ID IL8_CANLF Reviewed; 101 AA.
AC P41324;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Interleukin-8;
DE Short=IL-8;
DE AltName: Full=C-X-C motif chemokine 8;
DE AltName: Full=Chemokine (C-X-C motif) ligand 8;
DE Flags: Precursor;
GN Name=CXCL8; Synonyms=IL8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916715; DOI=10.1016/0378-1119(93)90313-r;
RA Ishikawa J., Suzuki S., Hotta K., Hirota Y., Mizuno S., Suzuki K.;
RT "Cloning of a canine gene homologous to the human interleukin-8-encoding
RT gene.";
RL Gene 131:305-306(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymph node;
RX PubMed=7827282; DOI=10.1016/1043-4666(94)90071-x;
RA Matsumoto Y., Mohamed A., Onodera T., Kato H., Ohashi T., Goitsuka R.,
RA Tsujimoto H., Hasegawa A., Furusawa S., Yoshihara K., Ishikawa J.,
RA Hotta K., Suzuki K., Hirota Y.;
RT "Molecular cloning and expression of canine interleukin 8 cDNA.";
RL Cytokine 6:455-461(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Mongrel; TISSUE=Jugular vein;
RX PubMed=7814650; DOI=10.1172/jci117680;
RA Kukielka G.L., Smith W.C., Larosa G.J., Manning A.M., Mendoza L.H.,
RA Daly T.J., Hughes B.J., Youker K.A., Hawkins H.K., Michael L.H., Rot A.,
RA Entman M.L.;
RT "Interleukin-8 gene induction in the myocardium after ischemia and
RT reperfusion in vivo.";
RL J. Clin. Invest. 95:89-103(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle;
RX PubMed=9119462; DOI=10.1128/iai.65.4.1273-1285.1997;
RA Straubinger R.K., Straubinger A.F., Harter L., Jacobson R.H., Chang Y.-F.,
RA Summers B.A., Erb H.N., Appel M.J.;
RT "Borrelia burgdorferi migrates into joint capsules and causes an up-
RT regulation of interleukin-8 in synovial membranes of dogs experimentally
RT infected with ticks.";
RL Infect. Immun. 65:1273-1285(1997).
CC -!- FUNCTION: Chemotactic factor that mediates inflammatory response by
CC attracting neutrophils, basophils, and T-cells to clear pathogens and
CC protect the host from infection. Also plays an important role in
CC neutrophil activation. Released in response to an inflammatory
CC stimulus, exerts its effect by binding to the G-protein-coupled
CC receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes
CC and endothelial cells. G-protein heterotrimer (alpha, beta, gamma
CC subunits) constitutively binds to CXCR1/CXCR2 receptor and activation
CC by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in
CC neutrophils) and activation of several downstream signaling pathways
CC including PI3K and MAPK pathways. {ECO:0000250|UniProtKB:P10145}.
CC -!- SUBUNIT: Homodimer. Interacts with TNFAIP6 (via Link domain); this
CC interaction interferes with chemokine binding to glycosaminoglycans.
CC {ECO:0000250|UniProtKB:P10145}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Citrullination at Arg-27 prevents proteolysis, and dampens tissue
CC inflammation, it also enhances leukocytosis, possibly through impaired
CC chemokine clearance from the blood circulation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; D28772; BAA05961.1; -; mRNA.
DR EMBL; D14285; BAA03246.1; -; Genomic_DNA.
DR EMBL; U10308; AAC48434.1; -; mRNA.
DR EMBL; AF048717; AAC05134.1; -; mRNA.
DR PIR; JN0841; JN0841.
DR RefSeq; NP_001003200.1; NM_001003200.1.
DR AlphaFoldDB; P41324; -.
DR SMR; P41324; -.
DR STRING; 9615.ENSCAFP00000004516; -.
DR PaxDb; 9612-ENSCAFP00000004516; -.
DR Ensembl; ENSCAFT00040014293.1; ENSCAFP00040012366.1; ENSCAFG00040007673.1.
DR GeneID; 403850; -.
DR KEGG; cfa:403850; -.
DR CTD; 3576; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR HOGENOM; CLU_143902_3_0_1; -.
DR InParanoid; P41324; -.
DR OMA; IGTELRC; -.
DR OrthoDB; 5343536at2759; -.
DR TreeFam; TF333433; -.
DR Reactome; R-CFA-375276; Peptide ligand-binding receptors.
DR Reactome; R-CFA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Chromosome 13.
DR Proteomes; UP000805418; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR CDD; cd00273; Chemokine_CXC; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR InterPro; IPR039809; Chemokine_b/g/d.
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; PTHR12015:SF211; INTERLEUKIN-8; 1.
DR PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR Pfam; PF00048; IL8; 1.
DR PRINTS; PR00436; INTERLEUKIN8.
DR PRINTS; PR00437; SMALLCYTKCXC.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; Interleukin 8-like chemokines; 1.
DR PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Citrullination; Cytokine; Disulfide bond;
KW Inflammatory response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..101
FT /note="Interleukin-8"
FT /id="PRO_0000005121"
FT MOD_RES 27
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT DISULFID 34..61
FT /evidence="ECO:0000250"
FT DISULFID 36..77
FT /evidence="ECO:0000250"
SQ SEQUENCE 101 AA; 11280 MW; 3A3A4676DA968376 CRC64;
MTSKLAVALL AAFVLSAALC EAAVLSRVSS ELRCQCIKTH STPFHPKYIK ELRVIDSGPH
CENSEIIVKL FNGNEVCLDP KEKWVQKVVQ IFLKKAEKQD P
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