Detail Information for IndEnz0002015366
IED ID IndEnz0002015366
Enzyme Type ID protease015366
Protein Name Interleukin-8
IL-8
C-X-C motif chemokine 8
Chemokine
C-X-C motif
ligand 8
Emoctakin
Granulocyte chemotactic protein 1
GCP-1
Monocyte-derived neutrophil chemotactic factor
MDNCF
Monocyte-derived neutrophil-activating peptide
MONAP
Neutrophil-activating protein 1
NAP-1
Protein 3-10C
T-cell chemotactic factor

Cleaved into: MDNCF-a
GCP/IL-8 protein IV
IL8/NAP1 form I
; Interleukin-8
Ala-IL-8
77
GCP/IL-8 protein II
IL-8
1-77
IL8/NAP1 form II
MDNCF-b
; IL-8
5-77
; IL-8
6-77
Ser-IL-8
72
GCP/IL-8 protein I
IL8/NAP1 form III
Lymphocyte-derived neutrophil-activating factor
LYNAP
MDNCF-c
Neutrophil-activating factor
NAF
; IL-8
7-77
GCP/IL-8 protein V
IL8/NAP1 form IV
; IL-8
8-77
GCP/IL-8 protein VI
IL8/NAP1 form V
; IL-8
9-77
GCP/IL-8 protein III
IL8/NAP1 form VI
Gene Name CXCL8 IL8
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MTSKLAVALLAAFLISAALCEGAVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS
Enzyme Length 99
Uniprot Accession Number P10145
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively. {ECO:0000269|PubMed:11978786, ECO:0000269|PubMed:2145175, ECO:0000269|PubMed:2212672}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (7); Disulfide bond (2); Helix (2); Modified residue (1); Mutagenesis (3); Sequence caution (1); Sequence conflict (1); Signal peptide (1); Site (2); Turn (1)
Keywords 3D-structure;Chemotaxis;Citrullination;Cytokine;Direct protein sequencing;Disulfide bond;Inflammatory response;Reference proteome;Secreted;Signal
Interact With P25025; P02776; P98066; P9WGV3; P9WMN3; Q6MX51
Induction INDUCTION: By ER stress in a DDIT3/CHOP-dependent manner. {ECO:0000269|PubMed:20829347}.
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 27; /note="Citrulline"; /evidence="ECO:0000269|PubMed:18710930, ECO:0000269|PubMed:19608678"
Post Translational Modification PTM: Several N-terminal processed forms are produced by proteolytic cleavage after secretion from at least peripheral blood monocytes, leukcocytes and endothelial cells. In general, IL-8(1-77) is referred to as interleukin-8. IL-8(6-77) is the most promiment form. {ECO:0000269|PubMed:11023497, ECO:0000269|PubMed:11978786, ECO:0000269|PubMed:2145175, ECO:0000269|PubMed:2212672, ECO:0000269|PubMed:2523801, ECO:0000269|PubMed:2648135}.; PTM: Citrullination at Arg-27 prevents proteolysis, and dampens tissue inflammation, it also enhances leukocytosis, possibly through impaired chemokine clearance from the blood circulation. {ECO:0000269|PubMed:18710930, ECO:0000269|PubMed:19608678}.
Signal Peptide SIGNAL 1..20; /evidence="ECO:0000269|PubMed:2145175, ECO:0000269|PubMed:2523801, ECO:0000269|PubMed:2648135"
Structure 3D NMR spectroscopy (9); Electron microscopy (2); X-ray crystallography (7)
Cross Reference PDB 1ICW; 1IKL; 1IKM; 1IL8; 1ILP; 1ILQ; 1QE6; 1ROD; 2IL8; 3IL8; 4XDX; 5D14; 5WDZ; 6LFM; 6LFO; 6N2U; 6WZM; 6XMN;
Mapped Pubmed ID 10319580; 10415057; 11083887; 11756416; 11784713; 11814358; 11854210; 11855786; 11868823; 11876744; 11884401; 11884459; 11888846; 11896938; 11910304; 11911801; 11950481; 11956621; 11960393; 11964077; 11966578; 11973337; 11989790; 11999552; 12027404; 12033786; 12034575; 12039947; 12055326; 12060853; 12067976; 12081586; 12090473; 12091490; 12093676; 12096924; 12096927; 12100025; 12101072; 12115500; 12117737; 12117926; 12117969; 12117995; 12123753; 12126643; 12133438; 12139952; 12149127; 12150710; 12151316; 12151344; 12163591; 12164325; 12165085; 12169092; 12169272; 12186702; 12186913; 12195386; 12223528; 12225945; 12239630; 12359770; 12364441; 12366401; 12382118; 12384994; 12388718; 12391099; 12393171; 12410798; 12415593; 12453441; 12480084; 12485855; 12496258; 12513912; 12520365; 12524080; 12529421; 12530093; 12533683; 12543081; 12547728; 12565901; 12573991; 12576442; 12584113; 12594001; 12594058; 12615831; 12626597; 12628493; 12632066; 12633940; 12634636; 12637525; 12646250; 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Motif
Gene Encoded By
Mass 11,098
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda