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C-C chemokine receptor type 6 (C-C CKR-6) (CC-CKR-6) (CCR-6) (KY411) (CD antigen CD196)

 CCR6_MOUSE              Reviewed;         367 AA.
O54689;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
20-JUN-2018, entry version 141.
RecName: Full=C-C chemokine receptor type 6;
Short=C-C CKR-6;
Short=CC-CKR-6;
Short=CCR-6;
AltName: Full=KY411;
AltName: CD_antigen=CD196;
Name=Ccr6; Synonyms=Cmkbr6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
Yanagihara S., Komura E., Yamaguchi Y.;
"Mouse G protein-coupled receptor KY411.";
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9862452; DOI=10.1016/S0014-5793(98)01450-1;
Varona R., Zaballos A., Gutierrez J., Martin P., Roncal F.,
Albar J.P., Ardavin C., Marquez G.;
"Molecular cloning, functional characterization and mRNA expression
analysis of the murine chemokine receptor CCR6 and its specific ligand
MIP-3alpha.";
FEBS Lett. 440:188-194(1998).
[3]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=19050256; DOI=10.4049/jimmunol.181.12.8391;
Yamazaki T., Yang X.O., Chung Y., Fukunaga A., Nurieva R., Pappu B.,
Martin-Orozco N., Kang H.S., Ma L., Panopoulos A.D., Craig S.,
Watowich S.S., Jetten A.M., Tian Q., Dong C.;
"CCR6 regulates the migration of inflammatory and regulatory T
cells.";
J. Immunol. 181:8391-8401(2008).
[4]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=19129757; DOI=10.1038/mi.2008.84;
Wang C., Kang S.G., Lee J., Sun Z., Kim C.H.;
"The roles of CCR6 in migration of Th17 cells and regulation of
effector T-cell balance in the gut.";
Mucosal Immunol. 2:173-183(2009).
[5]
FUNCTION, AND BINDING TO CCL20; DEFB4 AND DEFB4A.
PubMed=20068036; DOI=10.1074/jbc.M109.091090;
Roehrl J., Yang D., Oppenheim J.J., Hehlgans T.;
"Specific binding and chemotactic activity of mBD4 and its functional
orthologue hBD2 to CCR6-expressing cells.";
J. Biol. Chem. 285:7028-7034(2010).
[6]
REVIEW, AND FUNCTION.
PubMed=21376174; DOI=10.1016/j.yexcr.2010.12.018;
Ito T., Carson W.F. IV, Cavassani K.A., Connett J.M., Kunkel S.L.;
"CCR6 as a mediator of immunity in the lung and gut.";
Exp. Cell Res. 317:613-619(2011).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24638065; DOI=10.1038/icb.2014.14;
Bunting M.D., Comerford I., Kara E.E., Korner H., McColl S.R.;
"CCR6 supports migration and differentiation of a subset of DN1 early
thymocyte progenitors but is not required for thymic nTreg
development.";
Immunol. Cell Biol. 92:489-498(2014).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23765988; DOI=10.1002/jcp.24418;
Caballero-Campo P., Buffone M.G., Benencia F., Conejo-Garcia J.R.,
Rinaudo P.F., Gerton G.L.;
"A role for the chemokine receptor CCR6 in mammalian sperm motility
and chemotaxis.";
J. Cell. Physiol. 229:68-78(2014).
[9]
FUNCTION.
PubMed=25122636; DOI=10.1126/scitranslmed.3009071;
Diao R., Fok K.L., Chen H., Yu M.K., Duan Y., Chung C.M., Li Z.,
Wu H., Li Z., Zhang H., Ji Z., Zhen W., Ng C.F., Gui Y., Cai Z.,
Chan H.C.;
"Deficient human beta-defensin 1 underlies male infertility associated
with poor sperm motility and genital tract infection.";
Sci. Transl. Med. 6:249RA108-249RA108(2014).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25505290; DOI=10.4049/jimmunol.1401553;
Elgueta R., Marks E., Nowak E., Menezes S., Benson M., Raman V.S.,
Ortiz C., O'Connell S., Hess H., Lord G.M., Noelle R.;
"CCR6-dependent positioning of memory B cells is essential for their
ability to mount a recall response to antigen.";
J. Immunol. 194:505-513(2015).
[11]
FUNCTION, AND INDUCTION.
PubMed=27174992; DOI=10.1126/science.aaf4822;
Reboldi A., Arnon T.I., Rodda L.B., Atakilit A., Sheppard D.,
Cyster J.G.;
"IgA production requires B cell interaction with subepithelial
dendritic cells in Peyer's patches.";
Science 352:0-0(2016).
-!- FUNCTION: Receptor for the C-C type chemokine CCL20. Binds to
CCL20 and subsequently transduces a signal by increasing the
intracellular calcium ion levels (PubMed:20068036). Although CCL20
is its major ligand it can also act as a receptor for non-
chemokine ligands such as beta-defensins (PubMed:25122636). Binds
to defensin DEFB1 leading to increase in intracellular calcium
ions and cAMP levels. Its binding to DEFB1 is essential for the
function of DEFB1 in regulating sperm motility and bactericidal
activity (By similarity). Binds to defensins DEFB4 and DEFB4A/B
and mediates their chemotactic effects (PubMed:20068036). The
ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis
of dendritic cells (DC), effector/memory T-cells and B-cells and
plays an important role at skin and mucosal surfaces under
homeostatic and inflammatory conditions, as well as in pathology,
including cancer and various autoimmune diseases. CCR6-mediated
signals are essential for immune responses to microbes in the
intestinal mucosa and in the modulation of inflammatory responses
initiated by tissue insult and trauma (PubMed:21376174). CCR6 is
essential for the recruitment of both the proinflammatory IL17
producing helper T-cells (Th17) and the regulatory T-cells (Treg)
to sites of inflammation (PubMed:19050256). Required for the
normal migration of Th17 cells in Peyers patches and other related
tissue sites of the intestine and plays a role in regulating
effector T-cell balance and distribution in inflamed intestine
(PubMed:19129757). Plays an important role in the coordination of
early thymocyte precursor migration events important for normal
subsequent thymocyte precursor development, but is not required
for the formation of normal thymic natural regulatory T-cells
(nTregs). Required for optimal differentiation of DN2 and DN3
thymocyte precursors (PubMed:24638065). Essential for B-cell
localization in the subepithelial dome of Peyers-patches and for
efficient B-cell isotype switching to IgA in the Peyers-patches
(PubMed:27174992). Essential for appropriate anatomical
distribution of memory B-cells in the spleen and for the secondary
recall response of memory B-cells (PubMed:25505290). Positively
regulates sperm motility and chemotaxis via its binding to CCL20
(PubMed:23765988). {ECO:0000250|UniProtKB:P51684,
ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:19129757,
ECO:0000269|PubMed:20068036, ECO:0000269|PubMed:23765988,
ECO:0000269|PubMed:24638065, ECO:0000269|PubMed:25122636,
ECO:0000269|PubMed:25505290, ECO:0000269|PubMed:27174992,
ECO:0000303|PubMed:21376174}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23765988};
Multi-pass membrane protein {ECO:0000255}. Cell surface
{ECO:0000250|UniProtKB:P51684}.
-!- TISSUE SPECIFICITY: Sperm. Mainly localized in the principal piece
and neck region of the tail but is also found in the acrosomal
region in a small percentage of sperm cells. Expressed in natural
regulatory T cells (nTregs) and a subset of early thymocyte
progenitor double-negative 1 (DN1) cells. Expressed in memory B
cells. Expressed by IL17 producing helper T-cells (Th17), type 1
effector cells (Th1), type 2 effector cells (Th2) and regulatory
T-cells (Treg) (at protein level). Expressed by Th17 cells in
spleen, Peyers patches, and lamina propria of small and large
intestine. Highly expressed in testis, lung, colon, and dendritic
cells. {ECO:0000269|PubMed:19050256, ECO:0000269|PubMed:19129757,
ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:24638065,
ECO:0000269|PubMed:25505290}.
-!- INDUCTION: Up-regulated on pre-germinal center B-cells in a CD40-
dependent manner. Up-regulated and down-regulated in Th17 cells by
TGFB1 and IL2 respectively. {ECO:0000269|PubMed:19050256,
ECO:0000269|PubMed:19129757, ECO:0000269|PubMed:27174992}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AB009369; BAA23776.1; -; mRNA.
EMBL; AJ222714; CAA10956.1; -; Genomic_DNA.
CCDS; CCDS28381.1; -.
RefSeq; NP_001177262.1; NM_001190333.1.
RefSeq; NP_001177263.1; NM_001190334.1.
RefSeq; NP_001177264.1; NM_001190335.1.
RefSeq; NP_001177265.1; NM_001190336.1.
RefSeq; NP_001177266.1; NM_001190337.1.
RefSeq; NP_033965.1; NM_009835.4.
RefSeq; XP_006523349.1; XM_006523286.3.
RefSeq; XP_006523351.1; XM_006523288.3.
RefSeq; XP_006523353.1; XM_006523290.3.
RefSeq; XP_006523354.1; XM_006523291.1.
RefSeq; XP_006523355.1; XM_006523292.3.
RefSeq; XP_011244488.1; XM_011246186.2.
RefSeq; XP_011244490.1; XM_011246188.1.
RefSeq; XP_017172707.1; XM_017317218.1.
RefSeq; XP_017172708.1; XM_017317219.1.
RefSeq; XP_017172709.1; XM_017317220.1.
UniGene; Mm.8007; -.
ProteinModelPortal; O54689; -.
STRING; 10090.ENSMUSP00000095029; -.
iPTMnet; O54689; -.
PhosphoSitePlus; O54689; -.
PaxDb; O54689; -.
PRIDE; O54689; -.
Ensembl; ENSMUST00000097418; ENSMUSP00000095029; ENSMUSG00000040899.
Ensembl; ENSMUST00000164411; ENSMUSP00000131153; ENSMUSG00000040899.
Ensembl; ENSMUST00000166348; ENSMUSP00000128559; ENSMUSG00000040899.
Ensembl; ENSMUST00000167956; ENSMUSP00000128529; ENSMUSG00000040899.
Ensembl; ENSMUST00000177568; ENSMUSP00000137249; ENSMUSG00000040899.
Ensembl; ENSMUST00000180103; ENSMUSP00000135945; ENSMUSG00000040899.
GeneID; 12458; -.
KEGG; mmu:12458; -.
UCSC; uc008ajd.2; mouse.
CTD; 1235; -.
MGI; MGI:1333797; Ccr6.
eggNOG; ENOG410IKPR; Eukaryota.
eggNOG; ENOG410XSP7; LUCA.
GeneTree; ENSGT00760000118785; -.
HOGENOM; HOG000234122; -.
HOVERGEN; HBG106917; -.
InParanoid; O54689; -.
KO; K04181; -.
OMA; IMKDLWC; -.
OrthoDB; EOG091G08B0; -.
PhylomeDB; O54689; -.
TreeFam; TF330966; -.
Reactome; R-MMU-1461957; Beta defensins.
Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
Reactome; R-MMU-418594; G alpha (i) signalling events.
PRO; PR:O54689; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000040899; -.
CleanEx; MM_CCR6; -.
ExpressionAtlas; O54689; baseline and differential.
Genevisible; O54689; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB.
GO; GO:0097225; C:sperm midpiece; ISO:MGI.
GO; GO:0097524; C:sperm plasma membrane; IDA:UniProtKB.
GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
GO; GO:0019957; F:C-C chemokine binding; IDA:UniProtKB.
GO; GO:0016493; F:C-C chemokine receptor activity; IDA:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
GO; GO:1904155; P:DN2 thymocyte differentiation; IMP:UniProtKB.
GO; GO:1904156; P:DN3 thymocyte differentiation; IMP:UniProtKB.
GO; GO:0048290; P:isotype switching to IgA isotypes; IMP:UniProtKB.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:UniProtKB.
GO; GO:0072676; P:lymphocyte migration; IMP:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0060474; P:positive regulation of flagellated sperm motility involved in capacitation; IDA:UniProtKB.
GO; GO:2000404; P:regulation of T cell migration; IMP:UniProtKB.
GO; GO:0072678; P:T cell migration; IDA:UniProtKB.
GO; GO:0072679; P:thymocyte migration; IDA:UniProtKB.
CDD; cd15172; 7tmA_CCR6; 1.
InterPro; IPR004067; Chemokine_CCR6.
InterPro; IPR000355; Chemokine_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR10489:SF611; PTHR10489:SF611; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00657; CCCHEMOKINER.
PRINTS; PR01529; CHEMOKINER6.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 367 C-C chemokine receptor type 6.
/FTId=PRO_0000069287.
TOPO_DOM 1 39 Extracellular. {ECO:0000255}.
TRANSMEM 40 66 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 67 75 Cytoplasmic. {ECO:0000255}.
TRANSMEM 76 96 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 97 111 Extracellular. {ECO:0000255}.
TRANSMEM 112 133 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 134 151 Cytoplasmic. {ECO:0000255}.
TRANSMEM 152 172 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 173 203 Extracellular. {ECO:0000255}.
TRANSMEM 204 230 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 231 246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 247 271 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 272 295 Extracellular. {ECO:0000255}.
TRANSMEM 296 313 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 314 367 Cytoplasmic. {ECO:0000255}.
CARBOHYD 2 2 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 110 189 {ECO:0000250|UniProtKB:P51684,
ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 367 AA; 42103 MW; 6A309AF833B1117E CRC64;
MNSTESYFGT DDYDNTEYYS IPPDHGPCSL EEVRNFTKVF VPIAYSLICV FGLLGNIMVV
MTFAFYKKAR SMTDVYLLNM AITDILFVLT LPFWAVTHAT NTWVFSDALC KLMKGTYAVN
FNCGMLLLAC ISMDRYIAIV QATKSFRVRS RTLTHSKVIC VAVWFISIII SSPTFIFNKK
YELQDRDVCE PRYRSVSEPI TWKLLGMGLE LFFGFFTPLL FMVFCYLFII KTLVQAQNSK
RHRAIRVVIA VVLVFLACQI PHNMVLLVTA VNTGKVGRSC STEKVLAYTR NVAEVLAFLH
CCLNPVLYAF IGQKFRNYFM KIMKDVWCMR RKNKMPGFLC ARVYSESYIS RQTSETVEND
NASSFTM


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