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CXCL5_MOUSE
ID   CXCL5_MOUSE             Reviewed;         132 AA.
AC   P50228; Q8K3I3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=C-X-C motif chemokine 5;
DE   AltName: Full=Cytokine LIX;
DE   AltName: Full=Small-inducible cytokine B5;
DE   Contains:
DE     RecName: Full=GCP-2(1-78);
DE   Contains:
DE     RecName: Full=GCP-2(9-78);
DE   Flags: Precursor;
GN   Name=Cxcl5; Synonyms=Scyb5;
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=7622488; DOI=10.1074/jbc.270.28.16756;
RA   Smith J.B., Herschman H.R.;
RT   "Glucocorticoid-attenuated response genes encode intercellular mediators,
RT   including a new C-X-C chemokine.";
RL   J. Biol. Chem. 270:16756-16765(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=12439624; DOI=10.1007/s00251-002-0501-5;
RA   Smith J.B., Wadleigh D.J., Xia Y.-R., Mar R.A., Herschman H.R., Lusis A.J.;
RT   "Cloning and genomic localization of the murine LPS-induced CXC chemokine
RT   (LIX) gene, Scyb5.";
RL   Immunogenetics 54:599-603(2002).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; 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   [5]
RP   PROTEIN SEQUENCE OF 41-118, IDENTIFICATION OF GCP-2(1-78), AND PROTEOLYTIC
RP   PROCESSING OF N-TERMINUS.
RX   PubMed=8759763;
RA   Wuyts A., Haelens A., Proost P., Lenaerts J.-P., Conings R., Opdenakker G.,
RA   Van Damme J.;
RT   "Identification of mouse granulocyte chemotactic protein-2 from fibroblasts
RT   and epithelial cells. Functional comparison with natural KC and macrophage
RT   inflammatory protein-2.";
RL   J. Immunol. 157:1736-1743(1996).
RN   [6]
RP   PROTEIN SEQUENCE OF 49-55, IDENTIFICATION OF GCP-2(9-78) BY MASS
RP   SPECTROMETRY, FUNCTION, AND PROTEOLYTIC PROCESSING OF N-TERMINUS AND
RP   C-TERMINAL.
RC   TISSUE=Fibroblast;
RX   PubMed=10570306;
RA   Wuyts A., D'Haese A., Cremers V., Menten P., Lenaerts J.-P., De Loof A.,
RA   Heremans H., Proost P., Van Damme J.;
RT   "NH2- and COOH-terminal truncations of murine granulocyte chemotactic
RT   protein-2 augment the in vitro and in vivo neutrophil chemotactic
RT   potency.";
RL   J. Immunol. 163:6155-6163(1999).
CC   -!- FUNCTION: May participate in the recruitment of inflammatory cells by
CC       injured or infected tissue. GCP-2(1-78) and, more potent, GCP-2(9-78)
CC       attract neutrophils and are involved in neutrophil activation.
CC       {ECO:0000269|PubMed:10570306}.
CC   -!- SUBUNIT: Monomer. Homodimer. {ECO:0000250|UniProtKB:P42830}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- INDUCTION: By lipopolysaccharide (LPS).
CC   -!- PTM: GCP-2(1-78) and GCP-2(9-78) are produced by proteolytic cleavage
CC       after secretion from fibroblasts and epithelial cells. GCP-2(9-78) is
CC       the most prominent form. A number of additional N-terminal (processed
CC       between pos. 41 and 48) and C-terminal (processed between pos. 118 and
CC       132) processed forms have been identified, probably also representing
CC       intermediate states. {ECO:0000269|PubMed:10570306,
CC       ECO:0000269|PubMed:8759763}.
CC   -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC       {ECO:0000305}.
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DR   EMBL; U27267; AAC52238.1; -; mRNA.
DR   EMBL; AY100019; AAM48589.1; -; Genomic_DNA.
DR   EMBL; AC105995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC024392; AAH24392.1; -; mRNA.
DR   CCDS; CCDS19414.1; -.
DR   PIR; A57325; A57325.
DR   RefSeq; NP_033167.2; NM_009141.3.
DR   AlphaFoldDB; P50228; -.
DR   SMR; P50228; -.
DR   STRING; 10090.ENSMUSP00000031318; -.
DR   iPTMnet; P50228; -.
DR   PhosphoSitePlus; P50228; -.
DR   PaxDb; P50228; -.
DR   PRIDE; P50228; -.
DR   ProteomicsDB; 279221; -.
DR   ABCD; P50228; 2 sequenced antibodies.
DR   Antibodypedia; 13323; 277 antibodies from 22 providers.
DR   DNASU; 20311; -.
DR   Ensembl; ENSMUST00000031318; ENSMUSP00000031318; ENSMUSG00000029371.
DR   GeneID; 20311; -.
DR   KEGG; mmu:20311; -.
DR   UCSC; uc008ybg.2; mouse.
DR   CTD; 6374; -.
DR   MGI; MGI:1096868; Cxcl5.
DR   VEuPathDB; HostDB:ENSMUSG00000029371; -.
DR   eggNOG; ENOG502S7MM; Eukaryota.
DR   GeneTree; ENSGT00940000162749; -.
DR   HOGENOM; CLU_143902_1_0_1; -.
DR   InParanoid; P50228; -.
DR   OMA; KELRCTC; -.
DR   OrthoDB; 1556509at2759; -.
DR   PhylomeDB; P50228; -.
DR   TreeFam; TF333433; -.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 20311; 2 hits in 75 CRISPR screens.
DR   PRO; PR:P50228; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P50228; protein.
DR   Bgee; ENSMUSG00000029371; Expressed in right lobe of liver and 59 other tissues.
DR   Genevisible; P50228; MM.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0008009; F:chemokine activity; ISO:MGI.
DR   GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR   GO; GO:0001776; P:leukocyte homeostasis; IMP:MGI.
DR   GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR   GO; GO:0032642; P:regulation of chemokine production; IMP:MGI.
DR   GO; GO:0070951; P:regulation of neutrophil mediated killing of gram-negative bacterium; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   CDD; cd00273; Chemokine_CXC; 1.
DR   InterPro; IPR001089; Chemokine_CXC.
DR   InterPro; IPR018048; Chemokine_CXC_CS.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   InterPro; IPR033899; CXC_Chemokine_domain.
DR   InterPro; IPR036048; Interleukin_8-like_sf.
DR   PANTHER; PTHR10179; PTHR10179; 1.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR00437; SMALLCYTKCXC.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; SSF54117; 1.
DR   PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
PE   1: Evidence at protein level;
KW   Chemotaxis; Cytokine; Direct protein sequencing; Disulfide bond;
KW   Inflammatory response; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000269|PubMed:8759763"
FT   CHAIN           41..132
FT                   /note="C-X-C motif chemokine 5"
FT                   /id="PRO_0000005078"
FT   CHAIN           41..118
FT                   /note="GCP-2(1-78)"
FT                   /id="PRO_0000005079"
FT   CHAIN           49..118
FT                   /note="GCP-2(9-78)"
FT                   /id="PRO_0000005080"
FT   DISULFID        53..79
FT                   /evidence="ECO:0000250|UniProtKB:P42830"
FT   DISULFID        55..95
FT                   /evidence="ECO:0000250|UniProtKB:P42830"
FT   CONFLICT        10
FT                   /note="R -> H (in Ref. 1; AAC52238 and 4; AAH24392)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="I -> S (in Ref. 1; AAC52238 and 4; AAH24392)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81..82
FT                   /note="TV -> N (in Ref. 5; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   132 AA;  14235 MW;  B7E9C4E6094DE365 CRC64;
     MSLQLRSSAR IPSGSISPFM RMAPLAFLLL FTLPQHLAEA APSSVIAATE LRCVCLTVTP
     KINPKLIANL EVIPAGPQCP TVEVIAKLKN QKEVCLDPEA PVIKKIIQKI LGSDKKKAKR
     NALAVERTAS VQ
 
 
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