ID   IL8_CAVPO               Reviewed;         101 AA.
AC   P49113;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   AltName: Full=Neutrophil attractant protein 1;
DE            Short=NAP-1;
DE   Flags: Precursor;
GN   Name=CXCL8; Synonyms=IL8;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Spleen;
RX   PubMed=7504015;
RA   Yoshimura T., Johnson D.G.;
RT   "cDNA cloning and expression of guinea pig neutrophil attractant protein-1
RT   (NAP-1). NAP-1 is highly conserved in guinea pig.";
RL   J. Immunol. 151:6225-6236(1993).
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   -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC       {ECO:0000305}.
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DR   EMBL; L04986; AAA37049.1; -; Genomic_DNA.
DR   PIR; I48148; I48148.
DR   RefSeq; NP_001166870.1; NM_001173399.2.
DR   AlphaFoldDB; P49113; -.
DR   SMR; P49113; -.
DR   STRING; 10141.ENSCPOP00000009984; -.
DR   PRIDE; P49113; -.
DR   GeneID; 100379599; -.
DR   KEGG; cpoc:100379599; -.
DR   CTD; 3576; -.
DR   eggNOG; ENOG502S7MM; Eukaryota.
DR   InParanoid; P49113; -.
DR   OrthoDB; 1618797at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0008009; F:chemokine activity; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0005153; F:interleukin-8 receptor binding; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0042119; P:neutrophil activation; IEA:InterPro.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
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; IPR028469; Interleukin-8.
DR   InterPro; IPR036048; Interleukin_8-like_sf.
DR   PANTHER; PTHR10179; PTHR10179; 1.
DR   PANTHER; PTHR10179:SF42; PTHR10179:SF42; 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   3: Inferred from homology;
KW   Chemotaxis; Cytokine; Disulfide bond; Inflammatory response;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..101
FT                   /note="Interleukin-8"
FT                   /id="PRO_0000005122"
FT   DISULFID        34..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..77
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   101 AA;  11414 MW;  557E2A9E15F6727F CRC64;
     MPSQLRVAVL AAFLLSAVLC EGMVVTKLVS ELRCQCIKIH TTPFHPKFIK ELKVIESGPR
     CANSEIIVKL SDNRQLCLDP KKKWVQDVVS MFLKRTESQD S