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C-X-C motif chemokine 5 (ENA-78(1-78)) (Epithelial-derived neutrophil-activating protein 78) (Neutrophil-activating peptide ENA-78) (Small-inducible cytokine B5) [Cleaved into: ENA-78(8-78); ENA-78(9-78)]

 CXCL5_HUMAN             Reviewed;         114 AA.
P42830; Q96QE1;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=C-X-C motif chemokine 5;
AltName: Full=ENA-78(1-78);
AltName: Full=Epithelial-derived neutrophil-activating protein 78;
AltName: Full=Neutrophil-activating peptide ENA-78;
AltName: Full=Small-inducible cytokine B5;
Contains:
RecName: Full=ENA-78(8-78);
Contains:
RecName: Full=ENA-78(9-78);
Flags: Precursor;
Name=CXCL5; Synonyms=ENA78, SCYB5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7828901; DOI=10.1016/0378-1119(94)90682-3;
Power C.A., Furness R.B., Brawand C., Wells T.N.C.;
"Cloning of a full-length cDNA encoding the neutrophil-activating
peptide ENA-78 from human platelets.";
Gene 151:333-334(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7929219;
Chang M.S., McNinch J., Basu R., Simonet S.;
"Cloning and characterization of the human neutrophil-activating
peptide (ENA-78) gene.";
J. Biol. Chem. 269:25277-25282(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7999089; DOI=10.1006/bbrc.1994.2709;
Corbett M.S., Schmitt I., Riess O., Walz A.;
"Characterization of the gene for human neutrophil-activating peptide
78 (ENA-78).";
Biochem. Biophys. Res. Commun. 205:612-617(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11468158; DOI=10.1182/blood.V98.3.610;
Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M.,
Poncz M., McKenzie S.E., Reilly M.P.;
"Localization of distal regulatory domains in the megakaryocyte-
specific platelet basic protein/platelet factor 4 gene locus.";
Blood 98:610-617(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-80.
Amoli M.M., Thomson W., Hajeer A.H., Gonzalez-Gay M.A., Ollier W.E.R.;
"Novel polymorphism in ENA-78 gene.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 43-114.
TISSUE=Epithelium;
PubMed=1744577; DOI=10.1084/jem.174.6.1355;
Walz A., Burgener R., Car B., Baggiolini M., Kunkel S.L.,
Strieter R.M.;
"Structure and neutrophil-activating properties of a novel
inflammatory peptide (ENA-78) with homology to interleukin 8.";
J. Exp. Med. 174:1355-1362(1991).
[8]
PROTEIN SEQUENCE OF 37-51, IDENTIFICATION OF ENA-78(8-78) AND
ENA-78(9-78), PROTEOLYTIC PROCESSING OF N-TERMINUS, AND FUNCTION.
TISSUE=Peripheral blood monocyte;
PubMed=10095777; DOI=10.1046/j.1432-1327.1999.00166.x;
Wuyts A., Govaerts C., Struyf S., Lenaerts J.-P., Put W., Conings R.,
Proost P., Van Damme J.;
"Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from
tumor cells and leukocytes reveals NH2-terminal heterogeneity.
Functional comparison of different natural isoforms.";
Eur. J. Biochem. 260:421-429(1999).
[9]
PROTEIN SEQUENCE OF 37-45.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[10]
REVIEW.
PubMed=14711052; DOI=10.1016/S0065-2776(03)81001-5;
Struyf S., Proost P., Van Damme J.;
"Regulation of the immune response by the interaction of chemokines
and proteases.";
Adv. Immunol. 81:1-44(2003).
[11] {ECO:0000244|PDB:2MGS}
STRUCTURE BY NMR OF 37-114, DISULFIDE BONDS, AND SUBUNIT.
PubMed=24695525; DOI=10.1371/journal.pone.0093228;
Sepuru K.M., Poluri K.M., Rajarathnam K.;
"Solution structure of CXCL5--a novel chemokine and adipokine
implicated in inflammation and obesity.";
PLoS ONE 9:E93228-E93228(2014).
-!- FUNCTION: Involved in neutrophil activation. In vitro, ENA-78(8-
78) and ENA-78(9-78) show a threefold higher chemotactic activity
for neutrophil granulocytes. {ECO:0000269|PubMed:10095777}.
-!- SUBUNIT: Monomer (PubMed:24695525). Homodimer (PubMed:24695525).
{ECO:0000269|PubMed:24695525}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: N-terminal processed forms ENA-78(8-78) and ENA-78(9-78) are
produced by proteolytic cleavage after secretion from peripheral
blood monocytes. {ECO:0000269|PubMed:10095777}.
-!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CXCL5 entry;
URL="https://en.wikipedia.org/wiki/CXCL5";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X78686; CAA55355.1; -; mRNA.
EMBL; U12709; AAA62475.1; -; Genomic_DNA.
EMBL; L37036; AAA86426.1; -; Genomic_DNA.
EMBL; AF349466; AAK29641.1; -; Genomic_DNA.
EMBL; BC008376; AAH08376.1; -; mRNA.
EMBL; AJ315732; CAC42884.1; -; Genomic_DNA.
CCDS; CCDS34006.1; -.
PIR; JC2433; A55010.
RefSeq; NP_002985.1; NM_002994.4.
UniGene; Hs.89714; -.
PDB; 2MGS; NMR; -; A/B=37-114.
PDBsum; 2MGS; -.
ProteinModelPortal; P42830; -.
SMR; P42830; -.
BioGrid; 112276; 2.
DIP; DIP-5911N; -.
IntAct; P42830; 7.
STRING; 9606.ENSP00000296027; -.
iPTMnet; P42830; -.
PhosphoSitePlus; P42830; -.
DMDM; 1169525; -.
EPD; P42830; -.
PaxDb; P42830; -.
PeptideAtlas; P42830; -.
PRIDE; P42830; -.
ProteomicsDB; 55559; -.
DNASU; 6374; -.
Ensembl; ENST00000296027; ENSP00000296027; ENSG00000163735.
GeneID; 6374; -.
KEGG; hsa:6374; -.
CTD; 6374; -.
DisGeNET; 6374; -.
EuPathDB; HostDB:ENSG00000163735.6; -.
GeneCards; CXCL5; -.
HGNC; HGNC:10642; CXCL5.
HPA; HPA065474; -.
MIM; 600324; gene.
neXtProt; NX_P42830; -.
OpenTargets; ENSG00000163735; -.
PharmGKB; PA35573; -.
eggNOG; ENOG410J4TR; Eukaryota.
eggNOG; ENOG41117DC; LUCA.
GeneTree; ENSGT00530000062901; -.
HOGENOM; HOG000220915; -.
HOVERGEN; HBG107789; -.
InParanoid; P42830; -.
KO; K05506; -.
OMA; LRCVCLQ; -.
OrthoDB; EOG091G132U; -.
PhylomeDB; P42830; -.
TreeFam; TF333433; -.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
GeneWiki; CXCL5; -.
GenomeRNAi; 6374; -.
PMAP-CutDB; P42830; -.
PRO; PR:P42830; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163735; -.
CleanEx; HS_CXCL5; -.
ExpressionAtlas; P42830; baseline and differential.
Genevisible; P42830; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0002446; P:neutrophil mediated immunity; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00273; Chemokine_CXC; 1.
InterPro; IPR001089; Chemokine_CXC.
InterPro; IPR018048; Chemokine_CXC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR033899; CXC_Chemokine_domain.
InterPro; IPR036048; Interleukin_8-like_sf.
PANTHER; PTHR10179; PTHR10179; 1.
Pfam; PF00048; IL8; 1.
PRINTS; PR00437; SMALLCYTKCXC.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytokine; Direct protein sequencing;
Disulfide bond; Reference proteome; Secreted; Signal.
SIGNAL 1 36 {ECO:0000269|PubMed:10095777,
ECO:0000269|PubMed:12665801}.
CHAIN 37 114 C-X-C motif chemokine 5.
/FTId=PRO_0000005075.
CHAIN 44 114 ENA-78(8-78).
/FTId=PRO_0000005076.
CHAIN 45 114 ENA-78(9-78).
/FTId=PRO_0000005077.
SITE 44 45 Cleavage; by cathepsin G.
DISULFID 49 75 {ECO:0000244|PDB:2MGS,
ECO:0000269|PubMed:24695525}.
DISULFID 51 91 {ECO:0000244|PDB:2MGS,
ECO:0000269|PubMed:24695525}.
HELIX 60 62 {ECO:0000244|PDB:2MGS}.
STRAND 63 69 {ECO:0000244|PDB:2MGS}.
STRAND 79 87 {ECO:0000244|PDB:2MGS}.
STRAND 89 92 {ECO:0000244|PDB:2MGS}.
HELIX 97 108 {ECO:0000244|PDB:2MGS}.
TURN 109 112 {ECO:0000244|PDB:2MGS}.
SEQUENCE 114 AA; 11972 MW; 56B21EE86AE952D3 CRC64;
MSLLSSRAAR VPGPSSSLCA LLVLLLLLTQ PGPIASAGPA AAVLRELRCV CLQTTQGVHP
KMISNLQVFA IGPQCSKVEV VASLKNGKEI CLDPEAPFLK KVIQKILDGG NKEN


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