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IL8_RABIT
ID   IL8_RABIT               Reviewed;         101 AA.
AC   P19874;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 138.
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/activation protein 1;
DE            Short=NAP-1;
DE   AltName: Full=Permeability factor 1;
DE            Short=PF1;
DE            Short=rPF1;
DE   Flags: Precursor;
GN   Name=CXCL8; Synonyms=IL8;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Spleen;
RX   PubMed=2026877;
RA   Yoshimura T., Yuhki N.;
RT   "Neutrophil attractant/activation protein-1 and monocyte chemoattractant
RT   protein-1 in rabbit. cDNA cloning and their expression in spleen cells.";
RL   J. Immunol. 146:3483-3488(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-53.
RC   STRAIN=New Zealand white; TISSUE=Peritoneal cavity;
RX   PubMed=2244880; DOI=10.1042/bj2710797;
RA   Beaubien B.C., Collins P.D., Jose P.J., Totty N.F., Hsuan J.,
RA   Waterfield M.D., Williams T.J.;
RT   "A novel neutrophil chemoattractant generated during an inflammatory
RT   reaction in the rabbit peritoneal cavity in vivo. Purification, partial
RT   amino acid sequence and structural relationship to interleukin 8.";
RL   Biochem. J. 271:797-801(1990).
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; M57439; AAA31422.1; -; mRNA.
DR   PIR; I46871; I46871.
DR   RefSeq; NP_001075762.1; NM_001082293.1.
DR   AlphaFoldDB; P19874; -.
DR   SMR; P19874; -.
DR   STRING; 9986.ENSOCUP00000018795; -.
DR   ABCD; P19874; 7 sequenced antibodies.
DR   Ensembl; ENSOCUT00000030077; ENSOCUP00000018795; ENSOCUG00000011835.
DR   GeneID; 100009129; -.
DR   KEGG; ocu:100009129; -.
DR   CTD; 3576; -.
DR   eggNOG; ENOG502S7MM; Eukaryota.
DR   GeneTree; ENSGT00940000160757; -.
DR   HOGENOM; CLU_143902_3_0_1; -.
DR   InParanoid; P19874; -.
DR   OMA; IGTELRC; -.
DR   OrthoDB; 1618797at2759; -.
DR   Proteomes; UP000001811; Chromosome 15.
DR   Bgee; ENSOCUG00000011835; Expressed in ovary and 13 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0008009; F:chemokine activity; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0005153; F:interleukin-8 receptor binding; ISS:UniProtKB.
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; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0050930; P:induction of positive chemotaxis; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
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:0031328; P:positive regulation of cellular biosynthetic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Chemotaxis; Citrullination; Cytokine; Direct protein sequencing;
KW   Disulfide bond; Inflammatory response; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:2244880"
FT   CHAIN           23..101
FT                   /note="Interleukin-8"
FT                   /id="PRO_0000005135"
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"
FT   CONFLICT        50
FT                   /note="K -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   101 AA;  11403 MW;  152B110C43AD8726 CRC64;
     MNSKLAVALL ATFLLSLTLC EAAVLTRIGT ELRCQCIKTH STPFHPKFIK ELRVIESGPH
     CANSEIIVKL VDGRELCLDP KEKWVQKVVQ IFLKRAEQQE S
 
 
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