IL8_PIG
ID IL8_PIG Reviewed; 103 AA.
AC P26894; P22951;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Interleukin-8;
DE Short=IL-8;
DE AltName: Full=Alveolar macrophage chemotactic factor I;
DE Short=AMCF-I;
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8276881; DOI=10.1016/s0021-9258(17)42316-7;
RA Lin G., Pearson A.E., Scamurra R.W., Zhou Y., Baarsch M.J., Weiss D.J.,
RA Murtaugh M.P.;
RT "Regulation of interleukin-8 expression in porcine alveolar macrophages by
RT bacterial lipopolysaccharide.";
RL J. Biol. Chem. 269:77-85(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sanjanwala M.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-45.
RC TISSUE=Lung;
RX PubMed=1420165; DOI=10.1021/bi00158a011;
RA Goodman R.B., Foster D.C., Mathewes S.L., Osborn S.G., Kuijper J.L.,
RA Forstrom J.W., Martin T.R.;
RT "Molecular cloning of porcine alveolar macrophage-derived neutrophil
RT chemotactic factors I and II; identification of porcine IL-8 and another
RT intercrine-alpha protein.";
RL Biochemistry 31:10483-10490(1992).
RN [4]
RP SEQUENCE REVISION TO 23.
RA Goodman R.B.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 26-45.
RC STRAIN=Yorkshire;
RX PubMed=1850745; DOI=10.1016/s0021-9258(18)92996-0;
RA Goodman R.B., Forstrom J.W., Osborn S.G., Chi E.Y., Martin T.R.;
RT "Identification of two neutrophil chemotactic peptides produced by porcine
RT alveolar macrophages.";
RL J. Biol. Chem. 266:8455-8463(1991).
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 -!- TISSUE SPECIFICITY: Alveolar macrophages.
CC -!- INDUCTION: By lipopolysaccharide (LPS).
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; M86923; AAA16616.1; -; mRNA.
DR EMBL; X61151; CAA43461.1; -; mRNA.
DR EMBL; M99367; AAA92576.1; -; mRNA.
DR PIR; A39819; A39819.
DR PIR; A53096; A53096.
DR RefSeq; NP_999032.1; NM_213867.1.
DR RefSeq; XP_003362006.1; XM_003361958.3.
DR AlphaFoldDB; P26894; -.
DR SMR; P26894; -.
DR STRING; 9823.ENSSSCP00000009554; -.
DR PaxDb; P26894; -.
DR PRIDE; P26894; -.
DR Ensembl; ENSSSCT00000009807; ENSSSCP00000009554; ENSSSCG00000008953.
DR Ensembl; ENSSSCT00005065575; ENSSSCP00005040562; ENSSSCG00005040921.
DR Ensembl; ENSSSCT00025023573; ENSSSCP00025009879; ENSSSCG00025017428.
DR Ensembl; ENSSSCT00030050860; ENSSSCP00030023129; ENSSSCG00030036565.
DR Ensembl; ENSSSCT00035096660; ENSSSCP00035040729; ENSSSCG00035071462.
DR Ensembl; ENSSSCT00040103852; ENSSSCP00040047190; ENSSSCG00040074984.
DR Ensembl; ENSSSCT00045016902; ENSSSCP00045011673; ENSSSCG00045009964.
DR Ensembl; ENSSSCT00055061067; ENSSSCP00055048957; ENSSSCG00055030636.
DR Ensembl; ENSSSCT00060053953; ENSSSCP00060023007; ENSSSCG00060039839.
DR Ensembl; ENSSSCT00070012189; ENSSSCP00070010025; ENSSSCG00070006372.
DR GeneID; 396880; -.
DR KEGG; ssc:396880; -.
DR CTD; 3576; -.
DR VGNC; VGNC:87106; CXCL8.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000160757; -.
DR HOGENOM; CLU_143902_3_0_1; -.
DR InParanoid; P26894; -.
DR OMA; IGTELRC; -.
DR OrthoDB; 1618797at2759; -.
DR TreeFam; TF333433; -.
DR Reactome; R-SSC-375276; Peptide ligand-binding receptors.
DR Reactome; R-SSC-380108; Chemokine receptors bind chemokines.
DR Reactome; R-SSC-418594; G alpha (i) signalling events.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Chromosome 8.
DR Bgee; ENSSSCG00000008953; Expressed in ileum and 22 other tissues.
DR ExpressionAtlas; P26894; baseline and differential.
DR Genevisible; P26894; SS.
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: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: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 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..25
FT /evidence="ECO:0000269|PubMed:1420165,
FT ECO:0000269|PubMed:1850745"
FT CHAIN 26..103
FT /note="Interleukin-8"
FT /id="PRO_0000005134"
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 33..34
FT /note="RC -> CR (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="K -> KK (in Ref. 2; CAA43461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11633 MW; 9FE0E350E1928C64 CRC64;
MTSKLAVAFL AVFLLSAALC EAAVLARVSA ELRCQCINTH STPFHPKFIK ELRVIESGPH
CENSEIIVKL VNGKEVCLDP KEKWVQKVVQ IFLKRTEKQQ QQQ
