CCL5_HUMAN
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 03-AUG-2022, entry version 216.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 17q11.2
RT containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES.";
RL J. Interferon Cytokine Res. 19:227-234(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT PHE-24, AND CHARACTERIZATION
RP OF 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., Dudoit Y.,
RA Deterre P., Menu E., Barre-Sinoussi F., Debre P., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 24-55, FUNCTION, MASS SPECTROMETRY, GLYCOSYLATION AT
RP 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., 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; DOI=10.1007/978-1-4615-2952-1_13;
RA Schroeder J.-M., Kameyoshi Y., Christophers E.;
RT "Platelets secrete an eosinophil-chemotactic cytokine which is a member of
RT 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., Lusso P.;
RT "Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-
RT 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, AND
RP FUNCTION.
RX PubMed=9516414; DOI=10.1074/jbc.273.13.7222;
RA Proost P., De Meester I., Schols D., Struyf S., Lambeir A.-M., Wuyts A.,
RA Opdenakker G., De Clercq E., Scharpe S., Van Damme J.;
RT "Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV.
RT Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and
RT 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 PROTEOLYTIC CLEAVAGE, AND MASS SPECTROMETRY.
RX PubMed=16963625; DOI=10.1189/jlb.0406290;
RA Lim J.K., Lu W., Hartley O., DeVico A.L.;
RT "N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and
RT related analogs into a truncated 4-68 variant.";
RL J. Leukoc. Biol. 80:1395-1404(2006).
RN [15]
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 expressed
RT by islets and is coupled to stimulation of insulin secretion and improved
RT glucose homeostasis.";
RL Diabetologia 56:2467-2476(2013).
RN [16]
RP MUTAGENESIS OF THR-31; HIS-46; GLU-49; GLY-55; 67-ARG--ARG-70 AND
RP 78-LYS--ARG-82.
RX PubMed=25266725; DOI=10.1074/jbc.m114.599233;
RA Bonvin P., Dunn S.M., Rousseau F., Dyer D.P., Shaw J., Power C.A.,
RA Handel T.M., Proudfoot A.E.;
RT "Identification of the pharmacophore of the CC chemokine-binding proteins
RT Evasin-1 and -4 using phage display.";
RL J. Biol. Chem. 289:31846-31855(2014).
RN [17]
RP TISSUE SPECIFICITY.
RX PubMed=23765988; DOI=10.1002/jcp.24418;
RA Caballero-Campo P., Buffone M.G., Benencia F., Conejo-Garcia J.R.,
RA Rinaudo P.F., Gerton G.L.;
RT "A role for the chemokine receptor CCR6 in mammalian sperm motility and
RT chemotaxis.";
RL J. Cell. Physiol. 229:68-78(2014).
RN [18]
RP SUBUNIT.
RX PubMed=32817341; DOI=10.1074/jbc.ra120.013891;
RA Denisov S.S., Ramirez-Escudero M., Heinzmann A.C.A., Ippel J.H.,
RA Dawson P.E., Koenen R.R., Hackeng T.M., Janssen B.J.C., Dijkgraaf I.;
RT "Structural characterization of anti-CCL5 activity of the tick salivary
RT protein evasin-4.";
RL J. Biol. Chem. 295:14367-14378(2020).
RN [19] {ECO:0007744|PDB:1RTN, ECO:0007744|PDB:1RTO}
RP STRUCTURE BY NMR OF 24-91.
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 chemokine of
RT the C-C type.";
RL Biochemistry 34:5329-5342(1995).
RN [20] {ECO:0007744|PDB:1HRJ}
RP STRUCTURE BY NMR OF 24-91.
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 [21] {ECO:0007744|PDB:1B3A}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 25-91, AND SYNTHESIS OF 25-91.
RX PubMed=9889151; DOI=10.1016/s1074-5521(99)80019-2;
RA Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H., Picard L.,
RA 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 [22] {ECO:0007744|PDB:1EQT}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-91.
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 and
RT AOP-RANTES.";
RL Protein Pept. Lett. 7:73-82(2000).
CC -!- FUNCTION: Chemoattractant for blood monocytes, memory T-helper cells
CC and eosinophils. Causes the release of histamine from basophils and
CC activates eosinophils. May activate several chemokine receptors
CC including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive
CC factors produced by CD8+ T-cells. Recombinant RANTES protein induces a
CC dose-dependent inhibition of different strains of HIV-1, HIV-2, and
CC simian immunodeficiency virus (SIV). The processed form RANTES(3-68)
CC acts as a natural chemotaxis inhibitor and is a more potent inhibitor
CC of HIV-1-infection. The second processed form RANTES(4-68) exhibits
CC reduced chemotactic and HIV-suppressive activity compared with
CC RANTES(1-68) and RANTES(3-68) (PubMed:16791620, PubMed:1380064,
CC PubMed:8525373, PubMed:9516414, PubMed:15923218). May also be an
CC agonist of the G protein-coupled receptor GPR75, stimulating inositol
CC trisphosphate production and calcium mobilization through its
CC activation. Together with GPR75, may play a role in neuron survival
CC through activation of a downstream signaling pathway involving the PI3,
CC Akt and MAP kinases. By activating GPR75 may also play a role in
CC insulin secretion by islet cells (PubMed:23979485).
CC {ECO:0000269|PubMed:1380064, ECO:0000269|PubMed:15923218,
CC ECO:0000269|PubMed:16791620, ECO:0000269|PubMed:17001303,
CC ECO:0000269|PubMed:23979485, ECO:0000269|PubMed:8525373,
CC ECO:0000269|PubMed:9516414}.
CC -!- SUBUNIT: Homo and heterooligomers with other chemokines. Interacts with
CC the brown dog tick evasin-4. {ECO:0000269|PubMed:32817341}.
CC -!- INTERACTION:
CC P13501; P51671: CCL11; NbExp=2; IntAct=EBI-2848366, EBI-727357;
CC P13501; Q99616: CCL13; NbExp=3; IntAct=EBI-2848366, EBI-725342;
CC P13501; O15467: CCL16; NbExp=2; IntAct=EBI-2848366, EBI-12204739;
CC P13501; Q92583: CCL17; NbExp=9; IntAct=EBI-2848366, EBI-16640146;
CC P13501; P13500: CCL2; NbExp=2; IntAct=EBI-2848366, EBI-1034732;
CC P13501; P78556: CCL20; NbExp=2; IntAct=EBI-2848366, EBI-3913209;
CC P13501; O00585: CCL21; NbExp=2; IntAct=EBI-2848366, EBI-953695;
CC P13501; O00175: CCL24; NbExp=3; IntAct=EBI-2848366, EBI-16803966;
CC P13501; O15444: CCL25; NbExp=2; IntAct=EBI-2848366, EBI-7783341;
CC P13501; Q9Y258: CCL26; NbExp=4; IntAct=EBI-2848366, EBI-7783416;
CC P13501; Q9Y4X3: CCL27; NbExp=2; IntAct=EBI-2848366, EBI-16744026;
CC P13501; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-2848366, EBI-7783254;
CC P13501; P13501: CCL5; NbExp=11; IntAct=EBI-2848366, EBI-2848366;
CC P13501; P32246: CCR1; NbExp=2; IntAct=EBI-2848366, EBI-608322;
CC P13501; P51681: CCR5; NbExp=6; IntAct=EBI-2848366, EBI-489374;
CC P13501; P02778: CXCL10; NbExp=2; IntAct=EBI-2848366, EBI-7815386;
CC P13501; O14625: CXCL11; NbExp=2; IntAct=EBI-2848366, EBI-2871971;
CC P13501; P48061: CXCL12; NbExp=5; IntAct=EBI-2848366, EBI-3913254;
CC P13501; O95715: CXCL14; NbExp=2; IntAct=EBI-2848366, EBI-2798068;
CC P13501; Q6UXB2: CXCL17; NbExp=2; IntAct=EBI-2848366, EBI-16804198;
CC P13501; P19875: CXCL2; NbExp=2; IntAct=EBI-2848366, EBI-2114901;
CC P13501; P80162: CXCL6; NbExp=2; IntAct=EBI-2848366, EBI-9214033;
CC P13501; Q07325: CXCL9; NbExp=2; IntAct=EBI-2848366, EBI-3911467;
CC P13501; P02776: PF4; NbExp=6; IntAct=EBI-2848366, EBI-2565740;
CC P13501; PRO_0000351217 [P02776]: PF4; NbExp=2; IntAct=EBI-2848366, EBI-20561364;
CC P13501; P02775: PPBP; NbExp=2; IntAct=EBI-2848366, EBI-718973;
CC P13501; P47992: XCL1; NbExp=3; IntAct=EBI-2848366, EBI-10209901;
CC P13501; Q9UBD3: XCL2; NbExp=2; IntAct=EBI-2848366, EBI-10319095;
CC PRO_0000005175; Q92583: CCL17; NbExp=6; IntAct=EBI-11712923, EBI-16640146;
CC PRO_0000005175; P48061: CXCL12; NbExp=2; IntAct=EBI-11712923, EBI-3913254;
CC PRO_0000005175; P02776: PF4; NbExp=3; IntAct=EBI-11712923, EBI-2565740;
CC PRO_0000005175; PRO_0000351217 [P02776]: PF4; NbExp=2; IntAct=EBI-11712923, EBI-20561364;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in the follicular fluid (at protein
CC level). T-cell and macrophage specific. {ECO:0000269|PubMed:23765988,
CC ECO:0000269|PubMed:2456327}.
CC -!- INDUCTION: By mitogens.
CC -!- PTM: N-terminal processed form RANTES(3-68) is produced by proteolytic
CC cleavage, probably by DPP4, after secretion from peripheral blood
CC leukocytes and cultured sarcoma cells. {ECO:0000269|PubMed:9516414}.
CC -!- PTM: N-terminal processed form RANTES(4-68) is produced by proteolytic
CC cleavage by cathepsin CTSG. {ECO:0000269|PubMed:16963625}.
CC -!- PTM: The identity of the O-linked saccharides at Ser-27 and Ser-28 are
CC not reported in PubMed:1380064. They are assigned by similarity.
CC {ECO:0000269|PubMed:1380064}.
CC -!- MASS SPECTROMETRY: [RANTES(4-68)]: Mass=7515; Mass_error=1;
CC Method=SELDI; Evidence={ECO:0000269|PubMed:15923218,
CC ECO:0000269|PubMed:16963625};
CC -!- MASS SPECTROMETRY: [C-C motif chemokine 5]: Mass=7862.8;
CC Mass_error=1.1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:1380064};
CC -!- MASS SPECTROMETRY: [C-C motif chemokine 5]: Mass=7863.3; Method=SELDI;
CC Evidence={ECO:0000269|PubMed:16963625};
CC -!- MASS SPECTROMETRY: [C-C motif chemokine 5]: Mass=8355; Mass_error=10;
CC Method=Electrospray; Note=O-glycosylated.;
CC Evidence={ECO:0000269|PubMed:1380064};
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="https://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 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 PDB; 5CMD; X-ray; 3.09 A; A/B/C/D/E/F=27-91.
DR PDB; 5COY; X-ray; 1.44 A; A/B=27-91.
DR PDB; 5DNF; X-ray; 2.55 A; A/B/C/D/E/F/G/H/I=27-91.
DR PDB; 5L2U; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I=27-91.
DR PDB; 5UIW; X-ray; 2.20 A; B=33-91.
DR PDB; 6AEZ; X-ray; 1.63 A; A/B/C=24-91.
DR PDB; 6C6D; X-ray; 5.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=27-91.
DR PDB; 6FGP; NMR; -; B=24-91.
DR PDB; 6LOG; X-ray; 2.55 A; A=24-91.
DR PDB; 6STK; X-ray; 1.52 A; A/B=24-91.
DR PDB; 7F1R; EM; 3.00 A; R=24-91.
DR PDB; 7O7F; EM; 3.15 A; I=23-91.
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 PDBsum; 5CMD; -.
DR PDBsum; 5COY; -.
DR PDBsum; 5DNF; -.
DR PDBsum; 5L2U; -.
DR PDBsum; 5UIW; -.
DR PDBsum; 6AEZ; -.
DR PDBsum; 6C6D; -.
DR PDBsum; 6FGP; -.
DR PDBsum; 6LOG; -.
DR PDBsum; 6STK; -.
DR PDBsum; 7F1R; -.
DR PDBsum; 7O7F; -.
DR AlphaFoldDB; P13501; -.
DR BMRB; P13501; -.
DR SMR; P13501; -.
DR BioGRID; 112255; 61.
DR DIP; DIP-31N; -.
DR IntAct; P13501; 61.
DR MINT; P13501; -.
DR STRING; 9606.ENSP00000474412; -.
DR BindingDB; P13501; -.
DR ChEMBL; CHEMBL1275217; -.
DR DrugBank; DB02322; Heparin Disaccharide I-S.
DR DrugBank; DB02353; Heparin Disaccharide Iii-S.
DR GlyGen; P13501; 2 sites.
DR iPTMnet; P13501; -.
DR PhosphoSitePlus; P13501; -.
DR BioMuta; CCL5; -.
DR DMDM; 6175077; -.
DR EPD; P13501; -.
DR MassIVE; P13501; -.
DR PaxDb; P13501; -.
DR PeptideAtlas; P13501; -.
DR PRIDE; P13501; -.
DR ProteomicsDB; 52922; -.
DR TopDownProteomics; P13501; -.
DR ABCD; P13501; 5 sequenced antibodies.
DR Antibodypedia; 73329; 924 antibodies from 40 providers.
DR CPTC; P13501; 1 antibody.
DR DNASU; 6352; -.
DR Ensembl; ENST00000603197.6; ENSP00000474412.1; ENSG00000271503.6.
DR Ensembl; ENST00000605140.6; ENSP00000475057.1; ENSG00000271503.6.
DR Ensembl; ENST00000605509.2; ENSP00000474141.2; ENSG00000271503.6.
DR Ensembl; ENST00000613606.2; ENSP00000479894.1; ENSG00000274233.4.
DR Ensembl; ENST00000618639.4; ENSP00000484921.2; ENSG00000274233.4.
DR GeneID; 6352; -.
DR KEGG; hsa:6352; -.
DR UCSC; uc002hkf.5; human.
DR CTD; 6352; -.
DR DisGeNET; 6352; -.
DR GeneCards; CCL5; -.
DR HGNC; HGNC:10632; CCL5.
DR HPA; ENSG00000271503; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 187011; gene.
DR neXtProt; NX_P13501; -.
DR OpenTargets; ENSG00000271503; -.
DR PharmGKB; PA35564; -.
DR VEuPathDB; HostDB:ENSG00000271503; -.
DR eggNOG; ENOG502S8D1; Eukaryota.
DR GeneTree; ENSGT01050000246728; -.
DR HOGENOM; CLU_141716_4_2_1; -.
DR InParanoid; P13501; -.
DR OrthoDB; 1354015at2759; -.
DR PhylomeDB; P13501; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P13501; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; P13501; -.
DR SIGNOR; P13501; -.
DR BioGRID-ORCS; 6352; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; CCL5; human.
DR EvolutionaryTrace; P13501; -.
DR GeneWiki; CCL5; -.
DR GenomeRNAi; 6352; -.
DR Pharos; P13501; Tchem.
DR PRO; PR:P13501; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13501; protein.
DR Bgee; ENSG00000271503; Expressed in granulocyte and 102 other tissues.
DR ExpressionAtlas; P13501; baseline and differential.
DR Genevisible; P13501; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0031726; F:CCR1 chemokine receptor binding; IDA:BHF-UCL.
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; IDA:BHF-UCL.
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:0042802; F:identical protein binding; IPI:IntAct.
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: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:0098586; P:cellular response to virus; IEP:ARUK-UCL.
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:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor 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:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0010536; P:positive regulation of activation of Janus 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:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
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: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:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; TAS:BHF-UCL.
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: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; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR000827; Chemokine_CC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
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; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Inflammatory response; Oxidation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1380064,
FT ECO:0000269|PubMed:7524281"
FT CHAIN 24..91
FT /note="C-C motif chemokine 5"
FT /id="PRO_0000005175"
FT CHAIN 26..91
FT /note="RANTES(3-68)"
FT /id="PRO_0000005176"
FT CHAIN 27..91
FT /note="RANTES(4-68)"
FT /id="PRO_0000005177"
FT SITE 25..26
FT /note="Cleavage; by DPP4"
FT MOD_RES 90
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:1380064"
FT CARBOHYD 27
FT /note="O-linked (GalNAc...) serine; partial"
FT /evidence="ECO:0000269|PubMed:1380064"
FT CARBOHYD 28
FT /note="O-linked (GalNAc...) serine; partial"
FT /evidence="ECO:0000269|PubMed:1380064"
FT DISULFID 33..57
FT /evidence="ECO:0000269|PubMed:7537088,
FT ECO:0000269|PubMed:7542919, ECO:0000269|PubMed:9889151,
FT ECO:0000269|Ref.22, ECO:0007744|PDB:1B3A,
FT ECO:0007744|PDB:1EQT, ECO:0007744|PDB:1HRJ,
FT ECO:0007744|PDB:1RTN, ECO:0007744|PDB:1RTO"
FT DISULFID 34..73
FT /evidence="ECO:0000269|PubMed:7537088,
FT ECO:0000269|PubMed:7542919, ECO:0000269|PubMed:9889151,
FT ECO:0000269|Ref.22, ECO:0007744|PDB:1B3A,
FT ECO:0007744|PDB:1EQT, ECO:0007744|PDB:1HRJ,
FT ECO:0007744|PDB:1RTN, ECO:0007744|PDB:1RTO"
FT VARIANT 24
FT /note="S -> F (antagonist of the chemokine receptors CCR1
FT and CCR3; dbSNP:rs377415776)"
FT /evidence="ECO:0000269|PubMed:16791620"
FT /id="VAR_043043"
FT MUTAGEN 31
FT /note="T->A: No effect on inhibition of activity by tick
FT evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 31
FT /note="T->A: Reduced inhibition of activity by tick evasin-
FT 4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 46
FT /note="H->A: No effect on inhibition of activity by tick
FT evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 49
FT /note="E->A: No effect on inhibition of activity by tick
FT evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 55
FT /note="G->A,K: No effect on inhibition of activity by tick
FT evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 67..70
FT /note="RKNR->AANA: No effect on inhibition of activity by
FT tick evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT MUTAGEN 78..82
FT /note="KKWVR->AAWVA: No effect on inhibition of activity by
FT tick evasin-4."
FT /evidence="ECO:0000269|PubMed:25266725"
FT CONFLICT 7
FT /note="A -> R (in Ref. 1; AAA36725 and 5; AAF73070)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="A -> V (in Ref. 5; AAF73070)"
FT /evidence="ECO:0000305"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:7F1R"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6AEZ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5COY"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7F1R"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:5COY"
SQ SEQUENCE 91 AA; 9990 MW; FB0BFAF9A87C620F CRC64;
MKVSAAALAV ILIATALCAP ASASPYSSDT TPCCFAYIAR PLPRAHIKEY FYTSGKCSNP
AVVFVTRKNR QVCANPEKKW VREYINSLEM S
