CCR7_MOUSE
ID CCR7_MOUSE Reviewed; 378 AA.
AC P47774; Q8CAS2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
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=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, Ebi1h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for the MIP-3-beta chemokine. {ECO:0000250}.
CC -!- INTERACTION:
CC P47774; P20963: CD247; Xeno; NbExp=2; IntAct=EBI-8038963, EBI-1165705;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L31580; AAA74232.1; -; mRNA.
DR EMBL; AK037965; BAC29909.1; -; mRNA.
DR EMBL; AK154349; BAE32532.1; -; mRNA.
DR EMBL; AK154849; BAE32875.1; -; mRNA.
DR EMBL; AL591366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16180.1; -; Genomic_DNA.
DR CCDS; CCDS25373.1; -.
DR PIR; A55735; A55735.
DR RefSeq; NP_001288642.1; NM_001301713.1.
DR RefSeq; NP_031745.2; NM_007719.2.
DR AlphaFoldDB; P47774; -.
DR SMR; P47774; -.
DR IntAct; P47774; 1.
DR MINT; P47774; -.
DR STRING; 10090.ENSMUSP00000099423; -.
DR GlyGen; P47774; 1 site.
DR PhosphoSitePlus; P47774; -.
DR EPD; P47774; -.
DR PaxDb; P47774; -.
DR PRIDE; P47774; -.
DR ProteomicsDB; 279951; -.
DR Antibodypedia; 3533; 1017 antibodies from 49 providers.
DR DNASU; 12775; -.
DR Ensembl; ENSMUST00000103134; ENSMUSP00000099423; ENSMUSG00000037944.
DR GeneID; 12775; -.
DR KEGG; mmu:12775; -.
DR UCSC; uc007lih.1; mouse.
DR CTD; 1236; -.
DR MGI; MGI:103011; Ccr7.
DR VEuPathDB; HostDB:ENSMUSG00000037944; -.
DR eggNOG; ENOG502QUZ9; Eukaryota.
DR GeneTree; ENSGT01030000234667; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P47774; -.
DR OMA; TLACFRC; -.
DR OrthoDB; 715251at2759; -.
DR PhylomeDB; P47774; -.
DR TreeFam; TF330966; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 12775; 3 hits in 76 CRISPR screens.
DR PRO; PR:P47774; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P47774; protein.
DR Bgee; ENSMUSG00000037944; Expressed in peripheral lymph node and 53 other tissues.
DR Genevisible; P47774; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
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; IMP:BHF-UCL.
DR GO; GO:0038117; F:C-C motif chemokine 19 receptor activity; ISO:MGI.
DR GO; GO:0038121; F:C-C motif chemokine 21 receptor activity; ISO:MGI.
DR GO; GO:0035757; F:chemokine (C-C motif) ligand 19 binding; ISS:BHF-UCL.
DR GO; GO:0035758; F:chemokine (C-C motif) ligand 21 binding; ISS:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:BHF-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS: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; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR GO; GO:0001768; P:establishment of T cell polarity; TAS:BHF-UCL.
DR GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:BHF-UCL.
DR GO; GO:0048535; P:lymph node development; TAS:BHF-UCL.
DR GO; GO:0002518; P:lymphocyte chemotaxis across high endothelial venule; TAS: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; IMP:BHF-UCL.
DR GO; GO:0002408; P:myeloid dendritic cell chemotaxis; ISO:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IMP:BHF-UCL.
DR GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; TAS:BHF-UCL.
DR GO; GO:0045060; P:negative thymic T cell selection; IMP:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; TAS: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; IDA:BHF-UCL.
DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; TAS:BHF-UCL.
DR GO; GO:2000526; P:positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation; IMP:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IC:BHF-UCL.
DR GO; GO:0002922; P:positive regulation of humoral immune response; IMP:BHF-UCL.
DR GO; GO:0002885; P:positive regulation of hypersensitivity; IMP:BHF-UCL.
DR GO; GO:2000522; P:positive regulation of immunological synapse formation; IMP:BHF-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IC:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:BHF-UCL.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IC:BHF-UCL.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; NAS:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:BHF-UCL.
DR GO; GO:0050766; P:positive regulation of phagocytosis; NAS:BHF-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IC:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; TAS:BHF-UCL.
DR GO; GO:2000525; P:positive regulation of T cell costimulation; IMP:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IC:BHF-UCL.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IC:BHF-UCL.
DR GO; GO:2000412; P:positive regulation of thymocyte migration; TAS:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IC:BHF-UCL.
DR GO; GO:2000547; P:regulation of dendritic cell dendrite assembly; IC:BHF-UCL.
DR GO; GO:0032649; P:regulation of interferon-gamma production; IMP:BHF-UCL.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:BHF-UCL.
DR GO; GO:0002649; P:regulation of tolerance induction to self antigen; TAS:BHF-UCL.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:BHF-UCL.
DR GO; GO:0071731; P:response to nitric oxide; TAS:BHF-UCL.
DR GO; GO:0034695; P:response to prostaglandin E; TAS: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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW 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_0000012736"
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 CONFLICT 164
FT /note="A -> R (in Ref. 1; AAA74232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42856 MW; F027451989B59683 CRC64;
MDPGKPRKNV LVVALLVIFQ VCFCQDEVTD DYIGENTTVD YTLYESVCFK KDVRNFKAWF
LPLMYSVICF VGLLGNGLVI LTYIYFKRLK TMTDTYLLNL AVADILFLLI LPFWAYSEAK
SWIFGVYLCK GIFGIYKLSF FSGMLLLLCI SIDRYVAIVQ AVSAHRHRAR VLLISKLSCV
GIWMLALFLS IPELLYSGLQ KNSGEDTLRC SLVSAQVEAL ITIQVAQMVF GFLVPMLAMS
FCYLIIIRTL LQARNFERNK AIKVIIAVVV VFIVFQLPYN GVVLAQTVAN FNITNSSCET
SKQLNIAYDV TYSLASVRCC VNPFLYAFIG VKFRSDLFKL FKDLGCLSQE RLRHWSSCRH
VRNASVSMEA ETTTTFSP
