CCL3_MOUSE
ID CCL3_MOUSE Reviewed; 92 AA.
AC P10855; P14096;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=C-C motif chemokine 3;
DE AltName: Full=Heparin-binding chemotaxis protein;
DE AltName: Full=L2G25B;
DE AltName: Full=Macrophage inflammatory protein 1-alpha;
DE Short=MIP-1-alpha;
DE AltName: Full=SIS-alpha;
DE AltName: Full=Small-inducible cytokine A3;
DE AltName: Full=TY-5;
DE Flags: Precursor;
GN Name=Ccl3; Synonyms=Mip1a, Scya3;
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.
RX PubMed=3290382; DOI=10.1084/jem.167.6.1939;
RA Davatelis G., Tekamp-Olson P., Wolpe S.D., Hermsen K., Luedke C.,
RA Gallegos C., Coit D., Merryweather J., Cerami A.;
RT "Cloning and characterization of a cDNA for murine macrophage inflammatory
RT protein (MIP), a novel monokine with inflammatory and chemokinetic
RT properties.";
RL J. Exp. Med. 167:1939-1944(1988).
RN [2]
RP ERRATUM OF PUBMED:3290382, AND SEQUENCE REVISION.
RA Davatelis G., Tekamp-Olson P., Wolpe S.D., Hermsen K., Luedke C.,
RA Gallegos C., Coit D., Merryweather J., Cerami A.;
RL J. Exp. Med. 170:2189-2189(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2521353;
RA Brown K.D., Zurawski S.M., Mosmann T.R., Zurawski G.;
RT "A family of small inducible proteins secreted by leukocytes are members of
RT a new superfamily that includes leukocyte and fibroblast-derived
RT inflammatory agents, growth factors, and indicators of various activation
RT processes.";
RL J. Immunol. 142:679-687(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J;
RX PubMed=2216738; DOI=10.1093/nar/18.18.5561;
RA Grove M., Lowe S., Graham G., Pragnell I., Plumb M.;
RT "Sequence of the murine haemopoietic stem cell inhibitor/macrophage
RT inflammatory protein 1 alpha gene.";
RL Nucleic Acids Res. 18:5561-5561(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2784565; DOI=10.1073/pnas.86.6.1963;
RA Kwon B.S., Weissman S.M.;
RT "cDNA sequences of two inducible T-cell genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1963-1967(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2033269;
RA Widmer U., Yang Z., van Deventer S., Manogue K.R., Sherry B., Cerami A.;
RT "Genomic structure of murine macrophage inflammatory protein-1 alpha and
RT conservation of potential regulatory sequences with a human homolog,
RT LD78.";
RL J. Immunol. 146:4031-4040(1991).
RN [7]
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 [8]
RP PROTEIN SEQUENCE OF 24-42.
RX PubMed=3279154; DOI=10.1084/jem.167.2.570;
RA Wolpe S.D., Davatelis G., Sherry B., Beutler B., Hesse D.G., Nguyen H.T.,
RA Moldawer L.L., Nathan C.F., Lowry S.F., Cerami A.;
RT "Macrophages secrete a novel heparin-binding protein with inflammatory and
RT neutrophil chemokinetic properties.";
RL J. Exp. Med. 167:570-581(1988).
CC -!- FUNCTION: Monokine with inflammatory, pyrogenic and chemokinetic
CC properties. Has a potent chemotactic activity for eosinophils. Binding
CC to a high-affinity receptor activates calcium release in neutrophils.
CC -!- INTERACTION:
CC P10855; E9M5R0: RHVP.R17; Xeno; NbExp=4; IntAct=EBI-16188162, EBI-16188152;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in lung, spleen, and pancreas.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; M23447; AAA40146.1; -; mRNA.
DR EMBL; X12531; CAA31047.1; -; mRNA.
DR EMBL; X53372; CAA37452.1; -; Genomic_DNA.
DR EMBL; J04491; AAA40304.1; -; mRNA.
DR EMBL; M73061; AAA39707.1; -; Genomic_DNA.
DR EMBL; AF065939; AAC17506.1; -; mRNA.
DR EMBL; AF065940; AAC17507.1; -; mRNA.
DR EMBL; AF065941; AAC17508.1; -; mRNA.
DR EMBL; AF065942; AAC17509.1; -; mRNA.
DR EMBL; AF065943; AAC17510.1; -; mRNA.
DR CCDS; CCDS36255.1; -.
DR PIR; S11685; A32393.
DR RefSeq; NP_035467.1; NM_011337.2.
DR PDB; 4ZLT; X-ray; 3.00 A; F/L=24-92.
DR PDBsum; 4ZLT; -.
DR AlphaFoldDB; P10855; -.
DR SMR; P10855; -.
DR BioGRID; 203127; 1.
DR DIP; DIP-61916N; -.
DR IntAct; P10855; 1.
DR STRING; 10090.ENSMUSP00000001008; -.
DR PaxDb; P10855; -.
DR PeptideAtlas; P10855; -.
DR PRIDE; P10855; -.
DR DNASU; 20302; -.
DR Ensembl; ENSMUST00000001008; ENSMUSP00000001008; ENSMUSG00000000982.
DR GeneID; 20302; -.
DR KEGG; mmu:20302; -.
DR UCSC; uc007kpn.1; mouse.
DR CTD; 6348; -.
DR MGI; MGI:98260; Ccl3.
DR VEuPathDB; HostDB:ENSMUSG00000000982; -.
DR eggNOG; ENOG502SAF0; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_2_1; -.
DR InParanoid; P10855; -.
DR OMA; MKTSQRC; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P10855; -.
DR TreeFam; TF334888; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR BioGRID-ORCS; 20302; 7 hits in 76 CRISPR screens.
DR PRO; PR:P10855; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P10855; protein.
DR Bgee; ENSMUSG00000000982; Expressed in granulocyte and 43 other tissues.
DR ExpressionAtlas; P10855; baseline and differential.
DR Genevisible; P10855; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; ISS:UniProtKB.
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:0031730; F:CCR5 chemokine receptor binding; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISS:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0016004; F:phospholipase activator activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0043615; P:astrocyte cell migration; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0019722; P:calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0001775; P:cell activation; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
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; ISS:UniProtKB.
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:0006935; P:chemotaxis; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0043308; P:eosinophil degranulation; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048247; P:lymphocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; IGI:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:UniProtKB.
DR GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IGI:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070723; P:response to cholesterol; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0023052; P:signaling; ISS:UniProtKB.
DR GO; GO:0010818; P:T cell chemotaxis; ISS:UniProtKB.
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; Inflammatory response; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3279154"
FT CHAIN 24..92
FT /note="C-C motif chemokine 3"
FT /id="PRO_0000005158"
FT DISULFID 34..57
FT /evidence="ECO:0000250|UniProtKB:P10147"
FT DISULFID 35..73
FT /evidence="ECO:0000250|UniProtKB:P10147"
FT CONFLICT 22
FT /note="F -> L (in Ref. 3; AAA40146)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="V -> A (in Ref. 3; AAA40146)"
FT /evidence="ECO:0000305"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4ZLT"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4ZLT"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4ZLT"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4ZLT"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:4ZLT"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4ZLT"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:4ZLT"
SQ SEQUENCE 92 AA; 10345 MW; 8BFF2DE7C6DEDD38 CRC64;
MKVSTTALAV LLCTMTLCNQ VFSAPYGADT PTACCFSYSR KIPRQFIVDY FETSSLCSQP
GVIFLTKRNR QICADSKETW VQEYITDLEL NA
