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CCL1_MOUSE
ID   CCL1_MOUSE              Reviewed;          92 AA.
AC   P10146; P14098; Q9QUR9; Q9QUS5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=C-C motif chemokine 1;
DE   AltName: Full=P500;
DE   AltName: Full=SIS-epsilon;
DE   AltName: Full=Small-inducible cytokine A1;
DE   AltName: Full=T-cell activation protein 3;
DE            Short=TCA-3;
DE            Short=TCA3;
DE   Flags: Precursor;
GN   Name=Ccl1; Synonyms=Scya1, Tca3;
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] (ISOFORM 1).
RX   PubMed=3499466;
RA   Burd P.R., Freeman G.J., Wilson S.D., Berman M., Dekruyff R.,
RA   Billings P.R., Dorf M.E.;
RT   "Cloning and characterization of a novel T cell activation gene.";
RL   J. Immunol. 139:3126-3131(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA   Wilson S.D., Billings P.R., D'Eustachio P., Fournier R., Gessler E.,
RA   Lalley P.A., Burd P.R., Housman D.E., Taylor B.A., Dorf M.E.;
RT   "Molecular and functional characterization of TCA3: a novel inflammatory
RT   cytokine.";
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=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 [MRNA] OF 1-76 (ISOFORM 1), POLYMORPHISM, AND VARIANTS
RP   THR-36; ILE-64; LYS-68 AND ASP-70.
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).
CC   -!- FUNCTION: Cytokine that is chemotactic for neutrophils.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=TCA3;
CC         IsoId=P10146-1; Sequence=Displayed;
CC       Name=2; Synonyms=P500, SIS-epsilon;
CC         IsoId=P10146-2; Sequence=VSP_001059;
CC   -!- INDUCTION: Produced by T-cell after stimulation by antigen or induction
CC       by concanavalin a (Con-A).
CC   -!- POLYMORPHISM: The polymorphisms in strains DBA/2J and SJL/J may be
CC       associated with severity of clinical symptoms of experimental allergic
CC       encephalomyelitis, an animal model of multiple sclerosis, and
CC       susceptibility to the monophasic remitting/nonrelapsing form of the
CC       disease. {ECO:0000269|PubMed:10438970}.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
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DR   EMBL; M17957; AAB39499.1; -; mRNA.
DR   EMBL; M23501; AAA40147.1; -; mRNA.
DR   EMBL; X52401; CAB57869.1; -; Genomic_DNA.
DR   EMBL; AK019040; BAB31521.1; -; mRNA.
DR   EMBL; AF065924; AAF15374.1; -; mRNA.
DR   EMBL; AF065925; AAF15375.1; -; mRNA.
DR   EMBL; AF065926; AAF15376.1; -; mRNA.
DR   EMBL; AF065927; AAF15377.1; -; mRNA.
DR   EMBL; AF065928; AAF15378.1; -; mRNA.
DR   CCDS; CCDS36249.1; -. [P10146-1]
DR   PIR; S24236; S24236.
DR   RefSeq; NP_035459.1; NM_011329.3. [P10146-1]
DR   AlphaFoldDB; P10146; -.
DR   SMR; P10146; -.
DR   BioGRID; 203116; 2.
DR   STRING; 10090.ENSMUSP00000103824; -.
DR   GlyGen; P10146; 1 site.
DR   PaxDb; P10146; -.
DR   PRIDE; P10146; -.
DR   DNASU; 20290; -.
DR   Ensembl; ENSMUST00000108189; ENSMUSP00000103824; ENSMUSG00000020702. [P10146-1]
DR   GeneID; 20290; -.
DR   KEGG; mmu:20290; -.
DR   UCSC; uc007kmu.1; mouse. [P10146-1]
DR   CTD; 6346; -.
DR   MGI; MGI:98258; Ccl1.
DR   VEuPathDB; HostDB:ENSMUSG00000020702; -.
DR   eggNOG; ENOG502SZRS; Eukaryota.
DR   GeneTree; ENSGT01030000234760; -.
DR   HOGENOM; CLU_141716_5_0_1; -.
DR   InParanoid; P10146; -.
DR   OMA; MHVSSSN; -.
DR   PhylomeDB; P10146; -.
DR   TreeFam; TF334888; -.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 20290; 4 hits in 71 CRISPR screens.
DR   PRO; PR:P10146; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P10146; protein.
DR   Bgee; ENSMUSG00000020702; Expressed in peripheral lymph node and 18 other tissues.
DR   ExpressionAtlas; P10146; baseline and differential.
DR   Genevisible; P10146; MM.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0008009; F:chemokine activity; ISO:MGI.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; 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:0097398; P:cellular response to interleukin-17; IDA:MGI.
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; IDA:MGI.
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:0031640; P:killing of cells of another organism; ISO:MGI.
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:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
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   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR   GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
DR   GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
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   2: Evidence at transcript level;
KW   Alternative splicing; Chemotaxis; Cytokine; Disulfide bond; Glycoprotein;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..92
FT                   /note="C-C motif chemokine 1"
FT                   /id="PRO_0000005142"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..92
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         65..86
FT                   /note="FRLNKGRESCASTNKTWVQNHL -> VRSSGVPGLTEAEKTVTDSSE (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:2521353"
FT                   /id="VSP_001059"
FT   VARIANT         36
FT                   /note="N -> T (in strain: DBA/2J and SJL/J)"
FT                   /evidence="ECO:0000269|PubMed:10438970"
FT   VARIANT         64
FT                   /note="V -> I (in strain: DBA/2J and SJL/J)"
FT                   /evidence="ECO:0000269|PubMed:10438970"
FT   VARIANT         68
FT                   /note="N -> K (in strain: DBA/2J and SJL/J)"
FT                   /evidence="ECO:0000269|PubMed:10438970"
FT   VARIANT         70
FT                   /note="G -> D (in strain: DBA/2J and SJL/J)"
FT                   /evidence="ECO:0000269|PubMed:10438970"
FT   CONFLICT        26
FT                   /note="M -> V (in Ref. 3; CAB57869)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   92 AA;  10276 MW;  BF057DEAA1771096 CRC64;
     MKPTAMALMC LLLAAVWIQD VDSKSMLTVS NSCCLNTLKK ELPLKFIQCY RKMGSSCPDP
     PAVVFRLNKG RESCASTNKT WVQNHLKKVN PC
 
 
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