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P51677 (CCR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-C chemokine receptor type 3

Short name=C-C CKR-3
Short name=CC-CKR-3
Short name=CCR-3
Short name=CCR3
Short name=CKR3
Alternative name(s):
Eosinophil eotaxin receptor
CD_antigen=CD193
Gene names
Name:CCR3
Synonyms:CMKBR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for a C-C type chemokine. Binds to eotaxin, eotaxin-3, MCP-3, MCP-4, RANTES and MIP-1 delta. Subsequently transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection.

Subunit structure

Binds to HIV-1 Tat. Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

In eosinophils as well as trace amounts in neutrophils and monocytes.

Miscellaneous

Overexpression of CCR3 together with its ligands appears to be a characteristic of ulcerative colitis (UC). The production of CCR3 ligands by human colonic epithelial cells suggests further that the epithelium can play a role in modulating pathological T-cell-mediated mucosal inflammation (Ref.13).

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355C-C chemokine receptor type 3
PRO_0000069239

Regions

Topological domain1 – 3434Extracellular Potential
Transmembrane35 – 6228Helical; Name=1; Potential
Topological domain63 – 7210Cytoplasmic Potential
Transmembrane73 – 9321Helical; Name=2; Potential
Topological domain94 – 10714Extracellular Potential
Transmembrane108 – 12922Helical; Name=3; Potential
Topological domain130 – 14617Cytoplasmic Potential
Transmembrane147 – 17125Helical; Name=4; Potential
Topological domain172 – 20332Extracellular Potential
Transmembrane204 – 22320Helical; Name=5; Potential
Topological domain224 – 23916Cytoplasmic Potential
Transmembrane240 – 26425Helical; Name=6; Potential
Topological domain265 – 28117Extracellular Potential
Transmembrane282 – 30524Helical; Name=7; Potential
Topological domain306 – 35550Cytoplasmic Potential

Amino acid modifications

Disulfide bond106 ↔ 183 By similarity

Natural variations

Natural variant211G → D.
Corresponds to variant rs4987125 [ dbSNP | Ensembl ].
VAR_020067
Natural variant391P → L.
Corresponds to variant rs5742906 [ dbSNP | Ensembl ].
VAR_049382
Natural variant2181C → S Polymorphism found in about 7% of the population; may show reduced activity. Ref.6
VAR_010668

Experimental info

Sequence conflict2051I → V in BAG53863. Ref.10
Sequence conflict2761S → T in AAB09726. Ref.4
Sequence conflict2761S → T in BAA86964. Ref.6
Sequence conflict2771K → R in BAG53863. Ref.10
Sequence conflict3491P → R in BAG53863. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P51677 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E95DCD7A6C643874

FASTA35541,044
        10         20         30         40         50         60 
MTTSLDTVET FGTTSYYDDV GLLCEKADTR ALMAQFVPPL YSLVFTVGLL GNVVVVMILI 

        70         80         90        100        110        120 
KYRRLRIMTN IYLLNLAISD LLFLVTLPFW IHYVRGHNWV FGHGMCKLLS GFYHTGLYSE 

       130        140        150        160        170        180 
IFFIILLTID RYLAIVHAVF ALRARTVTFG VITSIVTWGL AVLAALPEFI FYETEELFEE 

       190        200        210        220        230        240 
TLCSALYPED TVYSWRHFHT LRMTIFCLVL PLLVMAICYT GIIKTLLRCP SKKKYKAIRL 

       250        260        270        280        290        300 
IFVIMAVFFI FWTPYNVAIL LSSYQSILFG NDCERSKHLD LVMLVTEVIA YSHCCMNPVI 

       310        320        330        340        350 
YAFVGERFRK YLRHFFHRHL LMHLGRYIPF LPSEKLERTS SVSPSTAEPE LSIVF 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional expression of a human eosinophil CC chemokine receptor."
Combadiere C., Ahuja S.K., Murphy P.M.
J. Biol. Chem. 270:16491-16494(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Monocyte.
[2]Erratum
Combadiere C., Ahuja S.K., Murphy P.M.
J. Biol. Chem. 270:30235-30235(1995)
[3]"Cloning, expression, and characterization of the human eosinophil eotaxin receptor."
Daugherty B.L., Siciliano S.J., Demartino J.A., Malkowitz L., Sirotina A., Springer M.S.
J. Exp. Med. 183:2349-2354(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Molecular cloning and characterization of a human eotaxin receptor expressed selectively on eosinophils."
Ponath P.D., Qin S., Post T.W., Wang J., Wu L., Gerard N.P., Newman W., Gerard C., Mackay C.R.
J. Exp. Med. 183:2437-2448(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Partial resistance to infection by syncytium-inducing primary HIV-1 in exposed uninfected individuals homozygous for CCR5 32bp deletion."
Xiao L., Weiss S., Qari S., Rudolph D., Hodge T., Lal R.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"New variations of human CC-chemokine receptors CCR3 and CCR4."
Kato H., Tsuchiya N., Izumi S., Miyamasu M., Nakajima T., Kawasaki H., Hirai K., Tokunaga K.
Genes Immun. 1:97-104(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-218.
[7]"Transcription regulation of human chemokine receptor CCR3: evidence for a rare TATA-less promoter structure conserved between Drosophila and humans."
Vijh S., Dayhoff D.E., Wang C.E., Imam Z., Ehrenberg P.K., Michael N.L.
Genomics 80:86-95(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Synovium.
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[12]"HIV-1 Tat protein mimicry of chemokines."
Albini A., Ferrini S., Benelli R., Sforzini S., Giunciuglio D., Aluigi M.G., Proudfoot A.E.I., Alouani S., Wells T.N.C., Mariani G., Rabin R.L., Farber J.M., Noonan D.M.
Proc. Natl. Acad. Sci. U.S.A. 95:13153-13158(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[13]"Increased expression of chemokine receptor CCR3 and its ligands in ulcerative colitis: the role of colonic epithelial cells in in vitro studies."
Manousou P., Kolios G., Valatas V., Drygiannakis I., Bourikas L., Pyrovolaki K., Koutroubakis I., Papadaki H.A., Kouroumalis E.
Clin. Exp. Immunol. 162:337-347(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEREXPRESSION.
+Additional computationally mapped references.

Web resources

Wikipedia

CC chemokine receptors entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28694 mRNA. Translation: AAC50469.1.
U51241 Genomic DNA. Translation: AAB16831.1.
U49727 Genomic DNA. Translation: AAB09726.1.
AF026535 mRNA. Translation: AAB82589.1.
AB023887 Genomic DNA. Translation: BAA86964.1.
AF247361 Genomic DNA. Translation: AAL85154.1.
AY221092 Genomic DNA. Translation: AAO65970.2.
EF064760 Genomic DNA. Translation: ABK41943.1.
AK123050 mRNA. Translation: BAG53863.1.
BC110297 mRNA. Translation: AAI10298.1.
BC130318 mRNA. Translation: AAI30319.1.
BC130320 mRNA. Translation: AAI30321.1.
IPIIPI00019957.
PIRG02436.
RefSeqNP_001828.1. NM_001837.3.
NP_847899.1. NM_178329.2.
UniGeneHs.506190.

3D structure databases

ProteinModelPortalP51677.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5846N.
MINTMINT-105239.
STRING9606.ENSP00000350003.

Protein family/group databases

GPCRDBSearch...

Polymorphism databases

DMDM1705892.

Proteomic databases

PaxDbP51677.
PRIDEP51677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357422; ENSP00000350003; ENSG00000183625.
ENST00000395940; ENSP00000379271; ENSG00000183625.
ENST00000395942; ENSP00000379273; ENSG00000183625.
ENST00000541018; ENSP00000440097; ENSG00000183625.
GeneID1232.
KEGGhsa:1232.
UCSCuc003cpg.2. human.

Organism-specific databases

CTD1232.
GeneCardsGC03P046227.
HGNCHGNC:1604. CCR3.
HPACAB003795.
MIM601268. gene.
neXtProtNX_P51677.
PharmGKBPA26168.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148353.
HOGENOMHOG000234122.
HOVERGENHBG106917.
InParanoidP51677.
KOK04178.
OrthoDBEOG4S1T7D.
PhylomeDBP51677.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP51677.
BgeeP51677.
CleanExHS_CCR3.
GenevestigatorP51677.
GermOnlineENSG00000183625. Homo sapiens.

Family and domain databases

InterProIPR002238. Chemokine_CCR3.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF13. PTHR24227:SF13. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00657. CCCHEMOKINER.
PR01108. CHEMOKINER3.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP51677.
ChEMBLCHEMBL3473.
GenomeRNAi1232.
NextBio5025.
SOURCESearch...

Entry information

Entry nameCCR3_HUMAN
AccessionPrimary (citable) accession number: P51677
Secondary accession number(s): B3KVQ1 expand/collapse secondary AC list , Q15748, Q2YDB9, Q86WD2, Q9ULY8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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SIMILARITY comments

Index of protein domains and families