ID   IL8_TURTR               Reviewed;         101 AA.
AC   Q7YRB5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14709826; DOI=10.1292/jvms.65.1351;
RA   Itou T., Yosida Y., Shoji Y., Sugisawa H., Endo T., Sakai T.;
RT   "Molecular cloning and expression of bottlenose dolphin (Tursiops
RT   truncatus) interleukin-8.";
RL   J. Vet. Med. Sci. 65:1351-1354(2003).
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. {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; AB096002; BAC81421.1; -; mRNA.
DR   RefSeq; NP_001267571.1; NM_001280642.1.
DR   AlphaFoldDB; Q7YRB5; -.
DR   SMR; Q7YRB5; -.
DR   STRING; 9739.XP_004319644.1; -.
DR   GeneID; 101331085; -.
DR   CTD; 3576; -.
DR   OrthoDB; 1618797at2759; -.
DR   Proteomes; UP000245320; Chromosome 5.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0008009; F:chemokine activity; IEA:InterPro.
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; IEA:InterPro.
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; 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_0000005137"
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;  11371 MW;  2A5DFE251D980E15 CRC64;
     MTSKLAIALL AAFLLSAALC KAAVLSRMTS ELRCQCINIH STPFHPKFIR ELRVIESGPH
     CENSEIIVKL VNGKEVCLNP KEKWVQKVVQ IFLKRAEKKD P