Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

C-C motif chemokine 5 (EoCP) (Eosinophil chemotactic cytokine) (SIS-delta) (Small-inducible cytokine A5) (T cell-specific protein P228) (TCP228) (T-cell-specific protein RANTES) [Cleaved into: RANTES(3-68); RANTES(4-68)]

 CCL5_HUMAN              Reviewed;          91 AA.
P13501; O43646; Q0QVW8; Q4ZGJ1; Q9NYA2; Q9UBG2; Q9UC99;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 3.
25-OCT-2017, entry version 189.
RecName: Full=C-C motif chemokine 5;
AltName: Full=EoCP;
AltName: Full=Eosinophil chemotactic cytokine;
AltName: Full=SIS-delta;
AltName: Full=Small-inducible cytokine A5;
AltName: Full=T cell-specific protein P228;
Short=TCP228;
AltName: Full=T-cell-specific protein RANTES;
Contains:
RecName: Full=RANTES(3-68);
Contains:
RecName: Full=RANTES(4-68);
Flags: Precursor;
Name=CCL5; Synonyms=D17S136E, SCYA5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=2456327;
Schall T.J., Jongstra J., Dyer B.J., Jorgensen J., Clayberger C.,
Davis M.M., Krensky A.M.;
"A human T cell-specific molecule is a member of a new gene family.";
J. Immunol. 141:1018-1025(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10213461; DOI=10.1089/107999099314153;
Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.;
"Organization of the chemokine gene cluster on human chromosome
17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and
RANTES.";
J. Interferon Cytokine Res. 19:227-234(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT PHE-24, AND
CHARACTERIZATION OF VARIANT PHE-24.
TISSUE=Blood;
PubMed=16791620; DOI=10.1007/s00251-006-0133-2;
Capoulade-Metay C., Ayouba A., Kfutwah A., Lole K., Petres S.,
Dudoit Y., Deterre P., Menu E., Barre-Sinoussi F., Debre P.,
Theodorou I.;
"A natural CCL5/RANTES variant antagonist for CCR1 and CCR3.";
Immunogenetics 58:533-541(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukocyte;
Jang J.S., Kim B.E.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Zeng Q.P., Yang R.Y., Fu L.C.;
"The complete sequence of human beta-chemokine RANTES mRNA.";
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 24-55, FUNCTION, MASS SPECTROMETRY, GLYCOSYLATION
AT SER-27 AND SER-28, AND OXIDATION AT MET-90.
PubMed=1380064; DOI=10.1084/jem.176.2.587;
Kameyoshi Y., Doerschner A., Mallet A.I., Christophers E.,
Schroeder J.-M.;
"Cytokine RANTES released by thrombin-stimulated platelets is a potent
attractant for human eosinophils.";
J. Exp. Med. 176:587-592(1992).
[9]
PROTEIN SEQUENCE OF 24-55.
PubMed=7524281;
Schroeder J.-M., Kameyoshi Y., Christophers E.;
"Platelets secrete an eosinophil-chemotactic cytokine which is a
member of the C-C-chemokine family.";
Adv. Exp. Med. Biol. 351:119-128(1993).
[10]
PROTEIN SEQUENCE OF 49-56; 71-79 AND 83-91, AND FUNCTION.
PubMed=8525373; DOI=10.1126/science.270.5243.1811;
Cocchi F., DeVico A.L., Garzino-Demo A., Arya S.K., Gallo R.C.,
Lusso P.;
"Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major
HIV-suppressive factors produced by CD8+ T cells.";
Science 270:1811-1815(1995).
[11]
IDENTIFICATION OF RANTES(3-68), PROTEOLYTIC PROCESSING OF N-TERMINUS,
AND FUNCTION.
PubMed=9516414; DOI=10.1074/jbc.273.13.7222;
Proost P., De Meester I., Schols D., Struyf S., Lambeir A.-M.,
Wuyts A., Opdenakker G., De Clercq E., Scharpe S., Van Damme J.;
"Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase
IV. Conversion of RANTES into a potent inhibitor of monocyte
chemotaxis and HIV-1-infection.";
J. Biol. Chem. 273:7222-7227(1998).
[12]
IDENTIFICATION OF RANTES(4-68), MASS SPECTROMETRY, AND FUNCTION.
PubMed=15923218; DOI=10.1189/jlb.0305161;
Lim J.K., Burns J.M., Lu W., DeVico A.L.;
"Multiple pathways of amino terminal processing produce two truncated
variants of RANTES/CCL5.";
J. Leukoc. Biol. 78:442-452(2005).
[13]
FUNCTION.
PubMed=17001303; DOI=10.1038/sj.bjp.0706909;
Ignatov A., Robert J., Gregory-Evans C., Schaller H.C.;
"RANTES stimulates Ca2+ mobilization and inositol trisphosphate (IP3)
formation in cells transfected with G protein-coupled receptor 75.";
Br. J. Pharmacol. 149:490-497(2006).
[14]
FUNCTION.
PubMed=23979485; DOI=10.1007/s00125-013-3022-x;
Liu B., Hassan Z., Amisten S., King A.J., Bowe J.E., Huang G.C.,
Jones P.M., Persaud S.J.;
"The novel chemokine receptor, G-protein-coupled receptor 75, is
expressed by islets and is coupled to stimulation of insulin secretion
and improved glucose homeostasis.";
Diabetologia 56:2467-2476(2013).
[15]
TISSUE SPECIFICITY.
PubMed=23765988; DOI=10.1002/jcp.24418;
Caballero-Campo P., Buffone M.G., Benencia F., Conejo-Garcia J.R.,
Rinaudo P.F., Gerton G.L.;
"A role for the chemokine receptor CCR6 in mammalian sperm motility
and chemotaxis.";
J. Cell. Physiol. 229:68-78(2014).
[16]
STRUCTURE BY NMR.
PubMed=7537088; DOI=10.1021/bi00016a004;
Skelton N.J., Aspiras F., Ogez J., Schall T.J.;
"Proton NMR assignments and solution conformation of RANTES, a
chemokine of the C-C type.";
Biochemistry 34:5329-5342(1995).
[17]
STRUCTURE BY NMR.
PubMed=7542919; DOI=10.1021/bi00029a005;
Chung C.-W., Cooke R.M., Proudfoot A.E.I., Wells T.N.C.;
"The three-dimensional solution structure of RANTES.";
Biochemistry 34:9307-9314(1995).
[18]
SYNTHESIS, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=9889151; DOI=10.1016/S1074-5521(99)80019-2;
Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H.,
Picard L., Wlodawer A., Lubkowski J., Kent S.B.;
"Total chemical synthesis and high-resolution crystal structure of the
potent anti-HIV protein AOP-RANTES.";
Chem. Biol. 6:43-51(1999).
[19]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Hoover D.M., Shaw J., Gryczynski Z., Proudfoot A.E.I., Wells T.N.C.,
Lubkowski J.;
"The crystal structure of Met-RANTES: comparison with native RANTES
and AOP-RANTES.";
Protein Pept. Lett. 7:73-82(2000).
-!- FUNCTION: Chemoattractant for blood monocytes, memory T-helper
cells and eosinophils. Causes the release of histamine from
basophils and activates eosinophils. May activate several
chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of
the major HIV-suppressive factors produced by CD8+ T-cells.
Recombinant RANTES protein induces a dose-dependent inhibition of
different strains of HIV-1, HIV-2, and simian immunodeficiency
virus (SIV). The processed form RANTES(3-68) acts as a natural
chemotaxis inhibitor and is a more potent inhibitor of HIV-1-
infection. The second processed form RANTES(4-68) exhibits reduced
chemotactic and HIV-suppressive activity compared with RANTES(1-
68) and RANTES(3-68) and is generated by an unidentified enzyme
associated with monocytes and neutrophils (PubMed:16791620,
PubMed:1380064, PubMed:8525373, PubMed:9516414, PubMed:15923218).
May also be an agonist of the G protein-coupled receptor GPR75,
stimulating inositol trisphosphate production and calcium
mobilization through its activation. Together with GPR75, may play
a role in neuron survival through activation of a downstream
signaling pathway involving the PI3, Akt and MAP kinases. By
activating GPR75 may also play a role in insulin secretion by
islet cells (PubMed:23979485). {ECO:0000269|PubMed:1380064,
ECO:0000269|PubMed:15923218, ECO:0000269|PubMed:16791620,
ECO:0000269|PubMed:17001303, ECO:0000269|PubMed:23979485,
ECO:0000269|PubMed:8525373, ECO:0000269|PubMed:9516414}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-2848366, EBI-2848366;
P51681:CCR5; NbExp=4; IntAct=EBI-2848366, EBI-489374;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in the follicular fluid (at protein
level). T-cell and macrophage specific.
{ECO:0000269|PubMed:23765988, ECO:0000269|PubMed:2456327}.
-!- INDUCTION: By mitogens.
-!- PTM: N-terminal processed form RANTES(3-68) is produced by
proteolytic cleavage, probably by DPP4, after secretion from
peripheral blood leukocytes and cultured sarcoma cells.
{ECO:0000269|PubMed:9516414}.
-!- PTM: The identity of the O-linked saccharides at Ser-27 and Ser-28
are not reported in PubMed:1380064. They are assigned by
similarity. {ECO:0000269|PubMed:1380064}.
-!- MASS SPECTROMETRY: Mass=7515; Mass_error=1; Method=SELDI;
Range=27-91; Evidence={ECO:0000269|PubMed:15923218};
-!- MASS SPECTROMETRY: Mass=7862.8; Mass_error=1.1;
Method=Electrospray; Range=24-91;
Evidence={ECO:0000269|PubMed:1380064};
-!- MASS SPECTROMETRY: Mass=8355; Mass_error=10; Method=Electrospray;
Range=24-91; Note=O-glycosylated.;
Evidence={ECO:0000269|PubMed:1380064};
-!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ccl5/";
-!- WEB RESOURCE: Name=Wikipedia; Note=RANTES entry;
URL="https://en.wikipedia.org/wiki/RANTES";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M21121; AAA36725.1; -; mRNA.
EMBL; AF088219; AAC63331.1; -; Genomic_DNA.
EMBL; DQ230537; ABB69929.1; -; mRNA.
EMBL; AF043341; AAC03541.1; -; mRNA.
EMBL; AF266753; AAF73070.1; -; mRNA.
EMBL; DQ017060; AAY22177.1; -; Genomic_DNA.
EMBL; BC008600; AAH08600.1; -; mRNA.
CCDS; CCDS11300.1; -.
PIR; A28815; A28815.
RefSeq; NP_002976.2; NM_002985.2.
UniGene; Hs.514821; -.
PDB; 1B3A; X-ray; 1.60 A; A/B=25-91.
PDB; 1EQT; X-ray; 1.60 A; A/B=26-91.
PDB; 1HRJ; NMR; -; A/B=24-91.
PDB; 1RTN; NMR; -; A/B=24-91.
PDB; 1RTO; NMR; -; A/B=24-91.
PDB; 1U4L; X-ray; 2.00 A; A/B=24-91.
PDB; 1U4M; X-ray; 2.00 A; A/B=24-91.
PDB; 1U4P; X-ray; 1.70 A; A/B=24-91.
PDB; 1U4R; X-ray; 2.20 A; A/B/C/D=24-91.
PDB; 2L9H; Other; -; A/B/C/D=24-91.
PDB; 2VXW; X-ray; 1.70 A; A/B/C/D=33-91.
PDB; 5CMD; X-ray; 3.09 A; A/B/C/D/E/F=27-91.
PDB; 5COY; X-ray; 1.44 A; A/B=27-91.
PDB; 5DNF; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I=27-91.
PDB; 5L2U; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I=27-91.
PDB; 5UIW; X-ray; 2.20 A; B=33-91.
PDBsum; 1B3A; -.
PDBsum; 1EQT; -.
PDBsum; 1HRJ; -.
PDBsum; 1RTN; -.
PDBsum; 1RTO; -.
PDBsum; 1U4L; -.
PDBsum; 1U4M; -.
PDBsum; 1U4P; -.
PDBsum; 1U4R; -.
PDBsum; 2L9H; -.
PDBsum; 2VXW; -.
PDBsum; 5CMD; -.
PDBsum; 5COY; -.
PDBsum; 5DNF; -.
PDBsum; 5L2U; -.
PDBsum; 5UIW; -.
ProteinModelPortal; P13501; -.
SMR; P13501; -.
BioGrid; 112255; 35.
DIP; DIP-31N; -.
IntAct; P13501; 26.
MINT; MINT-103226; -.
STRING; 9606.ENSP00000293272; -.
BindingDB; P13501; -.
ChEMBL; CHEMBL1275217; -.
DrugBank; DB02322; Heparin Disaccharide I-S.
DrugBank; DB02353; Heparin Disaccharide Iii-S.
iPTMnet; P13501; -.
PhosphoSitePlus; P13501; -.
BioMuta; CCL5; -.
DMDM; 6175077; -.
EPD; P13501; -.
PaxDb; P13501; -.
PeptideAtlas; P13501; -.
PRIDE; P13501; -.
TopDownProteomics; P13501; -.
DNASU; 6352; -.
Ensembl; ENST00000603197; ENSP00000474412; ENSG00000271503.
Ensembl; ENST00000605140; ENSP00000475057; ENSG00000271503.
Ensembl; ENST00000613606; ENSP00000479894; ENSG00000274233.
Ensembl; ENST00000618639; ENSP00000484921; ENSG00000274233.
GeneID; 6352; -.
KEGG; hsa:6352; -.
UCSC; uc002hkf.5; human.
CTD; 6352; -.
DisGeNET; 6352; -.
EuPathDB; HostDB:ENSG00000271503.5; -.
GeneCards; CCL5; -.
HGNC; HGNC:10632; CCL5.
MIM; 187011; gene.
neXtProt; NX_P13501; -.
OpenTargets; ENSG00000271503; -.
PharmGKB; PA35564; -.
eggNOG; ENOG410J0XH; Eukaryota.
eggNOG; ENOG410ZUYI; LUCA.
GeneTree; ENSGT00900000140870; -.
HOVERGEN; HBG017871; -.
InParanoid; P13501; -.
KO; K12499; -.
PhylomeDB; P13501; -.
TreeFam; TF334888; -.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
SIGNOR; P13501; -.
EvolutionaryTrace; P13501; -.
GeneWiki; CCL5; -.
GenomeRNAi; 6352; -.
PMAP-CutDB; P13501; -.
PRO; PR:P13501; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000271503; -.
CleanEx; HS_CCL5; -.
ExpressionAtlas; P13501; baseline and differential.
Genevisible; P13501; HS.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0031726; F:CCR1 chemokine receptor binding; IDA:BHF-UCL.
GO; GO:0031729; F:CCR4 chemokine receptor binding; TAS:BHF-UCL.
GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:BHF-UCL.
GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
GO; GO:0008009; F:chemokine activity; IDA:BHF-UCL.
GO; GO:0046817; F:chemokine receptor antagonist activity; IDA:BHF-UCL.
GO; GO:0042379; F:chemokine receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
GO; GO:0016004; F:phospholipase activator activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:BHF-UCL.
GO; GO:0030298; F:receptor signaling protein tyrosine kinase activator activity; IDA:BHF-UCL.
GO; GO:0031584; P:activation of phospholipase D activity; IDA:BHF-UCL.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
GO; GO:0043623; P:cellular protein complex assembly; IDA:BHF-UCL.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; NAS:UniProtKB.
GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL.
GO; GO:0048245; P:eosinophil chemotaxis; IDA:BHF-UCL.
GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0048246; P:macrophage chemotaxis; TAS:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0002548; P:monocyte chemotaxis; IC:UniProtKB.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IEA:Ensembl.
GO; GO:0070233; P:negative regulation of T cell apoptotic process; IDA:BHF-UCL.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:0042119; P:neutrophil activation; IDA:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; TAS:BHF-UCL.
GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IDA:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0045089; P:positive regulation of innate immune response; TAS:BHF-UCL.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; TAS:BHF-UCL.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IDA:BHF-UCL.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:BHF-UCL.
GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0070234; P:positive regulation of T cell apoptotic process; IDA:BHF-UCL.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:BHF-UCL.
GO; GO:2000406; P:positive regulation of T cell migration; IDA:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0045948; P:positive regulation of translational initiation; NAS:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0045070; P:positive regulation of viral genome replication; TAS:BHF-UCL.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IDA:BHF-UCL.
GO; GO:0002676; P:regulation of chronic inflammatory response; TAS:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; IDA:UniProtKB.
GO; GO:0050863; P:regulation of T cell activation; IDA:BHF-UCL.
GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; TAS:BHF-UCL.
InterPro; IPR030595; CCL5.
InterPro; IPR000827; Chemokine_CC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR036048; Interleukin_8-like_sf.
PANTHER; PTHR12015:SF82; PTHR12015:SF82; 1.
Pfam; PF00048; IL8; 1.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
1: Evidence at protein level;
3D-structure; Chemotaxis; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Inflammatory response; Oxidation; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:1380064,
ECO:0000269|PubMed:7524281}.
CHAIN 24 91 C-C motif chemokine 5.
/FTId=PRO_0000005175.
CHAIN 26 91 RANTES(3-68).
/FTId=PRO_0000005176.
CHAIN 27 91 RANTES(4-68).
/FTId=PRO_0000005177.
SITE 25 26 Cleavage; by DPP4.
MOD_RES 90 90 Methionine sulfoxide.
{ECO:0000269|PubMed:1380064}.
CARBOHYD 27 27 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:1380064}.
CARBOHYD 28 28 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:1380064}.
DISULFID 33 57
DISULFID 34 73
VARIANT 24 24 S -> F (polymorphism; antagonist of the
chemokine receptors CCR1 and CCR3;
dbSNP:rs377415776).
{ECO:0000269|PubMed:16791620}.
/FTId=VAR_043043.
CONFLICT 7 7 A -> R (in Ref. 1; AAA36725 and 5;
AAF73070). {ECO:0000305}.
CONFLICT 14 14 A -> V (in Ref. 5; AAF73070).
{ECO:0000305}.
STRAND 31 33 {ECO:0000244|PDB:5COY}.
STRAND 35 40 {ECO:0000244|PDB:2VXW}.
HELIX 44 46 {ECO:0000244|PDB:5COY}.
STRAND 47 52 {ECO:0000244|PDB:5COY}.
STRAND 57 59 {ECO:0000244|PDB:5COY}.
STRAND 62 66 {ECO:0000244|PDB:5COY}.
STRAND 71 74 {ECO:0000244|PDB:5COY}.
HELIX 79 88 {ECO:0000244|PDB:5COY}.
SEQUENCE 91 AA; 9990 MW; FB0BFAF9A87C620F CRC64;
MKVSAAALAV ILIATALCAP ASASPYSSDT TPCCFAYIAR PLPRAHIKEY FYTSGKCSNP
AVVFVTRKNR QVCANPEKKW VREYINSLEM S


Related products :

Catalog number Product name Quantity
U0116h CLIA C-C motif chemokine 5,CCL5,D17S136E,EoCP,Eosinophil chemotactic cytokine,Homo sapiens,Human,SCYA5,SIS-delta,Small-inducible cytokine A5,T cell-specific protein P228,T-cell-specific protein RANTES 96T
18-783-76227 RABBIT ANTI HUMAN RANTES - CCL5; Small-inducible cytokine A5; T-cell-specific protein RANTES; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.1 mg
18-783-78913 RABBIT ANTI HUMAN RANTES Biotin - CCL5; Small-inducible cytokine A5; T-cell-specific protein RANTES; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.05 mg
E0116h ELISA kit C-C motif chemokine 5,CCL5,D17S136E,EoCP,Eosinophil chemotactic cytokine,Homo sapiens,Human,SCYA5,SIS-delta,Small-inducible cytokine A5,T cell-specific protein P228,T-cell-specific protein 96T
E0116h ELISA C-C motif chemokine 5,CCL5,D17S136E,EoCP,Eosinophil chemotactic cytokine,Homo sapiens,Human,SCYA5,SIS-delta,Small-inducible cytokine A5,T cell-specific protein P228,T-cell-specific protein RANTE 96T
15-288-21036 Small inducible cytokine A5 - CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.1 mg
15-288-21036 Small inducible cytokine A5 - CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.05 mg
E0116p ELISA kit C-C motif chemokine 5,CCL5,Pig,SCYA5,SIS-delta,Small-inducible cytokine A5,Sus scrofa,T-cell-specific protein RANTES 96T
U0116p CLIA C-C motif chemokine 5,CCL5,Pig,SCYA5,SIS-delta,Small-inducible cytokine A5,Sus scrofa,T-cell-specific protein RANTES 96T
E0116p ELISA C-C motif chemokine 5,CCL5,Pig,SCYA5,SIS-delta,Small-inducible cytokine A5,Sus scrofa,T-cell-specific protein RANTES 96T
18-272-195148 RANTES - Goat polyclonal to RANTES; CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.025 mg
E0116b ELISA Bos taurus,Bovine,C-C motif chemokine 5,CCL5,SCYA5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
E0116b ELISA kit Bos taurus,Bovine,C-C motif chemokine 5,CCL5,SCYA5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
E0116r ELISA kit C-C motif chemokine 5,Ccl5,Rat,Rattus norvegicus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
U0116b CLIA Bos taurus,Bovine,C-C motif chemokine 5,CCL5,SCYA5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
U0116r CLIA C-C motif chemokine 5,Ccl5,Rat,Rattus norvegicus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
E0116r ELISA C-C motif chemokine 5,Ccl5,Rat,Rattus norvegicus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
E0116m ELISA C-C motif chemokine 5,Ccl5,Mouse,MuRantes,Mus musculus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
U0116m CLIA C-C motif chemokine 5,Ccl5,Mouse,MuRantes,Mus musculus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
E0116m ELISA kit C-C motif chemokine 5,Ccl5,Mouse,MuRantes,Mus musculus,Scya5,SIS-delta,Small-inducible cytokine A5,T-cell-specific protein RANTES 96T
18-272-195808 RANTES ( Biotin ) - Rabbit polyclonal to RANTES ( Biotin ); CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 Polyclonal 0.025 mg
20-272-190532 RANTES (FITC) - Mouse monoclonal [VL1] to RANTES (FITC); CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 Monoclonal 0.05 mg
10-663-45034 Rantes (CCL5) Human - CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 N_A 0.005 mg
10-663-45034 Rantes (CCL5) Human - CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 N_A 0.02 mg
10-663-45034 Rantes (CCL5) Human - CCL5; T-cell-specific RANTES protein; SIS-delta; T cell-specific protein P228; TCP228 N_A 1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur