CCL5_MOUSE
ID CCL5_MOUSE Reviewed; 91 AA.
AC P30882;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=C-C motif chemokine 5;
DE AltName: Full=MuRantes;
DE AltName: Full=SIS-delta;
DE AltName: Full=Small-inducible cytokine A5;
DE AltName: Full=T-cell-specific protein RANTES;
DE Flags: Precursor;
GN Name=Ccl5; Synonyms=Scya5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1375672; DOI=10.1038/ki.1992.31;
RA Heeger P., Wolf G., Meyers C., Sun M.J., O'Farrell S.C., Krensky A.M.,
RA Neilson E.G.;
RT "Isolation and characterization of cDNA from renal tubular epithelium
RT encoding murine Rantes.";
RL Kidney Int. 41:220-225(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1376260; DOI=10.1002/eji.1830220621;
RA Schall T.J., Simpson N.J., Mak J.Y.;
RT "Molecular cloning and expression of the murine RANTES cytokine: structural
RT and functional conservation between mouse and man.";
RL Eur. J. Immunol. 22:1477-1481(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH Swiss;
RX PubMed=7507961;
RA Danoff T.M., Lalley P.A., Chang Y.S., Heeger P.S., Neilson E.G.;
RT "Cloning, genomic organization, and chromosomal localization of the Scya5
RT gene encoding the murine chemokine RANTES.";
RL J. Immunol. 152:1182-1189(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=7513046; DOI=10.1128/mcb.14.5.2914-2925.1994;
RA Shin H.S., Drysdale B.E., Shin M.L., Noble P.W., Fisher S.N.,
RA Paznekas W.A.;
RT "Definition of a lipopolysaccharide-responsive element in the 5'-flanking
RT regions of MuRantes and crg-2.";
RL Mol. Cell. Biol. 14:2914-2925(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10.S/J, BALB/cJ, DBA/2J, NOD/LtJ, and SJL/J; TISSUE=Spleen;
RX PubMed=10438970;
RA Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W.,
RA Blankenhorn E.P.;
RT "Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte
RT chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for
RT eae7, a locus controlling susceptibility to monophasic
RT remitting/nonrelapsing experimental allergic encephalomyelitis.";
RL J. Immunol. 163:2262-2266(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/Sv;
RA Nomiyama H.;
RT "Organization of the mouse CC chemokine cluster containing the genes for
RT C10, MRP-2 and RANTES.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
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. May also be an agonist of the G
CC protein-coupled receptor GPR75. Together with GPR75, may play a role in
CC neuron survival through activation of a downstream signaling pathway
CC involving the PI3, Akt and MAP kinases. By activating GPR75 may also
CC play a role in insulin secretion by islet cells.
CC {ECO:0000250|UniProtKB:P13501}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: T-cell and macrophage specific.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; M77747; AAA40029.1; -; mRNA.
DR EMBL; S37648; AAB22330.1; -; mRNA.
DR EMBL; U02298; AAA18302.1; -; Unassigned_DNA.
DR EMBL; X70675; CAA50011.1; -; Genomic_DNA.
DR EMBL; AF065944; AAC17511.1; -; mRNA.
DR EMBL; AF065945; AAC17512.1; -; mRNA.
DR EMBL; AF065946; AAC17513.1; -; mRNA.
DR EMBL; AF065947; AAC17514.1; -; mRNA.
DR EMBL; AF128187; AAF22528.1; -; mRNA.
DR EMBL; AB051897; BAB18731.1; -; Genomic_DNA.
DR EMBL; AK003101; BAB22566.1; -; mRNA.
DR EMBL; BC033508; AAH33508.1; -; mRNA.
DR CCDS; CCDS36254.1; -.
DR PIR; I48875; A46539.
DR RefSeq; NP_038681.2; NM_013653.3.
DR PDB; 5YAM; NMR; -; A/B=24-91.
DR PDBsum; 5YAM; -.
DR AlphaFoldDB; P30882; -.
DR SMR; P30882; -.
DR IntAct; P30882; 4.
DR STRING; 10090.ENSMUSP00000039600; -.
DR PhosphoSitePlus; P30882; -.
DR PaxDb; P30882; -.
DR PRIDE; P30882; -.
DR ProteomicsDB; 281333; -.
DR DNASU; 20304; -.
DR Ensembl; ENSMUST00000035938; ENSMUSP00000039600; ENSMUSG00000035042.
DR GeneID; 20304; -.
DR KEGG; mmu:20304; -.
DR UCSC; uc007kpi.2; mouse.
DR CTD; 6352; -.
DR MGI; MGI:98262; Ccl5.
DR VEuPathDB; HostDB:ENSMUSG00000035042; -.
DR eggNOG; ENOG502S8D1; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_2_1; -.
DR InParanoid; P30882; -.
DR OMA; CCFAYLS; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P30882; -.
DR TreeFam; TF334888; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20304; 2 hits in 77 CRISPR screens.
DR PRO; PR:P30882; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P30882; protein.
DR Bgee; ENSMUSG00000035042; Expressed in peripheral lymph node and 99 other tissues.
DR ExpressionAtlas; P30882; baseline and differential.
DR Genevisible; P30882; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
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:0031730; F:CCR5 chemokine receptor binding; ISS:BHF-UCL.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; ISS:BHF-UCL.
DR GO; GO:0046817; F:chemokine receptor antagonist activity; ISS:BHF-UCL.
DR GO; GO:0042379; F:chemokine receptor binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISO:MGI.
DR GO; GO:0016004; F:phospholipase activator activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
DR GO; GO:0030298; F:receptor signaling protein tyrosine kinase activator activity; ISS:BHF-UCL.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISS:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISS:BHF-UCL.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISS:BHF-UCL.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0048247; P:lymphocyte chemotaxis; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IMP:BHF-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; ISS:BHF-UCL.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:BHF-UCL.
DR GO; GO:0042119; P:neutrophil activation; ISS:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:BHF-UCL.
DR GO; GO:0031328; P:positive regulation of cellular biosynthetic process; ISS:BHF-UCL.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; NAS:BHF-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IC:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0031622; P:positive regulation of fever generation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
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; ISS:BHF-UCL.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:BHF-UCL.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:BHF-UCL.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:BHF-UCL.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:BHF-UCL.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; ISS:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISS:BHF-UCL.
DR GO; GO:2000406; P:positive regulation of T cell migration; ISO:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:BHF-UCL.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:MGI.
DR GO; GO:0031269; P:pseudopodium assembly; ISO:MGI.
DR GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:1901214; P:regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0050863; P:regulation of T cell activation; ISS:BHF-UCL.
DR GO; GO:0034097; P:response to cytokine; IDA:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR GO; GO:0034612; P:response to tumor necrosis factor; IDA:MGI.
DR GO; GO:0035688; P:T-helper 1 cell diapedesis; ISO:MGI.
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; Disulfide bond; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..91
FT /note="C-C motif chemokine 5"
FT /id="PRO_0000005179"
FT DISULFID 33..57
FT /evidence="ECO:0000250"
FT DISULFID 34..73
FT /evidence="ECO:0000250"
FT CONFLICT 19
FT /note="T -> A (in Ref. 2; AAB22330)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="A -> E (in Ref. 1; AAA40029)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5YAM"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5YAM"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5YAM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5YAM"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5YAM"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5YAM"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:5YAM"
SQ SEQUENCE 91 AA; 10071 MW; 5DFD66F4684FE1C8 CRC64;
MKISAAALTI ILTAAALCTP APASPYGSDT TPCCFAYLSL ALPRAHVKEY FYTSSKCSNL
AVVFVTRRNR QVCANPEKKW VQEYINYLEM S
