ID CCR6_HUMAN Reviewed; 374 AA. AC P51684; E1P5C6; P78553; Q92846; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 212. DE RecName: Full=C-C chemokine receptor type 6; DE Short=C-C CKR-6; DE Short=CC-CKR-6; DE Short=CCR-6; DE AltName: Full=Chemokine receptor-like 3; DE Short=CKR-L3; DE AltName: Full=DRY6; DE AltName: Full=G-protein coupled receptor 29; DE AltName: Full=GPR-CY4; DE Short=GPRCY4; DE AltName: Full=LARC receptor; DE AltName: CD_antigen=CD196; GN Name=CCR6; Synonyms=CKRL3, CMKBR6, GPR29, STRL22; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=9169459; DOI=10.1074/jbc.272.23.14893; RA Baba M., Imai T., Nishimura M., Kakizaki M., Takagi S., Hieshima K., RA Nomiyama H., Yoshie O.; RT "Identification of CCR6, the specific receptor for a novel lymphocyte- RT directed CC chemokine LARC."; RL J. Biol. Chem. 272:14893-14898(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RA Lautens L.L., Modi W., Bonner T.I.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX PubMed=8886020; DOI=10.1006/bbrc.1996.1595; RA Zaballos A., Varona R., Gutierrez J., Lind P., Marquez G.; RT "Molecular cloning and RNA expression of two new human chemokine receptor- RT like genes."; RL Biochem. Biophys. Res. Commun. 227:846-853(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA McCoy R., Perlmutter D.H.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9070937; DOI=10.1006/geno.1996.4544; RA Liao F., Lee H.-H., Farber J.M.; RT "Cloning of STRL22, a new human gene encoding a G-protein-coupled receptor RT related to chemokine receptors and located on chromosome 6q27."; RL Genomics 40:175-180(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Warren C.N., Aronstam R.S., Sharma S.V.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP DISULFIDE BOND, MUTAGENESIS OF CYS-36; CYS-57; CYS-118; CYS-131; CYS-138; RP CYS-168; CYS-197; CYS-233; CYS-266; CYS-288; CYS-309; CYS-310; CYS-336 AND RP CYS-348, AND SUBCELLULAR LOCATION. RX PubMed=12081481; DOI=10.1021/bi025855y; RA Ai L.S., Liao F.; RT "Mutating the four extracellular cysteines in the chemokine receptor CCR6 RT reveals their differing roles in receptor trafficking, ligand binding, and RT signaling."; RL Biochemistry 41:8332-8341(2002). RN [11] RP FUNCTION, AND BINDING TO CCL20; DEFB4 AND DEFB4A. RX PubMed=20068036; DOI=10.1074/jbc.m109.091090; RA Roehrl J., Yang D., Oppenheim J.J., Hehlgans T.; RT "Specific binding and chemotactic activity of mBD4 and its functional RT orthologue hBD2 to CCR6-expressing cells."; RL J. Biol. Chem. 285:7028-7034(2010). RN [12] RP REVIEW, AND FUNCTION. RX PubMed=21376174; DOI=10.1016/j.yexcr.2010.12.018; RA Ito T., Carson W.F. IV, Cavassani K.A., Connett J.M., Kunkel S.L.; RT "CCR6 as a mediator of immunity in the lung and gut."; RL Exp. Cell Res. 317:613-619(2011). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=23765988; DOI=10.1002/jcp.24418; RA Caballero-Campo P., Buffone M.G., Benencia F., Conejo-Garcia J.R., RA Rinaudo P.F., Gerton G.L.; RT "A role for the chemokine receptor CCR6 in mammalian sperm motility and RT chemotaxis."; RL J. Cell. Physiol. 229:68-78(2014). RN [14] RP FUNCTION, TISSUE SPECIFICITY, AND BINDING TO DEFB1. RX PubMed=25122636; DOI=10.1126/scitranslmed.3009071; RA Diao R., Fok K.L., Chen H., Yu M.K., Duan Y., Chung C.M., Li Z., Wu H., RA Li Z., Zhang H., Ji Z., Zhen W., Ng C.F., Gui Y., Cai Z., Chan H.C.; RT "Deficient human beta-defensin 1 underlies male infertility associated with RT poor sperm motility and genital tract infection."; RL Sci. Transl. Med. 6:249RA108-249RA108(2014). RN [15] RP REVIEW, AND FUNCTION. RX PubMed=25585877; DOI=10.1016/j.cyto.2014.11.029; RA Lee A.Y., Phan T.K., Hulett M.D., Koerner H.; RT "The relationship between CCR6 and its binding partners: does the CCR6- RT CCL20 axis have to be extended?"; RL Cytokine 72:97-101(2015). CC -!- FUNCTION: Receptor for the C-C type chemokine CCL20 (PubMed:9169459). CC Binds to CCL20 and subsequently transduces a signal by increasing the CC intracellular calcium ion levels (PubMed:20068036). Although CCL20 is CC its major ligand it can also act as a receptor for non-chemokine CC ligands such as beta-defensins (PubMed:25585877). Binds to defensin CC DEFB1 leading to increase in intracellular calcium ions and cAMP CC levels. Its binding to DEFB1 is essential for the function of DEFB1 in CC regulating sperm motility and bactericidal activity (PubMed:25122636). CC Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic CC effects (PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is CC responsible for the chemotaxis of dendritic cells (DC), effector/ CC memory T-cells and B-cells and plays an important role at skin and CC mucosal surfaces under homeostatic and inflammatory conditions, as well CC as in pathology, including cancer and various autoimmune diseases. CC CCR6-mediated signals are essential for immune responses to microbes in CC the intestinal mucosa and in the modulation of inflammatory responses CC initiated by tissue insult and trauma (PubMed:21376174). CCR6 is CC essential for the recruitment of both the pro-inflammatory IL17 CC producing helper T-cells (Th17) and the regulatory T-cells (Treg) to CC sites of inflammation. Required for the normal migration of Th17 cells CC in Peyers-patches and other related tissue sites of the intestine and CC plays a role in regulating effector T-cell balance and distribution in CC inflamed intestine. Plays an important role in the coordination of CC early thymocyte precursor migration events important for normal CC subsequent thymocyte precursor development, but is not required for the CC formation of normal thymic natural regulatory T-cells (nTregs). CC Required for optimal differentiation of DN2 and DN3 thymocyte CC precursors. Essential for B-cell localization in the subepithelial dome CC of Peyers-patches and for efficient B-cell isotype switching to IgA in CC the Peyers-patches. Essential for appropriate anatomical distribution CC of memory B-cells in the spleen and for the secondary recall response CC of memory B-cells (By similarity). Positively regulates sperm motility CC and chemotaxis via its binding to CCL20 (PubMed:23765988). CC {ECO:0000250|UniProtKB:O54689, ECO:0000269|PubMed:20068036, CC ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:25122636, CC ECO:0000269|PubMed:9169459, ECO:0000303|PubMed:21376174, CC ECO:0000303|PubMed:25585877}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23765988}; CC Multi-pass membrane protein {ECO:0000255}. Cell surface CC {ECO:0000269|PubMed:12081481}. CC -!- TISSUE SPECIFICITY: Sperm. Mainly localized in the tail and in the CC postacrosomal region but is also found in the midpiece and basal region CC in a small percentage of sperm cells. Reduced levels found in the CC sperms of asthenozoospermia and leukocytospermia patients (at protein CC level). Spleen, lymph nodes, appendix, and fetal liver. Expressed in CC lymphocytes, T-cells and B-cells but not in natural killer cells, CC monocytes or granulocytes. {ECO:0000269|PubMed:23765988, CC ECO:0000269|PubMed:25122636, ECO:0000269|PubMed:8886020}. CC -!- INDUCTION: By IL2/interleukin-2. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB02144.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry; CC URL="https://en.wikipedia.org/wiki/CC_chemokine_receptors"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U45984; AAB62714.1; -; Genomic_DNA. DR EMBL; Z79784; CAB02144.1; ALT_INIT; Genomic_DNA. DR EMBL; U60000; AAB06949.1; -; mRNA. DR EMBL; U68030; AAC51124.1; -; mRNA. DR EMBL; U68032; AAC51125.1; -; Genomic_DNA. DR EMBL; AY242126; AAO92293.1; -; mRNA. DR EMBL; AL121935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47506.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47507.1; -; Genomic_DNA. DR EMBL; BC037960; AAH37960.1; -; mRNA. DR CCDS; CCDS5298.1; -. DR PIR; JC5068; JC5068. DR RefSeq; NP_004358.2; NM_004367.5. DR RefSeq; NP_113597.2; NM_031409.3. DR PDB; 6WWZ; EM; 3.34 A; R=2-374. DR PDBsum; 6WWZ; -. DR AlphaFoldDB; P51684; -. DR EMDB; EMD-21950; -. DR SMR; P51684; -. DR BioGRID; 107640; 88. DR DIP; DIP-5865N; -. DR IntAct; P51684; 1. DR MINT; P51684; -. DR STRING; 9606.ENSP00000343952; -. DR BindingDB; P51684; -. DR ChEMBL; CHEMBL4423; -. DR GuidetoPHARMACOLOGY; 63; -. DR GlyCosmos; P51684; 2 sites, No reported glycans. DR GlyGen; P51684; 2 sites. DR iPTMnet; P51684; -. DR PhosphoSitePlus; P51684; -. DR BioMuta; CCR6; -. DR DMDM; 2851567; -. DR MassIVE; P51684; -. DR PaxDb; 9606-ENSP00000343952; -. DR PeptideAtlas; P51684; -. DR ProteomicsDB; 56368; -. DR Antibodypedia; 2930; 896 antibodies from 40 providers. DR DNASU; 1235; -. DR Ensembl; ENST00000341935.10; ENSP00000343952.5; ENSG00000112486.18. DR Ensembl; ENST00000349984.6; ENSP00000339393.4; ENSG00000112486.18. DR Ensembl; ENST00000400926.5; ENSP00000383715.2; ENSG00000112486.18. DR Ensembl; ENST00000643861.1; ENSP00000493637.1; ENSG00000112486.18. DR GeneID; 1235; -. DR KEGG; hsa:1235; -. DR MANE-Select; ENST00000341935.10; ENSP00000343952.5; NM_031409.4; NP_113597.2. DR UCSC; uc003qvm.5; human. DR AGR; HGNC:1607; -. DR CTD; 1235; -. DR DisGeNET; 1235; -. DR GeneCards; CCR6; -. DR HGNC; HGNC:1607; CCR6. DR HPA; ENSG00000112486; Tissue enriched (lymphoid). DR MalaCards; CCR6; -. DR MIM; 601835; gene. DR neXtProt; NX_P51684; -. DR OpenTargets; ENSG00000112486; -. DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis. DR Orphanet; 220402; Limited cutaneous systemic sclerosis. DR PharmGKB; PA26171; -. DR VEuPathDB; HostDB:ENSG00000112486; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01030000234667; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; P51684; -. DR OMA; TKEICDH; -. DR OrthoDB; 5257535at2759; -. DR PhylomeDB; P51684; -. DR TreeFam; TF330966; -. DR PathwayCommons; P51684; -. DR Reactome; R-HSA-1461957; Beta defensins. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; P51684; -. DR BioGRID-ORCS; 1235; 9 hits in 1145 CRISPR screens. DR ChiTaRS; CCR6; human. DR GeneWiki; C-C_chemokine_receptor_type_6; -. DR GenomeRNAi; 1235; -. DR Pharos; P51684; Tchem. DR PRO; PR:P51684; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P51684; Protein. DR Bgee; ENSG00000112486; Expressed in lymph node and 78 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0036126; C:sperm flagellum; IDA:UniProtKB. DR GO; GO:0097225; C:sperm midpiece; IDA:UniProtKB. DR GO; GO:0097524; C:sperm plasma membrane; IDA:UniProtKB. DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB. DR GO; GO:0019957; F:C-C chemokine binding; IDA:UniProtKB. DR GO; GO:0016493; F:C-C chemokine receptor activity; IDA:UniProtKB. DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB. DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB. DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc. DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB. DR GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL. DR GO; GO:1904155; P:DN2 thymocyte differentiation; ISS:UniProtKB. DR GO; GO:1904156; P:DN3 thymocyte differentiation; ISS:UniProtKB. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0048290; P:isotype switching to IgA isotypes; ISS:UniProtKB. DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB. DR GO; GO:0072676; P:lymphocyte migration; ISS:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central. DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IBA:GO_Central. DR GO; GO:0060474; P:positive regulation of flagellated sperm motility involved in capacitation; IDA:UniProtKB. DR GO; GO:2000404; P:regulation of T cell migration; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0072678; P:T cell migration; ISS:UniProtKB. DR GO; GO:0072679; P:thymocyte migration; ISS:UniProtKB. DR CDD; cd15172; 7tmA_CCR6; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR004067; Chemokine_CCR6. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF611; C-C CHEMOKINE RECEPTOR TYPE 6; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. DR PRINTS; PR01529; CHEMOKINER6. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P51684; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor; KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..374 FT /note="C-C chemokine receptor type 6" FT /id="PRO_0000069286" FT TOPO_DOM 1..47 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 48..74 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 75..83 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 84..104 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 105..119 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 120..141 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 142..159 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 160..180 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 181..211 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 212..238 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 239..254 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 255..279 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 280..303 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 304..321 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 322..374 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 23 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 118..197 FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 36 FT /note="C->A: No loss of calcium flux but loss of chemotaxis FT in response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 36 FT /note="C->D,G: Loss of calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 36 FT /note="C->S: No loss of calcium flux but loss of chemotaxis FT in response to CCL20 stimulation, impaired CCL20-binding FT and no effect on cell surface expression; when associated FT with or without S-288. Loss of calcium flux in response to FT CCL20 stimulation and significant reduction in cell surface FT expression; when associated with S-118; S-197 and S-288." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 57 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 118 FT /note="C->S: Loss of calcium flux and chemotaxis in FT response to CCL20 stimulation, impaired CCL20-binding and FT significant reduction in cell surface expression; when FT associated with or without S-197. Loss of calcium flux in FT response to CCL20 stimulation and significant reduction in FT cell surface expression; when associated with S-36; S-197 FT and S-288." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 131 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 138 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 168 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 197 FT /note="C->S: Loss of calcium flux and chemotaxis in FT response to CCL20 stimulation, impaired CCL20-binding and FT significant reduction in cell surface expression; when FT associated with or without S-118. Loss of calcium flux in FT response to CCL20 stimulation and significant reduction in FT cell surface expression; when associated with S-36; S-118 FT and S-288." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 233 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 266 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 288 FT /note="C->A,G,R: No loss of calcium flux but loss of FT chemotaxis in response to CCL20 stimulation. No effect on FT cell surface expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 288 FT /note="C->S: No loss of calcium flux but loss of chemotaxis FT in response to CCL20 stimulation, impaired CCL20-binding FT and no effect on cell surface expression; when associated FT with or without S-36. Loss of calcium flux in response to FT CCL20 stimulation and significant reduction in cell surface FT expression; when associated with S-36; S-118 and S-197." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 309 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 310 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on cell surface FT expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 336 FT /note="C->S: Reduced calcium flux and chemotaxis in FT response to CCL20 stimulation, and reduced CCL20-binding. FT No effect on cell surface expression." FT /evidence="ECO:0000269|PubMed:12081481" FT MUTAGEN 348 FT /note="C->S: No effect on calcium flux and chemotaxis in FT response to CCL20 stimulation. No effect on CCL20-binding FT and cell surface expression." FT /evidence="ECO:0000269|PubMed:12081481" FT CONFLICT 60 FT /note="G -> A (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 74 FT /note="Y -> N (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 86 FT /note="L -> V (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="S -> T (in Ref. 5; AAC51124/AAC51125)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="T -> S (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 192 FT /note="Q -> L (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 206 FT /note="E -> V (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="I -> F (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT CONFLICT 370..374 FT /note="SSFTM -> VVLHYVIES (in Ref. 4; AAB06949)" FT /evidence="ECO:0000305" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 40..72 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 81..97 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 100..108 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 115..148 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 150..156 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 161..185 FT /evidence="ECO:0007829|PDB:6WWZ" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:6WWZ" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:6WWZ" FT STRAND 196..199 FT /evidence="ECO:0007829|PDB:6WWZ" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 207..241 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 249..279 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 288..319 FT /evidence="ECO:0007829|PDB:6WWZ" FT HELIX 321..334 FT /evidence="ECO:0007829|PDB:6WWZ" SQ SEQUENCE 374 AA; 42494 MW; D7F963534E990BC4 CRC64; MSGESMNFSD VFDSSEDYFV SVNTSYYSVD SEMLLCSLQE VRQFSRLFVP IAYSLICVFG LLGNILVVIT FAFYKKARSM TDVYLLNMAI ADILFVLTLP FWAVSHATGA WVFSNATCKL LKGIYAINFN CGMLLLTCIS MDRYIAIVQA TKSFRLRSRT LPRSKIICLV VWGLSVIISS STFVFNQKYN TQGSDVCEPK YQTVSEPIRW KLLMLGLELL FGFFIPLMFM IFCYTFIVKT LVQAQNSKRH KAIRVIIAVV LVFLACQIPH NMVLLVTAAN LGKMNRSCQS EKLIGYTKTV TEVLAFLHCC LNPVLYAFIG QKFRNYFLKI LKDLWCVRRK YKSSGFSCAG RYSENISRQT SETADNDNAS SFTM //