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   24-JAN-2024, entry version 167.
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 {ECO:0000303|PubMed:8597875};
DE   AltName: Full=Macrophage inflammatory protein-related protein 2 {ECO:0000303|PubMed:7650394};
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   -!- PTM: The N-terminal is proteolytically cleaved by proteases associated
CC       with inflammatory responses. The processed forms CCL9(29-101), CCL9(30-
CC       101) and CCL9(31-101) exhibit increase in CCR1-mediated signaling and
CC       chemotaxis assays in vitro. {ECO:0000269|PubMed:15905581}.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 10090-ENSMUSP00000019266; -.
DR   PeptideAtlas; P51670; -.
DR   ProteomicsDB; 281249; -.
DR   DNASU; 20308; -.
DR   Ensembl; ENSMUST00000019266.6; ENSMUSP00000019266.6; ENSMUSG00000019122.9.
DR   GeneID; 20308; -.
DR   KEGG; mmu:20308; -.
DR   UCSC; uc007kpj.1; mouse.
DR   AGR; MGI:104533; -.
DR   CTD; 20308; -.
DR   MGI; MGI:104533; Ccl9.
DR   VEuPathDB; HostDB:ENSMUSG00000019122; -.
DR   eggNOG; ENOG502TJX7; Eukaryota.
DR   GeneTree; ENSGT01100000263482; -.
DR   HOGENOM; CLU_141716_4_1_1; -.
DR   InParanoid; P51670; -.
DR   OMA; KIGPQMT; -.
DR   OrthoDB; 4265193at2759; -.
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 79 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 142 other cell types or tissues.
DR   ExpressionAtlas; P51670; baseline and differential.
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: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:0071346; P:cellular response to type II interferon; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0048245; P:eosinophil chemotaxis; 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:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR   CDD; cd00272; Chemokine_CC; 1.
DR   Gene3D; 2.40.50.40; -; 1.
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:SF77; C-C MOTIF CHEMOKINE 15; 1.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   Pfam; PF00048; IL8; 1.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 1.
DR   PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
DR   Genevisible; P51670; MM.
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                   /evidence="ECO:0000269|PubMed:15905581"
FT                   /id="PRO_0000041865"
FT   CHAIN           51..122
FT                   /note="CCL9(30-101)"
FT                   /evidence="ECO:0000269|PubMed:15905581"
FT                   /id="PRO_0000041866"
FT   CHAIN           52..122
FT                   /note="CCL9(31-101)"
FT                   /evidence="ECO:0000269|PubMed:15905581"
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
//