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C-C motif chemokine 6 (Protein C10) (Small-inducible cytokine A6) [Cleaved into: CCL6(22-95); CCL6(23-95)]

 CCL6_MOUSE              Reviewed;         116 AA.
P27784; Q3U3W3; Q5QNW1; Q99M24; Q9D830;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
28-FEB-2018, entry version 142.
RecName: Full=C-C motif chemokine 6;
AltName: Full=Protein C10;
AltName: Full=Small-inducible cytokine A6;
Contains:
RecName: Full=CCL6(22-95);
Contains:
RecName: Full=CCL6(23-95);
Flags: Precursor;
Name=Ccl6; Synonyms=C10, Scya6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CBA/J; TISSUE=Bone marrow;
PubMed=1832565;
Orlofsky A., Berger M.S., Prystowsky M.B.;
"Novel expression pattern of a new member of the MIP-1 family of
cytokine-like genes.";
Cell Regul. 2:403-412(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=B10.S/J, BALB/cJ, DBA/2J, NOD/LtJ, and SJL/J; TISSUE=Spleen;
PubMed=10438970;
Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W.,
Blankenhorn E.P.;
"Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2
(monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are
candidates for eae7, a locus controlling susceptibility to monophasic
remitting/nonrelapsing experimental allergic encephalomyelitis.";
J. Immunol. 163:2262-2266(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Sv;
Nomiyama H.;
"Organization of the mouse CC chemokine cluster containing the genes
for C10, MRP-2 and RANTES.";
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION OF CCL6(22-95) AND CCL6(23-95), PROTEOLYTIC PROCESSING
OF N-TERMINAL, AND FUNCTION.
PubMed=15905581; DOI=10.4049/jimmunol.174.11.7341;
Berahovich R.D., Miao Z., Wang Y., Premack B., Howard M.C.,
Schall T.J.;
"Proteolytic activation of alternative CCR1 ligands in inflammation.";
J. Immunol. 174:7341-7351(2005).
-!- FUNCTION: CCL6(22-95) and CCL6(23-95) are potent chemoattractants.
{ECO:0000269|PubMed:15905581}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in myelopoietic bone marrow cultures
stimulated by GM-CSF.
-!- INDUCTION: Associated with stimuli that promote myeloid
differentiation.
-!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M58004; AAA37329.1; -; mRNA.
EMBL; AF128188; AAF22529.1; -; mRNA.
EMBL; AF128189; AAF22530.1; -; mRNA.
EMBL; AF128190; AAF22531.1; -; mRNA.
EMBL; AF128191; AAF22532.1; -; mRNA.
EMBL; AF128192; AAF22533.1; -; mRNA.
EMBL; AB051897; BAB18729.1; -; Genomic_DNA.
EMBL; AK002697; BAB22291.1; -; mRNA.
EMBL; AK008547; BAB25734.1; -; mRNA.
EMBL; AK150336; BAE29478.1; -; mRNA.
EMBL; AK154553; BAE32672.1; -; mRNA.
EMBL; AL596122; CAI25134.1; -; Genomic_DNA.
EMBL; BC002073; AAH02073.1; -; mRNA.
CCDS; CCDS25171.1; -.
PIR; I49555; I49555.
RefSeq; NP_033165.1; NM_009139.3.
UniGene; Mm.137; -.
ProteinModelPortal; P27784; -.
SMR; P27784; -.
STRING; 10090.ENSMUSP00000019071; -.
iPTMnet; P27784; -.
PhosphoSitePlus; P27784; -.
MaxQB; P27784; -.
PaxDb; P27784; -.
PeptideAtlas; P27784; -.
PRIDE; P27784; -.
Ensembl; ENSMUST00000019071; ENSMUSP00000019071; ENSMUSG00000018927.
GeneID; 20305; -.
KEGG; mmu:20305; -.
UCSC; uc007kpm.1; mouse.
CTD; 20305; -.
MGI; MGI:98263; Ccl6.
eggNOG; ENOG410J4DG; Eukaryota.
eggNOG; ENOG4111C2C; LUCA.
GeneTree; ENSGT00910000144306; -.
HOGENOM; HOG000036685; -.
HOVERGEN; HBG017871; -.
InParanoid; P27784; -.
KO; K05510; -.
OMA; SDCCFSY; -.
OrthoDB; EOG091G14Y2; -.
PhylomeDB; P27784; -.
TreeFam; TF334888; -.
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
ChiTaRS; Ccl6; mouse.
PRO; PR:P27784; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018927; -.
CleanEx; MM_CCL6; -.
Genevisible; P27784; MM.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
InterPro; IPR000827; Chemokine_CC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR036048; Interleukin_8-like_sf.
Pfam; PF00048; IL8; 1.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
1: Evidence at protein level;
Chemotaxis; Complete proteome; Cytokine; Disulfide bond;
Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 116 C-C motif chemokine 6.
/FTId=PRO_0000005182.
CHAIN 43 116 CCL6(22-95).
/FTId=PRO_0000041844.
CHAIN 44 116 CCL6(23-95).
/FTId=PRO_0000041845.
DISULFID 50 73 {ECO:0000250}.
DISULFID 51 89 {ECO:0000250}.
DISULFID 60 100 {ECO:0000250}.
CONFLICT 43 43 F -> V (in Ref. 6; AAH02073).
{ECO:0000305}.
CONFLICT 93 93 S -> R (in Ref. 4; BAB25734).
{ECO:0000305}.
CONFLICT 111 111 G -> R (in Ref. 6; AAH02073).
{ECO:0000305}.
SEQUENCE 116 AA; 12984 MW; 2B483B5DE8417082 CRC64;
MRNSKTAISF FILVAVLGSQ AGLIQEMEKE DRRYNPPIIH QGFQDTSSDC CFSYATQIPC
KRFIYYFPTS GGCIKPGIIF ISRRGTQVCA DPSDRRVQRC LSTLKQGPRS GNKVIA


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