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Atypical chemokine receptor 2 (C-C chemokine receptor D6) (Chemokine receptor CCR-10) (Chemokine receptor CCR-9) (Chemokine-binding protein 2) (Chemokine-binding protein D6)

 ACKR2_HUMAN             Reviewed;         384 AA.
O00590; B2R8Y8; O00537; Q53YA1; Q86UN9; Q96A02;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
02-MAY-2002, sequence version 2.
18-JUL-2018, entry version 161.
RecName: Full=Atypical chemokine receptor 2;
AltName: Full=C-C chemokine receptor D6;
AltName: Full=Chemokine receptor CCR-10;
AltName: Full=Chemokine receptor CCR-9;
AltName: Full=Chemokine-binding protein 2;
AltName: Full=Chemokine-binding protein D6;
Name=ACKR2; Synonyms=CCBP2, CCR10, CMKBR9, D6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=9364936; DOI=10.1089/dna.1997.16.1249;
Bonini J.A., Martin S.K., Dralyuk F., Roe M.W., Philipson L.H.,
Steiner D.F.;
"Cloning, expression, and chromosomal mapping of a novel human CC-
chemokine receptor (CCR10) that displays high-affinity binding for
MCP-1 and MCP-3.";
DNA Cell Biol. 16:1249-1256(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9405404; DOI=10.1074/jbc.272.51.32078;
Nibbs R.J.B., Wylie S.M., Yang J., Landau N.R., Graham G.J.;
"Cloning and characterization of a novel promiscuous human beta-
chemokine receptor D6.";
J. Biol. Chem. 272:32078-32083(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-373.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=11238036; DOI=10.1016/S0002-9440(10)64035-7;
Nibbs R.J.B., Kriehuber E., Ponath P.D., Parent D., Qin S.,
Campbell J.D., Henderson A., Kerjaschki D., Maurer D., Graham G.J.,
Rot A.;
"The beta-chemokine receptor D6 is expressed by lymphatic endothelium
and a subset of vascular tumors.";
Am. J. Pathol. 158:867-877(2001).
[8]
C-TERMINAL CYTOPLASMIC TAIL, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION.
PubMed=18201974; DOI=10.1074/jbc.M710128200;
McCulloch C.V., Morrow V., Milasta S., Comerford I., Milligan G.,
Graham G.J., Isaacs N.W., Nibbs R.J.;
"Multiple roles for the C-terminal tail of the chemokine scavenger
D6.";
J. Biol. Chem. 283:7972-7982(2008).
[9]
ERRATUM.
McCulloch C.V., Morrow V., Milasta S., Comerford I., Milligan G.,
Graham G.J., Isaacs N.W., Nibbs R.J.;
J. Biol. Chem. 288:26820-26820(2013).
[10]
REVIEW.
PubMed=20373092; DOI=10.1007/82_2010_19;
Bonecchi R., Savino B., Borroni E.M., Mantovani A., Locati M.;
"Chemokine decoy receptors: structure-function and biological
properties.";
Curr. Top. Microbiol. Immunol. 341:15-36(2010).
[11]
TISSUE SPECIFICITY.
PubMed=22651933; DOI=10.1096/fj.11-194894;
Pashover-Schallinger E., Aswad M., Schif-Zuck S., Shapiro H.,
Singer P., Ariel A.;
"The atypical chemokine receptor D6 controls macrophage efferocytosis
and cytokine secretion during the resolution of inflammation.";
FASEB J. 26:3891-3900(2012).
[12]
REVIEW.
PubMed=22698181; DOI=10.1016/j.imlet.2012.04.004;
Graham G.J., Locati M., Mantovani A., Rot A., Thelen M.;
"The biochemistry and biology of the atypical chemokine receptors.";
Immunol. Lett. 145:30-38(2012).
[13]
REVIEW.
PubMed=23356288; DOI=10.1042/BST20120246;
Cancellieri C., Vacchini A., Locati M., Bonecchi R., Borroni E.M.;
"Atypical chemokine receptors: from silence to sound.";
Biochem. Soc. Trans. 41:231-236(2013).
[14]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=23479571; DOI=10.1182/blood-2012-04-425314;
McKimmie C.S., Singh M.D., Hewit K., Lopez-Franco O., Le Brocq M.,
Rose-John S., Lee K.M., Baker A.H., Wheat R., Blackbourn D.J.,
Nibbs R.J., Graham G.J.;
"An analysis of the function and expression of D6 on lymphatic
endothelial cells.";
Blood 121:3768-3777(2013).
[15]
REVIEW.
PubMed=23125030; DOI=10.1002/path.4123;
Graham G.J., Locati M.;
"Regulation of the immune and inflammatory responses by the 'atypical'
chemokine receptor D6.";
J. Pathol. 229:168-175(2013).
[16]
REVIEW.
PubMed=22939232; DOI=10.1016/j.molimm.2012.08.003;
Cancellieri C., Caronni N., Vacchini A., Savino B., Borroni E.M.,
Locati M., Bonecchi R.;
"Review: Structure-function and biological properties of the atypical
chemokine receptor D6.";
Mol. Immunol. 55:87-93(2013).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23633677; DOI=10.1126/scisignal.2003627;
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B.,
Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A.,
Bonecchi R., Locati M.;
"Beta-arrestin-dependent activation of the cofilin pathway is required
for the scavenging activity of the atypical chemokine receptor D6.";
Sci. Signal. 6:RA30-RA30(2013).
-!- 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
including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11,
CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha,
SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation,
activates a beta-arrestin 1 (ARRB1)-dependent, G protein-
independent signaling pathway that results in the phosphorylation
of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-
LIMK1 signaling pathway. Activation of this pathway results in up-
regulation of ACKR2 from endosomal compartment to cell membrane,
increasing its efficiency in chemokine uptake and degradation. By
scavenging chemokines in tissues, on the surfaces of lymphatic
vessels, and in placenta, plays an essential role in the
resolution (termination) of the inflammatory response and in the
regulation of adaptive immune responses. Plays a major role in the
immune silencing of macrophages during the resolution of
inflammation. Acts as a regulator of inflammatory leukocyte
interactions with lymphatic endothelial cells (LECs) and is
required for immature/mature dendritic cells discrimination by
LECs. {ECO:0000269|PubMed:23479571, ECO:0000269|PubMed:23633677}.
-!- SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cell
membrane; Multi-pass membrane protein. Note=Predominantly
localizes to endocytic vesicles, and upon stimulation by the
ligand is internalized via clathrin-coated pits. Once
internalized, the ligand dissociates from the receptor, and is
targeted to degradation while the receptor is recycled back to the
cell membrane.
-!- TISSUE SPECIFICITY: Found in endothelial cells lining afferent
lymphatics in dermis and lymph nodes. Also found in lymph nodes
subcapsular and medullary sinuses, tonsillar lymphatic sinuses and
lymphatics in mucosa and submucosa of small and large intestine
and appendix. Also found in some malignant vascular tumors.
Expressed at high levels in Kaposi sarcoma-related pathologies.
Expressed on apoptotic neutrophils (at protein level). Expressed
primarily in placenta and fetal liver, and found at very low
levels in the lung and lymph node. {ECO:0000269|PubMed:11238036,
ECO:0000269|PubMed:22651933, ECO:0000269|PubMed:23479571}.
-!- INDUCTION: By interleukin-6 and interferon-gamma.
{ECO:0000269|PubMed:23479571}.
-!- DOMAIN: The C-terminal cytoplasmic tail controls its
phosphorylation, stability, intracellular trafficking itinerary,
and chemokine scavenging properties.
-!- PTM: Phosphorylated on serine residues in the C-terminal
cytoplasmic tail. {ECO:0000269|PubMed:18201974}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
Atypical chemokine receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; U94888; AAB97728.1; -; mRNA.
EMBL; Y12815; CAA73346.1; -; mRNA.
EMBL; AY262687; AAP20651.1; -; Genomic_DNA.
EMBL; BT006800; AAP35446.1; -; mRNA.
EMBL; AK313561; BAG36335.1; -; mRNA.
EMBL; BC008816; AAH08816.1; -; mRNA.
EMBL; BC011631; AAH11631.1; -; mRNA.
EMBL; BC020558; AAH20558.1; -; mRNA.
EMBL; BC101629; AAI01630.1; -; mRNA.
EMBL; BC112045; AAI12046.1; -; mRNA.
CCDS; CCDS2706.1; -.
RefSeq; NP_001287.2; NM_001296.4.
UniGene; Hs.146346; -.
ProteinModelPortal; O00590; -.
BioGrid; 107643; 9.
IntAct; O00590; 6.
STRING; 9606.ENSP00000273145; -.
iPTMnet; O00590; -.
PhosphoSitePlus; O00590; -.
BioMuta; CCBP2; -.
PaxDb; O00590; -.
PeptideAtlas; O00590; -.
PRIDE; O00590; -.
ProteomicsDB; 47990; -.
DNASU; 1238; -.
Ensembl; ENST00000422265; ENSP00000416996; ENSG00000144648.
Ensembl; ENST00000442925; ENSP00000396150; ENSG00000144648.
GeneID; 1238; -.
KEGG; hsa:1238; -.
UCSC; uc003cme.4; human.
CTD; 1238; -.
DisGeNET; 1238; -.
EuPathDB; HostDB:ENSG00000144648.15; -.
GeneCards; ACKR2; -.
HGNC; HGNC:1565; ACKR2.
HPA; HPA013819; -.
HPA; HPA073493; -.
MIM; 602648; gene.
neXtProt; NX_O00590; -.
OpenTargets; ENSG00000144648; -.
PharmGKB; PA26139; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118785; -.
HOGENOM; HOG000234122; -.
HOVERGEN; HBG106917; -.
InParanoid; O00590; -.
KO; K04187; -.
OMA; LWFPYNL; -.
OrthoDB; EOG091G0FFG; -.
PhylomeDB; O00590; -.
TreeFam; TF330966; -.
GeneWiki; CCBP2; -.
GenomeRNAi; 1238; -.
PRO; PR:O00590; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144648; -.
CleanEx; HS_CCBP2; -.
CleanEx; HS_CCR10; -.
ExpressionAtlas; O00590; baseline and differential.
Genevisible; O00590; HS.
GO; GO:0005884; C:actin filament; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0019957; F:C-C chemokine binding; IEA:Ensembl.
GO; GO:0016493; F:C-C chemokine receptor activity; IEA:Ensembl.
GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
GO; GO:0005044; F:scavenger receptor activity; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
InterPro; IPR033037; Ackr2.
InterPro; IPR000355; Chemokine_rcpt.
InterPro; IPR001277; CXCR4/ACKR2.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR10489:SF735; PTHR10489:SF735; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00657; CCCHEMOKINER.
PRINTS; PR00645; CXCCHMKINER4.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Inflammatory response;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 384 Atypical chemokine receptor 2.
/FTId=PRO_0000069219.
TOPO_DOM 1 50 Extracellular. {ECO:0000255}.
TRANSMEM 51 71 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 72 92 Cytoplasmic. {ECO:0000255}.
TRANSMEM 93 113 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 114 118 Extracellular. {ECO:0000255}.
TRANSMEM 119 140 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 141 162 Cytoplasmic. {ECO:0000255}.
TRANSMEM 163 183 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 184 217 Extracellular. {ECO:0000255}.
TRANSMEM 218 238 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 239 250 Cytoplasmic. {ECO:0000255}.
TRANSMEM 251 271 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 272 293 Extracellular. {ECO:0000255}.
TRANSMEM 294 314 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 315 384 Cytoplasmic. {ECO:0000255}.
REGION 327 384 C-terminal cytoplasmic tail.
CARBOHYD 19 19 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 117 195 {ECO:0000255|PROSITE-ProRule:PRU00521}.
VARIANT 41 41 V -> A (in dbSNP:rs2228467).
/FTId=VAR_049379.
VARIANT 248 248 A -> V (in dbSNP:rs2228469).
/FTId=VAR_049380.
VARIANT 311 311 L -> V (in dbSNP:rs6779520).
/FTId=VAR_049381.
VARIANT 373 373 Y -> S (in dbSNP:rs2228468).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_024252.
CONFLICT 17 17 S -> A (in Ref. 1; AAB97728).
{ECO:0000305}.
CONFLICT 161 161 S -> N (in Ref. 1; AAB97728).
{ECO:0000305}.
CONFLICT 356 356 Q -> L (in Ref. 1; AAB97728).
{ECO:0000305}.
SEQUENCE 384 AA; 43443 MW; 464C5703C1DE9A6A CRC64;
MAATASPQPL ATEDADSENS SFYYYDYLDE VAFMLCRKDA VVSFGKVFLP VFYSLIFVLG
LSGNLLLLMV LLRYVPRRRM VEIYLLNLAI SNLLFLVTLP FWGISVAWHW VFGSFLCKMV
STLYTINFYS GIFFISCMSL DKYLEIVHAQ PYHRLRTRAK SLLLATIVWA VSLAVSIPDM
VFVQTHENPK GVWNCHADFG GHGTIWKLFL RFQQNLLGFL LPLLAMIFFY SRIGCVLVRL
RPAGQGRALK IAAALVVAFF VLWFPYNLTL FLHTLLDLQV FGNCEVSQHL DYALQVTESI
AFLHCCFSPI LYAFSSHRFR QYLKAFLAAV LGWHLAPGTA QASLSSCSES SILTAQEEMT
GMNDLGERQS ENYPNKEDVG NKSA


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18-461-10474 C-C chemokine receptor type 6 - C-C CKR-6; CC-CKR-6; CCR-6; LARC receptor; GPR-CY4; GPRCY4; Chemokine receptor-like 3; CKR-L3; DRY6; G-protein coupled receptor 29; CD196 antigen Polyclonal 0.05 ml
15-288-21049 C-C chemokine receptor type 6 - C-C CKR-6; CC-CKR-6; CCR-6; LARC receptor; GPR-CY4; GPRCY4; Chemokine receptor-like 3; CKR-L3; DRY6; G-protein coupled receptor 29; CD196 antigen Polyclonal 0.1 mg
18-661-15051 CX3C chemokine receptor 1 - C-X3-C CKR-1; CX3CR1; Fractalkine receptor; G-protein coupled receptor 13; V28; Beta chemokine receptor-like 1; CMK-BRL-1; CMKBLR1 Polyclonal 0.1 mg
15-288-21051 CX3C chemokine receptor 1 - C-X3-C CKR-1; CX3CR1; Fractalkine receptor; G-protein coupled receptor 13; V28; Beta chemokine receptor-like 1; CMK-BRL-1; CMKBLR1 Polyclonal 0.1 mg
18-661-15074 CX3C chemokine receptor 1 - C-X3-C CKR-1; CX3CR1; Fractalkine receptor; G-protein coupled receptor 13; V28; Beta chemokine receptor-like 1; CMK-BRL-1; CMKBLR1 Polyclonal 0.1 mg
15-288-21051 CX3C chemokine receptor 1 - C-X3-C CKR-1; CX3CR1; Fractalkine receptor; G-protein coupled receptor 13; V28; Beta chemokine receptor-like 1; CMK-BRL-1; CMKBLR1 Polyclonal 0.05 mg


 

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