENSG00000144476.
DR GeneID; 57007; -.
DR KEGG; hsa:57007; -.
DR UCSC; uc002vwd.4; human.
DR CTD; 57007; -.
DR DisGeNET; 57007; -.
DR GeneCards; ACKR3; -.
DR HGNC; HGNC:23692; ACKR3.
DR HPA; HPA032003; -.
DR HPA; HPA049718; -.
DR MIM; 610376; gene.
DR neXtProt; NX_P25106; -.
DR OpenTargets; ENSG00000144476; -.
DR PharmGKB; PA162383053; -.
DR eggNOG; KOG3656; Eukaryota.
DR eggNOG; ENOG410XRW9; LUCA.
DR GeneTree; ENSGT00760000119055; -.
DR HOGENOM; HOG000261660; -.
DR HOVERGEN; HBG106832; -.
DR InParanoid; P25106; -.
DR KO; K04304; -.
DR OMA; YIPFTCQ; -.
DR OrthoDB; EOG091G091W; -.
DR PhylomeDB; P25106; -.
DR TreeFam; TF333489; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P25106; -.
DR SIGNOR; P25106; -.
DR ChiTaRS; ACKR3; human.
DR GeneWiki; CXCR7; -.
DR GenomeRNAi; 57007; -.
DR PRO; PR:P25106; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000144476; -.
DR CleanEx; HS_CXCR7; -.
DR ExpressionAtlas; P25106; baseline and differential.
DR Genevisible; P25106; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019958; F:C-X-C chemokine binding; IMP:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; IMP:BHF-UCL.
DR GO; GO:0015026; F:coreceptor activity; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:1905322; P:positive regulation of mesenchymal stem cell migration; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; IEA:InterPro.
DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR InterPro; IPR001416; ACKR3.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF750; PTHR10489:SF750; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00646; RDC1ORPHANR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Complete proteome; Cytoplasm;
KW Developmental protein; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Host-virus interaction;
KW Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1 362 Atypical chemokine receptor 3.
FT /FTId=PRO_0000070101.
FT TOPO_DOM 1 40 Extracellular. {ECO:0000255}.
FT TRANSMEM 41 61 Helical; Name=1. {ECO:0000255}.
FT TOPO_DOM 62 81 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 82 102 Helical; Name=2. {ECO:0000255}.
FT TOPO_DOM 103 118 Extracellular. {ECO:0000255}.
FT TRANSMEM 119 139 Helical; Name=3. {ECO:0000255}.
FT TOPO_DOM 140 162 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.
FT TOPO_DOM 184 213 Extracellular. {ECO:0000255}.
FT TRANSMEM 214 234 Helical; Name=5. {ECO:0000255}.
FT TOPO_DOM 235 252 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 253 273 Helical; Name=6. {ECO:0000255}.
FT TOPO_DOM 274 296 Extracellular. {ECO:0000255}.
FT TRANSMEM 297 319 Helical; Name=7. {ECO:0000255}.
FT TOPO_DOM 320 362 Cytoplasmic. {ECO:0000255}.
FT REGION 324 362 C-terminal cytoplasmic tail.
FT MOD_RES 347 347 Phosphoserine.
FT {ECO:0000250|UniProtKB:P56485}.
FT MOD_RES 350 350 Phosphoserine.
FT {ECO:0000250|UniProtKB:P56485}.
FT MOD_RES 355 355 Phosphoserine.
FT {ECO:0000250|UniProtKB:P56485}.
FT CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 22 22 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 117 196 {ECO:0000255|PROSITE-ProRule:PRU00521}.
FT VARIANT 219 219 L -> W (in dbSNP:rs10183641).
FT /FTId=VAR_027477.
FT MUTAGEN 145 145 S->A: Does not result in CXCL12-inducible
FT chemotaxis, calcium mobilization or ERK
FT activation, and has no effect on CXCR7-
FT mediated CXCL12 degradation; when
FT associated with V-147.
FT {ECO:0000269|PubMed:20161793}.
FT MUTAGEN 147 147 T->V: Does not result in CXCL12-inducible
FT chemotaxis, calcium mobilization or ERK
FT activation, and has no effect on CXCR7-
FT mediated CXCL12 degradation; when
FT associated with A-145.
FT {ECO:0000269|PubMed:20161793}.
FT CONFLICT 9 9 S -> A (in Ref. 1; AAA62370).
FT {ECO:0000305}.
FT CONFLICT 130 130 G -> S (in Ref. 1; AAA62370, 2; AAB16913
FT and 3; AAB94130). {ECO:0000305}.
FT CONFLICT 131 131 S -> G (in Ref. 1; AAA62370).
FT {ECO:0000305}.
FT CONFLICT 228 228 I -> V (in Ref. 8; AAH36661).
FT {ECO:0000305}.
FT CONFLICT 360 361 ST -> NA (in Ref. 1; AAA62370).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 130 146 ipat:G_PROTEIN_RECEP_F1_1 [T]
FT MYHIT 62 315 ipfam:7tm_1 [T]
FT MYHIT 61 315 iprf:G_PROTEIN_RECEP_F1_2 [T]
SQ SEQUENCE 362 AA; 41493 MW; A863EC1AFB5B158B CRC64;
MDLHLFDYSE PGNFSDISWP CNSSDCIVVD TVMCPNMPNK SVLLYTLSFI YIFIFVIGMI
ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVLTIPVW VVSLVQHNQW PMGELTCKVT
HLIFSINLFG SIFFLTCMSV DRYLSITYFT NTPSSRKKMV RRVVCILVWL LAFCVSLPDT
YYLKTVTSAS NNETYCRSFY PEHSIKEWLI GMELVSVVLG FAVPFSIIAV FYFLLARAIS
ASSDQEKHSS RKIIFSYVVV FLVCWLPYHV AVLLDIFSIL HYIPFTCRLE HALFTALHVT
QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQS
TK
//
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