IL8_MACMU
ID IL8_MACMU Reviewed; 101 AA.
AC P67813; P51495;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, 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 Flags: Precursor;
GN Name=CXCL8; Synonyms=IL8;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7561102;
RA Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
RT "Comparative sequence analysis of cytokine genes from human and nonhuman
RT primates.";
RL J. Immunol. 155:3946-3954(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7628861; DOI=10.1007/bf01534390;
RA Minnerly J.C., Baganoff M.P., Deppeler C.L., Keller B.T., Rapp S.R.,
RA Widomski D.L., Fretland D.J., Bolanowski M.A.;
RT "Identification and characterization of rhesus macaque interleukin-8.";
RL Inflammation 19:313-331(1995).
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; U19849; AAA86711.1; -; mRNA.
DR EMBL; S78555; AAA80141.2; -; mRNA.
DR RefSeq; NP_001028137.1; NM_001032965.1.
DR AlphaFoldDB; P67813; -.
DR SMR; P67813; -.
DR STRING; 9544.ENSMMUP00000005115; -.
DR ABCD; P67813; 1 sequenced antibody.
DR Ensembl; ENSMMUT00000100547; ENSMMUP00000072289; ENSMMUG00000060156.
DR GeneID; 613028; -.
DR KEGG; mcc:613028; -.
DR CTD; 3576; -.
DR VEuPathDB; HostDB:ENSMMUG00000060156; -.
DR VGNC; VGNC:100214; CXCL8.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000160757; -.
DR InParanoid; P67813; -.
DR OrthoDB; 1618797at2759; -.
DR Proteomes; UP000006718; Chromosome 5.
DR Bgee; ENSMMUG00000060156; Expressed in fibroblast and 18 other 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; ISS:UniProtKB.
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; ISS:UniProtKB.
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; 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 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_0000005132"
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; 11320 MW; 42BCF9C97C84B5F9 CRC64;
MTSKLAVALL AAFLLSAALC EGAVLPRSAK ELRCECIKTY SKPFHPKFIK ELRVIESGPH
CANTEIIVKL SDGRELCLDP KEPWVQRVVE KFVKRAENQN P
