CCL6_MOUSE
ID CCL6_MOUSE Reviewed; 116 AA.
AC P27784; Q3U3W3; Q5QNW1; Q99M24; Q9D830;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=C-C motif chemokine 6;
DE AltName: Full=Protein C10;
DE AltName: Full=Small-inducible cytokine A6;
DE Contains:
DE RecName: Full=CCL6(22-95);
DE Contains:
DE RecName: Full=CCL6(23-95);
DE Flags: Precursor;
GN Name=Ccl6; Synonyms=C10, Scya6;
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].
RC STRAIN=CBA/J; TISSUE=Bone marrow;
RX PubMed=1832565; DOI=10.1091/mbc.2.5.403;
RA Orlofsky A., Berger M.S., Prystowsky M.B.;
RT "Novel expression pattern of a new member of the MIP-1 family of cytokine-
RT like genes.";
RL Cell Regul. 2:403-412(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and 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 [5]
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 [6]
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).
RN [7]
RP IDENTIFICATION OF CCL6(22-95) AND CCL6(23-95), PROTEOLYTIC PROCESSING OF
RP N-TERMINAL, AND FUNCTION.
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: CCL6(22-95) and CCL6(23-95) are potent chemoattractants.
CC {ECO:0000269|PubMed:15905581}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in myelopoietic bone marrow cultures
CC stimulated by GM-CSF.
CC -!- INDUCTION: Associated with stimuli that promote myeloid
CC differentiation.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; M58004; AAA37329.1; -; mRNA.
DR EMBL; AF128188; AAF22529.1; -; mRNA.
DR EMBL; AF128189; AAF22530.1; -; mRNA.
DR EMBL; AF128190; AAF22531.1; -; mRNA.
DR EMBL; AF128191; AAF22532.1; -; mRNA.
DR EMBL; AF128192; AAF22533.1; -; mRNA.
DR EMBL; AB051897; BAB18729.1; -; Genomic_DNA.
DR EMBL; AK002697; BAB22291.1; -; mRNA.
DR EMBL; AK008547; BAB25734.1; -; mRNA.
DR EMBL; AK150336; BAE29478.1; -; mRNA.
DR EMBL; AK154553; BAE32672.1; -; mRNA.
DR EMBL; AL596122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002073; AAH02073.1; -; mRNA.
DR CCDS; CCDS25171.1; -.
DR PIR; I49555; I49555.
DR RefSeq; NP_033165.1; NM_009139.3.
DR AlphaFoldDB; P27784; -.
DR SMR; P27784; -.
DR STRING; 10090.ENSMUSP00000019071; -.
DR iPTMnet; P27784; -.
DR PhosphoSitePlus; P27784; -.
DR MaxQB; P27784; -.
DR PaxDb; P27784; -.
DR PeptideAtlas; P27784; -.
DR PRIDE; P27784; -.
DR ProteomicsDB; 265613; -.
DR DNASU; 20305; -.
DR Ensembl; ENSMUST00000019071; ENSMUSP00000019071; ENSMUSG00000018927.
DR GeneID; 20305; -.
DR KEGG; mmu:20305; -.
DR UCSC; uc007kpm.1; mouse.
DR CTD; 20305; -.
DR MGI; MGI:98263; Ccl6.
DR VEuPathDB; HostDB:ENSMUSG00000018927; -.
DR eggNOG; ENOG502TJX7; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_1_1; -.
DR InParanoid; P27784; -.
DR OMA; RFIYYFP; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P27784; -.
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; 20305; 0 hits in 72 CRISPR screens.
DR PRO; PR:P27784; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P27784; protein.
DR Bgee; ENSMUSG00000018927; Expressed in granulocyte and 157 other tissues.
DR Genevisible; P27784; 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:0060326; P:cell chemotaxis; 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: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..116
FT /note="C-C motif chemokine 6"
FT /id="PRO_0000005182"
FT CHAIN 43..116
FT /note="CCL6(22-95)"
FT /id="PRO_0000041844"
FT CHAIN 44..116
FT /note="CCL6(23-95)"
FT /id="PRO_0000041845"
FT DISULFID 50..73
FT /evidence="ECO:0000250"
FT DISULFID 51..89
FT /evidence="ECO:0000250"
FT DISULFID 60..100
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="F -> V (in Ref. 6; AAH02073)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="S -> R (in Ref. 4; BAB25734)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> R (in Ref. 6; AAH02073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 116 AA; 12984 MW; 2B483B5DE8417082 CRC64;
MRNSKTAISF FILVAVLGSQ AGLIQEMEKE DRRYNPPIIH QGFQDTSSDC CFSYATQIPC
KRFIYYFPTS GGCIKPGIIF ISRRGTQVCA DPSDRRVQRC LSTLKQGPRS GNKVIA
