CCL9_MOUSE
ID CCL9_MOUSE Reviewed; 122 AA.
AC P51670; Q5QNW2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=C-C motif chemokine 9;
DE AltName: Full=CCF18;
DE AltName: Full=Macrophage inflammatory protein 1-gamma;
DE Short=MIP-1-gamma;
DE AltName: Full=Macrophage inflammatory protein-related protein 2;
DE Short=MRP-2;
DE AltName: Full=Small-inducible cytokine A9;
DE Contains:
DE RecName: Full=CCL9(29-101);
DE Contains:
DE RecName: Full=CCL9(30-101);
DE Contains:
DE RecName: Full=CCL9(31-101);
DE Flags: Precursor;
GN Name=Ccl9; Synonyms=Mrp2, Scya10, Scya9;
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=8597875;
RA Poltorak A.N., Bazzoni F., Smirnova I.I., Alejos E., Thompson P.,
RA Luheshi G., Rothwell N., Beutler B.;
RT "MIP-1 gamma: molecular cloning, expression, and biological activities of a
RT novel CC chemokine that is constitutively secreted in vivo.";
RL J. Inflamm. 45:207-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7650394;
RA Youn B.-S., Jang I.-K., Broxmeyer H.E., Cooper S., Jenkins N.A.,
RA Gilbert D.J., Copeland N.G., Elick T.A., Fraser M.J. Jr., Kwon B.S.;
RT "A novel chemokine, macrophage inflammatory protein-related protein-2,
RT inhibits colony formation of bone marrow myeloid progenitors.";
RL J. Immunol. 155:2661-2667(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7594550;
RA Hara T., Bacon K.B., Cho L.C., Yoshimura A., Morikawa Y., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Schall T.J., Miyajima A.;
RT "Molecular cloning and functional characterization of a novel member of the
RT C-C chemokine family.";
RL J. Immunol. 155:5352-5358(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP IDENTIFICATION OF CCL9(29-101); CCL9(30-101) AND CCL9(31-101), AND
RP PROTEOLYTIC PROCESSING OF N-TERMINUS.
RX PubMed=15905581; DOI=10.4049/jimmunol.174.11.7341;
RA Berahovich R.D., Miao Z., Wang Y., Premack B., Howard M.C., Schall T.J.;
RT "Proteolytic activation of alternative CCR1 ligands in inflammation.";
RL J. Immunol. 174:7341-7351(2005).
CC -!- FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic
CC properties. Circulates at high concentrations in the blood of healthy
CC animals. Binding to a high-affinity receptor activates calcium release
CC in neutrophils. It also inhibits colony formation of bone marrow
CC myeloid immature progenitors.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the liver, lung, and the
CC thymus, although some expression has been detected in a wide variety of
CC tissues except brain.
CC -!- INDUCTION: By interleukin-4; in the bone marrow macrophage.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; U49513; AAB02198.1; -; mRNA.
DR EMBL; U15209; AAA92583.1; -; mRNA.
DR EMBL; U19482; AAB17120.1; -; mRNA.
DR EMBL; AF128195; AAF22536.1; -; mRNA.
DR EMBL; AF128196; AAF22537.1; -; mRNA.
DR EMBL; AF128197; AAF22538.1; -; mRNA.
DR EMBL; AF128198; AAF22539.1; -; mRNA.
DR EMBL; AF128199; AAF22540.1; -; mRNA.
DR EMBL; AF128200; AAF22541.1; -; mRNA.
DR EMBL; AF128201; AAF22542.1; -; mRNA.
DR EMBL; AF128202; AAF22543.1; -; mRNA.
DR EMBL; AF128203; AAF22544.1; -; mRNA.
DR EMBL; AF128204; AAF22545.1; -; mRNA.
DR EMBL; AB051897; BAB18730.1; -; Genomic_DNA.
DR EMBL; AL596122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25170.1; -.
DR RefSeq; NP_035468.1; NM_011338.2.
DR AlphaFoldDB; P51670; -.
DR SMR; P51670; -.
DR DIP; DIP-5921N; -.
DR STRING; 10090.ENSMUSP00000019266; -.
DR iPTMnet; P51670; -.
DR PhosphoSitePlus; P51670; -.
DR PaxDb; P51670; -.
DR PeptideAtlas; P51670; -.
DR PRIDE; P51670; -.
DR ProteomicsDB; 281249; -.
DR DNASU; 20308; -.
DR Ensembl; ENSMUST00000019266; ENSMUSP00000019266; ENSMUSG00000019122.
DR GeneID; 20308; -.
DR KEGG; mmu:20308; -.
DR UCSC; uc007kpj.1; mouse.
DR CTD; 20308; -.
DR MGI; MGI:104533; Ccl9.
DR VEuPathDB; HostDB:ENSMUSG00000019122; -.
DR eggNOG; ENOG502TJX7; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_1_1; -.
DR InParanoid; P51670; -.
DR OMA; RKIRCEN; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P51670; -.
DR TreeFam; TF334888; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
DR BioGRID-ORCS; 20308; 1 hit in 74 CRISPR screens.
DR PRO; PR:P51670; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P51670; protein.
DR Bgee; ENSMUSG00000019122; Expressed in stroma of bone marrow and 141 other tissues.
DR ExpressionAtlas; P51670; baseline and differential.
DR Genevisible; P51670; MM.
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; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; 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:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
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 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 Chemotaxis; Cytokine; Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..122
FT /note="C-C motif chemokine 9"
FT /id="PRO_0000005192"
FT CHAIN 50..122
FT /note="CCL9(29-101)"
FT /id="PRO_0000041865"
FT CHAIN 51..122
FT /note="CCL9(30-101)"
FT /id="PRO_0000041866"
FT CHAIN 52..122
FT /note="CCL9(31-101)"
FT /id="PRO_0000041867"
FT DISULFID 57..80
FT /evidence="ECO:0000250"
FT DISULFID 58..96
FT /evidence="ECO:0000250"
FT DISULFID 67..107
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="Q -> K (in Ref. 1; AAB02198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 13871 MW; 9075F1FFEEFD30F7 CRC64;
MKPFHTALSF LILTTALGIW AQITHATETK EVQSSLKAQQ GLEIEMFHMG FQDSSDCCLS
YNSRIQCSRF IGYFPTSGGC TRPGIIFISK RGFQVCANPS DRRVQRCIER LEQNSQPRTY
KQ
