ID   IL8_FELCA               Reviewed;         101 AA.
AC   Q9XSX5;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 132.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Straubinger A.F., Simpson K.W., Straubinger R.K.;
RT   "Feline interleukin-8 mRNA.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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; AF158598; AAD40323.1; -; mRNA.
DR   RefSeq; NP_001009281.1; NM_001009281.1.
DR   AlphaFoldDB; Q9XSX5; -.
DR   SMR; Q9XSX5; -.
DR   STRING; 9685.ENSFCAP00000004310; -.
DR   PaxDb; 9685-ENSFCAP00000004310; -.
DR   Ensembl; ENSFCAT00000004666.5; ENSFCAP00000004310.3; ENSFCAG00000004666.5.
DR   GeneID; 493836; -.
DR   KEGG; fca:493836; -.
DR   VGNC; VGNC:67785; CXCL8.
DR   eggNOG; ENOG502S7MM; Eukaryota.
DR   GeneTree; ENSGT00940000160757; -.
DR   HOGENOM; CLU_143902_3_0_1; -.
DR   InParanoid; Q9XSX5; -.
DR   OMA; IGTELRC; -.
DR   OrthoDB; 5343536at2759; -.
DR   TreeFam; TF333433; -.
DR   Proteomes; UP000011712; Chromosome B1.
DR   Bgee; ENSFCAG00000004666; Expressed in zone of skin and 8 other cell types or tissues.
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:0005153; F:interleukin-8 receptor binding; IEA:Ensembl.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR   GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IEA:Ensembl.
DR   GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:2000535; P:regulation of entry of bacterium into host cell; IEA:Ensembl.
DR   GO; GO:0045091; P:regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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_0000005124"
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;  11165 MW;  690D97F13EF79170 CRC64;
     MTSKLVVALL AAFMLSAALC EAAVLSRISS ELRCQCIKTH STPFNPKLIK ELTVIDSGPH
     CENSEIIVKL VNGKEVCLDP KQKWVQKVVE IFLKKAEKQN A
//