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Database: UniProt
Entry: P13501
LinkDB: P13501
Original site: P13501 
ID   CCL5_HUMAN              Reviewed;          91 AA.
AC   P13501; O43646; Q0QVW8; Q4ZGJ1; Q9NYA2; Q9UBG2; Q9UC99;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   26-NOV-2014, entry version 166.
DE   RecName: Full=C-C motif chemokine 5;
DE   AltName: Full=EoCP;
DE   AltName: Full=Eosinophil chemotactic cytokine;
DE   AltName: Full=SIS-delta;
DE   AltName: Full=Small-inducible cytokine A5;
DE   AltName: Full=T cell-specific protein P228;
DE            Short=TCP228;
DE   AltName: Full=T-cell-specific protein RANTES;
DE   Contains:
DE     RecName: Full=RANTES(3-68);
DE   Contains:
DE     RecName: Full=RANTES(4-68);
DE   Flags: Precursor;
GN   Name=CCL5; Synonyms=D17S136E, SCYA5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2456327;
RA   Schall T.J., Jongstra J., Dyer B.J., Jorgensen J., Clayberger C.,
RA   Davis M.M., Krensky A.M.;
RT   "A human T cell-specific molecule is a member of a new gene family.";
RL   J. Immunol. 141:1018-1025(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10213461; DOI=10.1089/107999099314153;
RA   Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.;
RT   "Organization of the chemokine gene cluster on human chromosome
RT   17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and
RT   RANTES.";
RL   J. Interferon Cytokine Res. 19:227-234(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANT PHE-24.
RC   TISSUE=Blood;
RX   PubMed=16791620; DOI=10.1007/s00251-006-0133-2;
RA   Capoulade-Metay C., Ayouba A., Kfutwah A., Lole K., Petres S.,
RA   Dudoit Y., Deterre P., Menu E., Barre-Sinoussi F., Debre P.,
RA   Theodorou I.;
RT   "A natural CCL5/RANTES variant antagonist for CCR1 and CCR3.";
RL   Immunogenetics 58:533-541(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leukocyte;
RA   Jang J.S., Kim B.E.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zeng Q.P., Yang R.Y., Fu L.C.;
RT   "The complete sequence of human beta-chemokine RANTES mRNA.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 24-55, FUNCTION, MASS SPECTROMETRY, GLYCOSYLATION
RP   AT SER-27 AND SER-28, AND OXIDATION AT MET-90.
RX   PubMed=1380064; DOI=10.1084/jem.176.2.587;
RA   Kameyoshi Y., Doerschner A., Mallet A.I., Christophers E.,
RA   Schroeder J.-M.;
RT   "Cytokine RANTES released by thrombin-stimulated platelets is a potent
RT   attractant for human eosinophils.";
RL   J. Exp. Med. 176:587-592(1992).
RN   [9]
RP   PROTEIN SEQUENCE OF 24-55.
RX   PubMed=7524281;
RA   Schroeder J.-M., Kameyoshi Y., Christophers E.;
RT   "Platelets secrete an eosinophil-chemotactic cytokine which is a
RT   member of the C-C-chemokine family.";
RL   Adv. Exp. Med. Biol. 351:119-128(1993).
RN   [10]
RP   PROTEIN SEQUENCE OF 49-56; 71-79 AND 83-91, AND FUNCTION.
RX   PubMed=8525373; DOI=10.1126/science.270.5243.1811;
RA   Cocchi F., DeVico A.L., Garzino-Demo A., Arya S.K., Gallo R.C.,
RA   Lusso P.;
RT   "Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major
RT   HIV-suppressive factors produced by CD8+ T cells.";
RL   Science 270:1811-1815(1995).
RN   [11]
RP   IDENTIFICATION OF RANTES(3-68), PROTEOLYTIC PROCESSING OF N-TERMINUS,
RP   AND FUNCTION.
RX   PubMed=9516414; DOI=10.1074/jbc.273.13.7222;
RA   Proost P., De Meester I., Schols D., Struyf S., Lambeir A.-M.,
RA   Wuyts A., Opdenakker G., De Clercq E., Scharpe S., Van Damme J.;
RT   "Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase
RT   IV. Conversion of RANTES into a potent inhibitor of monocyte
RT   chemotaxis and HIV-1-infection.";
RL   J. Biol. Chem. 273:7222-7227(1998).
RN   [12]
RP   IDENTIFICATION OF RANTES(4-68), MASS SPECTROMETRY, AND FUNCTION.
RX   PubMed=15923218; DOI=10.1189/jlb.0305161;
RA   Lim J.K., Burns J.M., Lu W., DeVico A.L.;
RT   "Multiple pathways of amino terminal processing produce two truncated
RT   variants of RANTES/CCL5.";
RL   J. Leukoc. Biol. 78:442-452(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=17001303; DOI=10.1038/sj.bjp.0706909;
RA   Ignatov A., Robert J., Gregory-Evans C., Schaller H.C.;
RT   "RANTES stimulates Ca2+ mobilization and inositol trisphosphate (IP3)
RT   formation in cells transfected with G protein-coupled receptor 75.";
RL   Br. J. Pharmacol. 149:490-497(2006).
RN   [14]
RP   FUNCTION.
RX   PubMed=23979485; DOI=10.1007/s00125-013-3022-x;
RA   Liu B., Hassan Z., Amisten S., King A.J., Bowe J.E., Huang G.C.,
RA   Jones P.M., Persaud S.J.;
RT   "The novel chemokine receptor, G-protein-coupled receptor 75, is
RT   expressed by islets and is coupled to stimulation of insulin secretion
RT   and improved glucose homeostasis.";
RL   Diabetologia 56:2467-2476(2013).
RN   [15]
RP   STRUCTURE BY NMR.
RX   PubMed=7537088; DOI=10.1021/bi00016a004;
RA   Skelton N.J., Aspiras F., Ogez J., Schall T.J.;
RT   "Proton NMR assignments and solution conformation of RANTES, a
RT   chemokine of the C-C type.";
RL   Biochemistry 34:5329-5342(1995).
RN   [16]
RP   STRUCTURE BY NMR.
RX   PubMed=7542919; DOI=10.1021/bi00029a005;
RA   Chung C.-W., Cooke R.M., Proudfoot A.E.I., Wells T.N.C.;
RT   "The three-dimensional solution structure of RANTES.";
RL   Biochemistry 34:9307-9314(1995).
RN   [17]
RP   SYNTHESIS, AND X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=9889151; DOI=10.1016/S1074-5521(99)80019-2;
RA   Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H.,
RA   Picard L., Wlodawer A., Lubkowski J., Kent S.B.;
RT   "Total chemical synthesis and high-resolution crystal structure of the
RT   potent anti-HIV protein AOP-RANTES.";
RL   Chem. Biol. 6:43-51(1999).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RA   Hoover D.M., Shaw J., Gryczynski Z., Proudfoot A.E.I., Wells T.N.C.,
RA   Lubkowski J.;
RT   "The crystal structure of Met-RANTES: comparison with native RANTES
RT   and AOP-RANTES.";
RL   Protein Pept. Lett. 7:73-82(2000).
CC   -!- FUNCTION: Chemoattractant for blood monocytes, memory T-helper
CC       cells and eosinophils. Causes the release of histamine from
CC       basophils and activates eosinophils. May activate several
CC       chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of
CC       the major HIV-suppressive factors produced by CD8+ T-cells.
CC       Recombinant RANTES protein induces a dose-dependent inhibition of
CC       different strains of HIV-1, HIV-2, and simian immunodeficiency
CC       virus (SIV). The processed form RANTES(3-68) acts as a natural
CC       chemotaxis inhibitor and is a more potent inhibitor of HIV-1-
CC       infection. The second processed form RANTES(4-68) exhibits reduced
CC       chemotactic and HIV-suppressive activity compared with RANTES(1-
CC       68) and RANTES(3-68) and is generated by an unidentified enzyme
CC       associated with monocytes and neutrophils (PubMed:16791620,
CC       PubMed:1380064, PubMed:8525373, PubMed:9516414, PubMed:15923218).
CC       May also be an agonist of the G protein-coupled receptor GPR75,
CC       stimulating inositol trisphosphate production and calcium
CC       mobilization through its activation. Together with GPR75, may play
CC       a role in neuron survival through activation of a downstream
CC       signaling pathway involving the PI3, Akt and MAP kinases. By
CC       activating GPR75 may also play a role in insulin secretion by
CC       islet cells (PubMed:23979485). {ECO:0000269|PubMed:1380064,
CC       ECO:0000269|PubMed:15923218, ECO:0000269|PubMed:16791620,
CC       ECO:0000269|PubMed:17001303, ECO:0000269|PubMed:23979485,
CC       ECO:0000269|PubMed:8525373, ECO:0000269|PubMed:9516414}.
CC   -!- INTERACTION:
CC       P51681:CCR5; NbExp=4; IntAct=EBI-2848366, EBI-489374;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: T-cell and macrophage specific.
CC   -!- INDUCTION: By mitogens.
CC   -!- PTM: N-terminal processed form RANTES(3-68) is produced by
CC       proteolytic cleavage, probably by DPP4, after secretion from
CC       peripheral blood leukocytes and cultured sarcoma cells.
CC       {ECO:0000269|PubMed:9516414}.
CC   -!- PTM: The identity of the O-linked saccharides at Ser-27 and Ser-28
CC       are not reported in PubMed:1380064. They are assigned by
CC       similarity. {ECO:0000269|PubMed:1380064}.
CC   -!- MASS SPECTROMETRY: Mass=7515; Mass_error=1; Method=SELDI;
CC       Range=27-91; Evidence={ECO:0000269|PubMed:15923218};
CC   -!- MASS SPECTROMETRY: Mass=7862.8; Mass_error=1.1;
CC       Method=Electrospray; Range=24-91;
CC       Evidence={ECO:0000269|PubMed:1380064};
CC   -!- MASS SPECTROMETRY: Mass=8355; Mass_error=10; Method=Electrospray;
CC       Range=24-91; Note=O-glycosylated.;
CC       Evidence={ECO:0000269|PubMed:1380064};
CC   -!- POLYMORPHISM: The variant Phe-24 is an antagonist of the chemokine
CC       receptors CCR1 and CCR3.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ccl5/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=RANTES entry;
CC       URL="http://en.wikipedia.org/wiki/RANTES";
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DR   EMBL; M21121; AAA36725.1; -; mRNA.
DR   EMBL; AF088219; AAC63331.1; -; Genomic_DNA.
DR   EMBL; DQ230537; ABB69929.1; -; mRNA.
DR   EMBL; AF043341; AAC03541.1; -; mRNA.
DR   EMBL; AF266753; AAF73070.1; -; mRNA.
DR   EMBL; DQ017060; AAY22177.1; -; Genomic_DNA.
DR   EMBL; BC008600; AAH08600.1; -; mRNA.
DR   CCDS; CCDS11300.1; -.
DR   PIR; A28815; A28815.
DR   RefSeq; NP_002976.2; NM_002985.2.
DR   UniGene; Hs.514821; -.
DR   PDB; 1B3A; X-ray; 1.60 A; A/B=25-91.
DR   PDB; 1EQT; X-ray; 1.60 A; A/B=26-91.
DR   PDB; 1HRJ; NMR; -; A/B=24-91.
DR   PDB; 1RTN; NMR; -; A/B=24-91.
DR   PDB; 1RTO; NMR; -; A/B=24-91.
DR   PDB; 1U4L; X-ray; 2.00 A; A/B=24-91.
DR   PDB; 1U4M; X-ray; 2.00 A; A/B=24-91.
DR   PDB; 1U4P; X-ray; 1.70 A; A/B=24-91.
DR   PDB; 1U4R; X-ray; 2.20 A; A/B/C/D=24-91.
DR   PDB; 2L9H; Other; -; A/B/C/D=24-91.
DR   PDB; 2VXW; X-ray; 1.70 A; A/B/C/D=33-91.
DR   PDBsum; 1B3A; -.
DR   PDBsum; 1EQT; -.
DR   PDBsum; 1HRJ; -.
DR   PDBsum; 1RTN; -.
DR   PDBsum; 1RTO; -.
DR   PDBsum; 1U4L; -.
DR   PDBsum; 1U4M; -.
DR   PDBsum; 1U4P; -.
DR   PDBsum; 1U4R; -.
DR   PDBsum; 2L9H; -.
DR   PDBsum; 2VXW; -.
DR   ProteinModelPortal; P13501; -.
DR   SMR; P13501; 25-91.
DR   BioGrid; 112255; 16.
DR   DIP; DIP-31N; -.
DR   IntAct; P13501; 13.
DR   MINT; MINT-103226; -.
DR   STRING; 9606.ENSP00000293272; -.
DR   BindingDB; P13501; -.
DR   ChEMBL; CHEMBL1275217; -.
DR   PhosphoSite; P13501; -.
DR   DMDM; 6175077; -.
DR   PaxDb; P13501; -.
DR   PeptideAtlas; P13501; -.
DR   PRIDE; P13501; -.
DR   DNASU; 6352; -.
DR   Ensembl; ENST00000603197; ENSP00000474412; ENSG00000271503.
DR   Ensembl; ENST00000605140; ENSP00000475057; ENSG00000271503.
DR   Ensembl; ENST00000613606; ENSP00000479894; ENSG00000274233.
DR   GeneID; 6352; -.
DR   KEGG; hsa:6352; -.
DR   UCSC; uc002hkf.3; human.
DR   CTD; 6352; -.
DR   GeneCards; GC17M034198; -.
DR   HGNC; HGNC:10632; CCL5.
DR   MIM; 187011; gene.
DR   neXtProt; NX_P13501; -.
DR   PharmGKB; PA35564; -.
DR   eggNOG; NOG38896; -.
DR   GeneTree; ENSGT00730000110278; -.
DR   HOVERGEN; HBG017871; -.
DR   InParanoid; P13501; -.
DR   KO; K12499; -.
DR   OrthoDB; EOG7CVQ1F; -.
DR   PhylomeDB; P13501; -.
DR   TreeFam; TF334888; -.
DR   Reactome; REACT_15344; Chemokine receptors bind chemokines.
DR   Reactome; REACT_19231; G alpha (i) signalling events.
DR   EvolutionaryTrace; P13501; -.
DR   GeneWiki; CCL5; -.
DR   GenomeRNAi; 6352; -.
DR   NextBio; 24676; -.
DR   PMAP-CutDB; P13501; -.
DR   PRO; PR:P13501; -.
DR   Bgee; P13501; -.
DR   CleanEx; HS_CCL5; -.
DR   ExpressionAtlas; P13501; differential.
DR   Genevestigator; P13501; -.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0031726; F:CCR1 chemokine receptor binding; IPI:UniProtKB.
DR   GO; GO:0031729; F:CCR4 chemokine receptor binding; TAS:BHF-UCL.
DR   GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:BHF-UCL.
DR   GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR   GO; GO:0008009; F:chemokine activity; NAS:UniProtKB.
DR   GO; GO:0046817; F:chemokine receptor antagonist activity; IDA:BHF-UCL.
DR   GO; GO:0042379; F:chemokine receptor binding; IPI:BHF-UCL.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR   GO; GO:0016004; F:phospholipase activator activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR   GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; IDA:BHF-UCL.
DR   GO; GO:0030298; F:receptor signaling protein tyrosine kinase activator activity; IDA:BHF-UCL.
DR   GO; GO:0031584; P:activation of phospholipase D activity; IDA:BHF-UCL.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
DR   GO; GO:0043623; P:cellular protein complex assembly; IDA:BHF-UCL.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006935; P:chemotaxis; NAS:UniProtKB.
DR   GO; GO:0002407; P:dendritic cell chemotaxis; TAS:BHF-UCL.
DR   GO; GO:0048245; P:eosinophil chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0048246; P:macrophage chemotaxis; TAS:BHF-UCL.
DR   GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0002548; P:monocyte chemotaxis; IC:UniProtKB.
DR   GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR   GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IDA:GOC.
DR   GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
DR   GO; GO:0070233; P:negative regulation of T cell apoptotic process; IDA:BHF-UCL.
DR   GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
DR   GO; GO:0042119; P:neutrophil activation; IDA:BHF-UCL.
DR   GO; GO:0050918; P:positive chemotaxis; IDA:GOC.
DR   GO; GO:0010535; P:positive regulation of activation of JAK2 kinase activity; TAS:BHF-UCL.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:BHF-UCL.
DR   GO; GO:0031328; P:positive regulation of cellular biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0034112; P:positive regulation of homotypic cell-cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0045089; P:positive regulation of innate immune response; TAS:BHF-UCL.
DR   GO; GO:0046427; P:positive regulation of JAK-STAT cascade; TAS:BHF-UCL.
DR   GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IDA:BHF-UCL.
DR   GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:BHF-UCL.
DR   GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR   GO; GO:0042327; P:positive regulation of phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IDA:GOC.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0070234; P:positive regulation of T cell apoptotic process; IDA:BHF-UCL.
DR   GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:BHF-UCL.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IDA:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0045948; P:positive regulation of translational initiation; NAS:BHF-UCL.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; TAS:BHF-UCL.
DR   GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:GOC.
DR   GO; GO:0051262; P:protein tetramerization; IDA:BHF-UCL.
DR   GO; GO:0002676; P:regulation of chronic inflammatory response; TAS:BHF-UCL.
DR   GO; GO:0050796; P:regulation of insulin secretion; IDA:UniProtKB.
DR   GO; GO:1901214; P:regulation of neuron death; IDA:UniProtKB.
DR   GO; GO:0050863; P:regulation of T cell activation; IDA:BHF-UCL.
DR   GO; GO:0009636; P:response to toxic substance; IDA:UniProtKB.
DR   GO; GO:0009615; P:response to virus; TAS:BHF-UCL.
DR   InterPro; IPR000827; Chemokine_CC_CS.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   Pfam; PF00048; IL8; 1.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; SSF54117; 1.
DR   PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chemotaxis; Complete proteome; Cytokine;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Inflammatory response; Oxidation; Polymorphism; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL        1     23       {ECO:0000269|PubMed:1380064,
FT                                ECO:0000269|PubMed:7524281}.
FT   CHAIN        24     91       C-C motif chemokine 5.
FT                                /FTId=PRO_0000005175.
FT   CHAIN        26     91       RANTES(3-68).
FT                                /FTId=PRO_0000005176.
FT   CHAIN        27     91       RANTES(4-68).
FT                                /FTId=PRO_0000005177.
FT   SITE         25     26       Cleavage; by DPP4.
FT   MOD_RES      90     90       Methionine sulfoxide.
FT                                {ECO:0000269|PubMed:1380064}.
FT   CARBOHYD     27     27       O-linked (GalNAc...); partial.
FT                                {ECO:0000269|PubMed:1380064}.
FT   CARBOHYD     28     28       O-linked (GalNAc...); partial.
FT                                {ECO:0000269|PubMed:1380064}.
FT   DISULFID     33     57
FT   DISULFID     34     73
FT   VARIANT      24     24       S -> F. {ECO:0000269|PubMed:16791620}.
FT                                /FTId=VAR_043043.
FT   CONFLICT      7      7       A -> R (in Ref. 1; AAA36725 and 5;
FT                                AAF73070). {ECO:0000305}.
FT   CONFLICT     14     14       A -> V (in Ref. 5; AAF73070).
FT                                {ECO:0000305}.
FT   STRAND       31     33       {ECO:0000244|PDB:1B3A}.
FT   STRAND       35     40       {ECO:0000244|PDB:2VXW}.
FT   HELIX        44     46       {ECO:0000244|PDB:1B3A}.
FT   STRAND       47     52       {ECO:0000244|PDB:1B3A}.
FT   STRAND       57     59       {ECO:0000244|PDB:1B3A}.
FT   STRAND       62     66       {ECO:0000244|PDB:1B3A}.
FT   STRAND       71     74       {ECO:0000244|PDB:1B3A}.
FT   HELIX        79     89       {ECO:0000244|PDB:1B3A}.
SQ   SEQUENCE   91 AA;  9990 MW;  FB0BFAF9A87C620F CRC64;
     MKVSAAALAV ILIATALCAP ASASPYSSDT TPCCFAYIAR PLPRAHIKEY FYTSGKCSNP
     AVVFVTRKNR QVCANPEKKW VREYINSLEM S
//
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