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P47774 (CCR7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-C chemokine receptor type 7

Short name=C-C CKR-7
Short name=CC-CKR-7
Short name=CCR-7
Alternative name(s):
Epstein-Barr virus-induced G-protein coupled receptor 1
Short name=EBI1
Short name=EBV-induced G-protein coupled receptor 1
MIP-3 beta receptor
CD_antigen=CD197
Gene names
Name:Ccr7
Synonyms:Cmkbr7, Ebi1, Ebi1h
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the MIP-3-beta chemokine By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement PubMed 16621978. Source: BHF-UCL

activation of JUN kinase activity

Inferred by curator PubMed 16027136. Source: BHF-UCL

chemotaxis

Inferred from mutant phenotype PubMed 10520991. Source: MGI

establishment of T cell polarity

Traceable author statement PubMed 16621978. Source: BHF-UCL

immune response

Inferred from mutant phenotype PubMed 10520991. Source: MGI

inflammatory response

Non-traceable author statement PubMed 20638137. Source: BHF-UCL

interleukin-12 secretion

Inferred from mutant phenotype PubMed 20176793. Source: BHF-UCL

lymph node development

Traceable author statement PubMed 12732660. Source: BHF-UCL

lymphocyte chemotaxis across high endothelial venule

Traceable author statement PubMed 21051556. Source: BHF-UCL

lymphocyte migration into lymph node

Traceable author statement PubMed 18379575. Source: BHF-UCL

mature dendritic cell differentiation

Inferred from mutant phenotype PubMed 15845453. Source: BHF-UCL

negative regulation of leukocyte apoptotic process

Traceable author statement PubMed 16621978. Source: BHF-UCL

negative thymic T cell selection

Inferred from mutant phenotype PubMed 17785582. Source: BHF-UCL

positive regulation of Cdc42 GTPase activity

Inferred by curator PubMed 12609829. Source: BHF-UCL

positive regulation of Ras GTPase activity

Inferred by curator PubMed 12609829. Source: BHF-UCL

positive regulation of T cell chemotaxis

Traceable author statement PubMed 21051556. Source: BHF-UCL

positive regulation of T cell costimulation

Inferred from mutant phenotype PubMed 15845453. Source: BHF-UCL

positive regulation of T cell proliferation

Inferred by curator PubMed 15845453. Source: BHF-UCL

positive regulation of T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 17785582. Source: BHF-UCL

positive regulation of T-helper 1 cell differentiation

Inferred by curator PubMed 15845453. Source: BHF-UCL

positive regulation of cell motility

Traceable author statement PubMed 16621978. Source: BHF-UCL

positive regulation of dendritic cell antigen processing and presentation

Inferred from direct assay PubMed 15845453. Source: BHF-UCL

positive regulation of dendritic cell chemotaxis

Inferred from mutant phenotype PubMed 10520991. Source: BHF-UCL

positive regulation of filopodium assembly

Traceable author statement PubMed 16621978. Source: BHF-UCL

positive regulation of glycoprotein biosynthetic process involved in immunological synapse formation

Inferred from mutant phenotype PubMed 15845453. Source: BHF-UCL

positive regulation of humoral immune response

Inferred from mutant phenotype PubMed 10520991. Source: BHF-UCL

positive regulation of hypersensitivity

Inferred from mutant phenotype PubMed 10520991. Source: BHF-UCL

positive regulation of immunological synapse formation

Inferred from mutant phenotype PubMed 15845453. Source: BHF-UCL

positive regulation of interleukin-1 beta secretion

Inferred by curator PubMed 15845453. Source: BHF-UCL

positive regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 15845453. Source: BHF-UCL

positive regulation of macrophage chemotaxis

Non-traceable author statement PubMed 20605225. Source: BHF-UCL

positive regulation of neutrophil chemotaxis

Inferred from mutant phenotype PubMed 21051556. Source: BHF-UCL

positive regulation of phagocytosis

Non-traceable author statement PubMed 15965301. Source: BHF-UCL

positive regulation of receptor-mediated endocytosis

Inferred by curator PubMed 12609829. Source: BHF-UCL

positive regulation of thymocyte migration

Traceable author statement PubMed 11700037. Source: BHF-UCL

positive regulation of tumor necrosis factor production

Inferred by curator PubMed 15845453. Source: BHF-UCL

regulation of dendritic cell dendrite assembly

Inferred by curator PubMed 12200351. Source: BHF-UCL

regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 20176793. Source: BHF-UCL

regulation of interleukin-1 beta secretion

Inferred from mutant phenotype PubMed 20176793. Source: BHF-UCL

regulation of tolerance induction to self antigen

Traceable author statement PubMed 17785582. Source: BHF-UCL

response to lipopolysaccharide

Inferred from direct assay PubMed 20638137. Source: BHF-UCL

response to nitric oxide

Traceable author statement PubMed 16621978. Source: BHF-UCL

response to prostaglandin E

Traceable author statement PubMed 16621978. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 23620790. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 19008373. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay PubMed 21051556. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 21051556. Source: BHF-UCL

   Molecular_functionC-C chemokine receptor activity

Inferred from mutant phenotype PubMed 10520991. Source: BHF-UCL

C-C motif chemokine 19 receptor activity

Inferred from electronic annotation. Source: Ensembl

C-C motif chemokine 21 receptor activity

Inferred from electronic annotation. Source: Ensembl

G-protein coupled receptor activity

Traceable author statement PubMed 16621978. Source: BHF-UCL

chemokine (C-C motif) ligand 19 binding

Inferred from sequence or structural similarity. Source: BHF-UCL

chemokine (C-C motif) ligand 21 binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 22922463. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CD247P209632EBI-8038963,EBI-1165705From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 378354C-C chemokine receptor type 7
PRO_0000012736

Regions

Topological domain25 – 5935Extracellular Potential
Transmembrane60 – 8627Helical; Name=1; Potential
Topological domain87 – 959Cytoplasmic Potential
Transmembrane96 – 11621Helical; Name=2; Potential
Topological domain117 – 13014Extracellular Potential
Transmembrane131 – 15222Helical; Name=3; Potential
Topological domain153 – 17018Cytoplasmic Potential
Transmembrane171 – 19121Helical; Name=4; Potential
Topological domain192 – 21928Extracellular Potential
Transmembrane220 – 24728Helical; Name=5; Potential
Topological domain248 – 26316Cytoplasmic Potential
Transmembrane264 – 28926Helical; Name=6; Potential
Topological domain290 – 31324Extracellular Potential
Transmembrane314 – 33118Helical; Name=7; Potential
Topological domain332 – 37847Cytoplasmic Potential

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Potential
Disulfide bond129 ↔ 210 By similarity

Experimental info

Sequence conflict1641A → R in AAA74232. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47774 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F027451989B59683

FASTA37842,856
        10         20         30         40         50         60 
MDPGKPRKNV LVVALLVIFQ VCFCQDEVTD DYIGENTTVD YTLYESVCFK KDVRNFKAWF 

        70         80         90        100        110        120 
LPLMYSVICF VGLLGNGLVI LTYIYFKRLK TMTDTYLLNL AVADILFLLI LPFWAYSEAK 

       130        140        150        160        170        180 
SWIFGVYLCK GIFGIYKLSF FSGMLLLLCI SIDRYVAIVQ AVSAHRHRAR VLLISKLSCV 

       190        200        210        220        230        240 
GIWMLALFLS IPELLYSGLQ KNSGEDTLRC SLVSAQVEAL ITIQVAQMVF GFLVPMLAMS 

       250        260        270        280        290        300 
FCYLIIIRTL LQARNFERNK AIKVIIAVVV VFIVFQLPYN GVVLAQTVAN FNITNSSCET 

       310        320        330        340        350        360 
SKQLNIAYDV TYSLASVRCC VNPFLYAFIG VKFRSDLFKL FKDLGCLSQE RLRHWSSCRH 

       370 
VRNASVSMEA ETTTTFSP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of human and mouse EBI1, a lymphoid-specific G-protein-coupled receptor encoded on human chromosome 17q12-q21.2."
Schweickart V.L., Raport C.J., Godiska R., Byers M.G., Eddy R.L. Jr., Shows T.B., Gray P.W.
Genomics 23:643-650(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Thymus.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L31580 mRNA. Translation: AAA74232.1.
AK037965 mRNA. Translation: BAC29909.1.
AK154349 mRNA. Translation: BAE32532.1.
AK154849 mRNA. Translation: BAE32875.1.
AL591366 Genomic DNA. Translation: CAM26977.1.
CH466556 Genomic DNA. Translation: EDL16180.1.
CCDSCCDS25373.1.
PIRA55735.
RefSeqNP_031745.2. NM_007719.2.
UniGeneMm.2932.

3D structure databases

ProteinModelPortalP47774.
SMRP47774. Positions 52-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP47774. 1 interaction.

Chemistry

GuidetoPHARMACOLOGY64.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP47774.

Proteomic databases

PRIDEP47774.

Protocols and materials databases

DNASU12775.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103134; ENSMUSP00000099423; ENSMUSG00000037944.
GeneID12775.
KEGGmmu:12775.
UCSCuc007lih.1. mouse.

Organism-specific databases

CTD1236.
MGIMGI:103011. Ccr7.

Phylogenomic databases

eggNOGNOG149643.
GeneTreeENSGT00730000110640.
HOGENOMHOG000234122.
HOVERGENHBG106917.
InParanoidQ8CAS2.
KOK04182.
OMACFKKDVR.
OrthoDBEOG79CXZN.
TreeFamTF330966.

Gene expression databases

BgeeP47774.
CleanExMM_CCR7.
GenevestigatorP47774.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001718. Chemokine_CCR7.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF29. PTHR24227:SF29. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00657. CCCHEMOKINER.
PR00641. CHEMOKINER7.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282162.
PROP47774.
SOURCESearch...

Entry information

Entry nameCCR7_MOUSE
AccessionPrimary (citable) accession number: P47774
Secondary accession number(s): Q8CAS2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries