CCR7_HUMAN
ID CCR7_HUMAN Reviewed; 378 AA.
AC P32248;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=C-C chemokine receptor type 7;
DE Short=C-C CKR-7;
DE Short=CC-CKR-7;
DE Short=CCR-7;
DE AltName: Full=BLR2;
DE AltName: Full=CDw197;
DE AltName: Full=Epstein-Barr virus-induced G-protein coupled receptor 1;
DE Short=EBI1;
DE Short=EBV-induced G-protein coupled receptor 1;
DE AltName: Full=MIP-3 beta receptor;
DE AltName: CD_antigen=CD197;
DE Flags: Precursor;
GN Name=CCR7; Synonyms=CMKBR7, EBI1, EVI1;
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 [MRNA].
RX PubMed=8383238; DOI=10.1128/jvi.67.4.2209-2220.1993;
RA Birkenbach M.P., Josefsen K., Yalamanchili R.R., Lenoir G.M., Kieff E.;
RT "Epstein-Barr virus-induced genes: first lymphocyte-specific G protein-
RT coupled peptide receptors.";
RL J. Virol. 67:2209-2220(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Placenta;
RX PubMed=7851893; DOI=10.1006/geno.1994.1553;
RA Schweickart V.L., Raport C.J., Godiska R., Byers M.G., Eddy R.L. Jr.,
RA Shows T.B., Gray P.W.;
RT "Cloning of human and mouse EBI1, a lymphoid-specific G-protein-coupled
RT receptor encoded on human chromosome 17q12-q21.2.";
RL Genomics 23:643-650(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., 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 (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Receptor for the MIP-3-beta chemokine. Probable mediator of
CC EBV effects on B-lymphocytes or of normal lymphocyte functions.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in various lymphoid tissues and activated
CC B- and T-lymphocytes, strongly up-regulated in B-cells infected with
CC Epstein-Barr virus and T-cells infected with herpesvirus 6 or 7.
CC -!- INDUCTION: By Epstein-Barr virus (EBV).
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry;
CC URL="https://en.wikipedia.org/wiki/CC_chemokine_receptors";
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DR EMBL; L08176; AAA58615.1; -; mRNA.
DR EMBL; L31584; AAA74230.1; -; Genomic_DNA.
DR EMBL; L31582; AAA74230.1; JOINED; Genomic_DNA.
DR EMBL; L31583; AAA74230.1; JOINED; Genomic_DNA.
DR EMBL; L31581; AAA74231.1; -; mRNA.
DR EMBL; AY587876; AAT52232.1; -; mRNA.
DR EMBL; BC035343; AAH35343.1; -; mRNA.
DR CCDS; CCDS11369.1; -.
DR PIR; A45680; A45680.
DR PIR; B55735; B55735.
DR RefSeq; NP_001288643.1; NM_001301714.1.
DR RefSeq; NP_001288645.1; NM_001301716.1.
DR RefSeq; NP_001288646.1; NM_001301717.1.
DR RefSeq; NP_001288647.1; NM_001301718.1.
DR RefSeq; NP_001829.1; NM_001838.3.
DR PDB; 6QZH; X-ray; 2.10 A; A=46-247.
DR PDBsum; 6QZH; -.
DR AlphaFoldDB; P32248; -.
DR SMR; P32248; -.
DR BioGRID; 107641; 3.
DR DIP; DIP-5855N; -.
DR IntAct; P32248; 4.
DR MINT; P32248; -.
DR STRING; 9606.ENSP00000246657; -.
DR BindingDB; P32248; -.
DR ChEMBL; CHEMBL4594; -.
DR GuidetoPHARMACOLOGY; 64; -.
DR GlyGen; P32248; 1 site.
DR iPTMnet; P32248; -.
DR PhosphoSitePlus; P32248; -.
DR BioMuta; CCR7; -.
DR DMDM; 1352335; -.
DR MassIVE; P32248; -.
DR MaxQB; P32248; -.
DR PaxDb; P32248; -.
DR PeptideAtlas; P32248; -.
DR PRIDE; P32248; -.
DR ProteomicsDB; 54856; -.
DR ABCD; P32248; 3 sequenced antibodies.
DR Antibodypedia; 3533; 1017 antibodies from 49 providers.
DR DNASU; 1236; -.
DR Ensembl; ENST00000246657.2; ENSP00000246657.2; ENSG00000126353.3.
DR GeneID; 1236; -.
DR KEGG; hsa:1236; -.
DR MANE-Select; ENST00000246657.2; ENSP00000246657.2; NM_001838.4; NP_001829.1.
DR UCSC; uc002huw.4; human.
DR CTD; 1236; -.
DR DisGeNET; 1236; -.
DR GeneCards; CCR7; -.
DR HGNC; HGNC:1608; CCR7.
DR HPA; ENSG00000126353; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 600242; gene.
DR neXtProt; NX_P32248; -.
DR OpenTargets; ENSG00000126353; -.
DR PharmGKB; PA26172; -.
DR VEuPathDB; HostDB:ENSG00000126353; -.
DR eggNOG; ENOG502QUZ9; Eukaryota.
DR GeneTree; ENSGT01030000234667; -.
DR InParanoid; P32248; -.
DR OMA; TLACFRC; -.
DR OrthoDB; 715251at2759; -.
DR PhylomeDB; P32248; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P32248; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P32248; -.
DR SIGNOR; P32248; -.
DR BioGRID-ORCS; 1236; 6 hits in 1068 CRISPR screens.
DR GeneWiki; C-C_chemokine_receptor_type_7; -.
DR GenomeRNAi; 1236; -.
DR Pharos; P32248; Tchem.
DR PRO; PR:P32248; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P32248; protein.
DR Bgee; ENSG00000126353; Expressed in vermiform appendix and 104 other tissues.
DR ExpressionAtlas; P32248; baseline and differential.
DR Genevisible; P32248; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; ISS:BHF-UCL.
DR GO; GO:0038117; F:C-C motif chemokine 19 receptor activity; IDA:UniProtKB.
DR GO; GO:0038121; F:C-C motif chemokine 21 receptor activity; IDA:UniProtKB.
DR GO; GO:0035757; F:chemokine (C-C motif) ligand 19 binding; IPI:BHF-UCL.
DR GO; GO:0035758; F:chemokine (C-C motif) ligand 21 binding; IPI:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:BHF-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; IC:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:BHF-UCL.
DR GO; GO:0002407; P:dendritic cell chemotaxis; IC:BHF-UCL.
DR GO; GO:0001768; P:establishment of T cell polarity; IC:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; NAS:BHF-UCL.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; TAS:BHF-UCL.
DR GO; GO:0097029; P:mature conventional dendritic cell differentiation; ISS:BHF-UCL.
DR GO; GO:0002408; P:myeloid dendritic cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IC:BHF-UCL.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; ISS:BHF-UCL.
DR GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IC:BHF-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; IC:BHF-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IC:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; ISS:BHF-UCL.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IC:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IC:BHF-UCL.
DR GO; GO:2000526; P:positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation; ISS:BHF-UCL.
DR GO; GO:0002922; P:positive regulation of humoral immune response; ISS:BHF-UCL.
DR GO; GO:0002885; P:positive regulation of hypersensitivity; ISS:BHF-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IC:BHF-UCL.
DR GO; GO:2000522; P:positive regulation of immunological synapse formation; ISS:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IC:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:BHF-UCL.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IC:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IC:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IC:BHF-UCL.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IC:BHF-UCL.
DR GO; GO:2000525; P:positive regulation of T cell costimulation; ISS:BHF-UCL.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2000547; P:regulation of dendritic cell dendrite assembly; ISS:BHF-UCL.
DR GO; GO:0032649; P:regulation of interferon-gamma production; ISS:BHF-UCL.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISS:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IC:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071731; P:response to nitric oxide; IC:BHF-UCL.
DR GO; GO:0034695; P:response to prostaglandin E; IC:BHF-UCL.
DR GO; GO:0031529; P:ruffle organization; IC:BHF-UCL.
DR InterPro; IPR001718; Chemokine_CCR7.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00641; CHEMOKINER7.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..378
FT /note="C-C chemokine receptor type 7"
FT /id="PRO_0000012735"
FT TOPO_DOM 25..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..130
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..152
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..247
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..331
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 7
FT /note="M -> V (in dbSNP:rs2228015)"
FT /id="VAR_049383"
FT CONFLICT 182..183
FT /note="IW -> SA (in Ref. 1; AAA58615)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> I (in Ref. 1; AAA58615)"
FT /evidence="ECO:0000305"
FT HELIX 56..84
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 125..157
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 173..190
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:6QZH"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6QZH"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6QZH"
FT HELIX 233..247
FT /evidence="ECO:0007829|PDB:6QZH"
SQ SEQUENCE 378 AA; 42874 MW; D4CB4213841A1BD4 CRC64;
MDLGKPMKSV LVVALLVIFQ VCLCQDEVTD DYIGDNTTVD YTLFESLCSK KDVRNFKAWF
LPIMYSIICF VGLLGNGLVV LTYIYFKRLK TMTDTYLLNL AVADILFLLT LPFWAYSAAK
SWVFGVHFCK LIFAIYKMSF FSGMLLLLCI SIDRYVAIVQ AVSAHRHRAR VLLISKLSCV
GIWILATVLS IPELLYSDLQ RSSSEQAMRC SLITEHVEAF ITIQVAQMVI GFLVPLLAMS
FCYLVIIRTL LQARNFERNK AIKVIIAVVV VFIVFQLPYN GVVLAQTVAN FNITSSTCEL
SKQLNIAYDV TYSLACVRCC VNPFLYAFIG VKFRNDLFKL FKDLGCLSQE QLRQWSSCRH
IRRSSMSVEA ETTTTFSP
