CXCL5_HUMAN
ID CXCL5_HUMAN Reviewed; 114 AA.
AC P42830; Q96QE1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=C-X-C motif chemokine 5;
DE AltName: Full=ENA-78(1-78);
DE AltName: Full=Epithelial-derived neutrophil-activating protein 78;
DE AltName: Full=Neutrophil-activating peptide ENA-78;
DE AltName: Full=Small-inducible cytokine B5;
DE Contains:
DE RecName: Full=ENA-78(8-78);
DE Contains:
DE RecName: Full=ENA-78(9-78);
DE Flags: Precursor;
GN Name=CXCL5; Synonyms=ENA78, SCYB5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7828901; DOI=10.1016/0378-1119(94)90682-3;
RA Power C.A., Furness R.B., Brawand C., Wells T.N.C.;
RT "Cloning of a full-length cDNA encoding the neutrophil-activating peptide
RT ENA-78 from human platelets.";
RL Gene 151:333-334(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7929219; DOI=10.1016/s0021-9258(18)47243-2;
RA Chang M.S., McNinch J., Basu R., Simonet S.;
RT "Cloning and characterization of the human neutrophil-activating peptide
RT (ENA-78) gene.";
RL J. Biol. Chem. 269:25277-25282(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7999089; DOI=10.1006/bbrc.1994.2709;
RA Corbett M.S., Schmitt I., Riess O., Walz A.;
RT "Characterization of the gene for human neutrophil-activating peptide 78
RT (ENA-78).";
RL Biochem. Biophys. Res. Commun. 205:612-617(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11468158; DOI=10.1182/blood.v98.3.610;
RA Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M., Poncz M.,
RA McKenzie S.E., Reilly M.P.;
RT "Localization of distal regulatory domains in the megakaryocyte-specific
RT platelet basic protein/platelet factor 4 gene locus.";
RL Blood 98:610-617(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-80.
RA Amoli M.M., Thomson W., Hajeer A.H., Gonzalez-Gay M.A., Ollier W.E.R.;
RT "Novel polymorphism in ENA-78 gene.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-114.
RC TISSUE=Epithelium;
RX PubMed=1744577; DOI=10.1084/jem.174.6.1355;
RA Walz A., Burgener R., Car B., Baggiolini M., Kunkel S.L., Strieter R.M.;
RT "Structure and neutrophil-activating properties of a novel inflammatory
RT peptide (ENA-78) with homology to interleukin 8.";
RL J. Exp. Med. 174:1355-1362(1991).
RN [8]
RP PROTEIN SEQUENCE OF 37-51, IDENTIFICATION OF ENA-78(8-78) AND ENA-78(9-78),
RP PROTEOLYTIC PROCESSING OF N-TERMINUS, AND FUNCTION.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=10095777; DOI=10.1046/j.1432-1327.1999.00166.x;
RA Wuyts A., Govaerts C., Struyf S., Lenaerts J.-P., Put W., Conings R.,
RA Proost P., Van Damme J.;
RT "Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor
RT cells and leukocytes reveals NH2-terminal heterogeneity. Functional
RT comparison of different natural isoforms.";
RL Eur. J. Biochem. 260:421-429(1999).
RN [9]
RP PROTEIN SEQUENCE OF 37-45.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP REVIEW.
RX PubMed=14711052; DOI=10.1016/s0065-2776(03)81001-5;
RA Struyf S., Proost P., Van Damme J.;
RT "Regulation of the immune response by the interaction of chemokines and
RT proteases.";
RL Adv. Immunol. 81:1-44(2003).
RN [11] {ECO:0007744|PDB:2MGS}
RP STRUCTURE BY NMR OF 37-114, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=24695525; DOI=10.1371/journal.pone.0093228;
RA Sepuru K.M., Poluri K.M., Rajarathnam K.;
RT "Solution structure of CXCL5--a novel chemokine and adipokine implicated in
RT inflammation and obesity.";
RL PLoS ONE 9:E93228-E93228(2014).
CC -!- FUNCTION: Involved in neutrophil activation. In vitro, ENA-78(8-78) and
CC ENA-78(9-78) show a threefold higher chemotactic activity for
CC neutrophil granulocytes. {ECO:0000269|PubMed:10095777}.
CC -!- SUBUNIT: Monomer (PubMed:24695525). Homodimer (PubMed:24695525).
CC {ECO:0000269|PubMed:24695525}.
CC -!- INTERACTION:
CC P42830; Q08043: ACTN3; NbExp=3; IntAct=EBI-12175919, EBI-2880652;
CC P42830; P05187: ALPP; NbExp=3; IntAct=EBI-12175919, EBI-1211484;
CC P42830; O95967: EFEMP2; NbExp=3; IntAct=EBI-12175919, EBI-743414;
CC P42830; P23142-4: FBLN1; NbExp=3; IntAct=EBI-12175919, EBI-11956479;
CC P42830; P28799: GRN; NbExp=3; IntAct=EBI-12175919, EBI-747754;
CC P42830; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12175919, EBI-16439278;
CC P42830; B2RUY7: VWC2L; NbExp=3; IntAct=EBI-12175919, EBI-11747707;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-terminal processed forms ENA-78(8-78) and ENA-78(9-78) are
CC produced by proteolytic cleavage after secretion from peripheral blood
CC monocytes. {ECO:0000269|PubMed:10095777}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL5 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL5";
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DR EMBL; X78686; CAA55355.1; -; mRNA.
DR EMBL; U12709; AAA62475.1; -; Genomic_DNA.
DR EMBL; L37036; AAA86426.1; -; Genomic_DNA.
DR EMBL; AF349466; AAK29641.1; -; Genomic_DNA.
DR EMBL; BC008376; AAH08376.1; -; mRNA.
DR EMBL; AJ315732; CAC42884.1; -; Genomic_DNA.
DR CCDS; CCDS34006.1; -.
DR PIR; JC2433; A55010.
DR RefSeq; NP_002985.1; NM_002994.4.
DR PDB; 2MGS; NMR; -; A/B=37-114.
DR PDBsum; 2MGS; -.
DR AlphaFoldDB; P42830; -.
DR BMRB; P42830; -.
DR SMR; P42830; -.
DR BioGRID; 112276; 50.
DR DIP; DIP-5911N; -.
DR IntAct; P42830; 16.
DR STRING; 9606.ENSP00000296027; -.
DR iPTMnet; P42830; -.
DR PhosphoSitePlus; P42830; -.
DR BioMuta; CXCL5; -.
DR DMDM; 1169525; -.
DR EPD; P42830; -.
DR MassIVE; P42830; -.
DR PaxDb; P42830; -.
DR PeptideAtlas; P42830; -.
DR PRIDE; P42830; -.
DR ProteomicsDB; 55559; -.
DR ABCD; P42830; 2 sequenced antibodies.
DR Antibodypedia; 13336; 545 antibodies from 36 providers.
DR DNASU; 6374; -.
DR Ensembl; ENST00000296027.5; ENSP00000296027.4; ENSG00000163735.7.
DR GeneID; 6374; -.
DR KEGG; hsa:6374; -.
DR MANE-Select; ENST00000296027.5; ENSP00000296027.4; NM_002994.5; NP_002985.1.
DR CTD; 6374; -.
DR DisGeNET; 6374; -.
DR GeneCards; CXCL5; -.
DR HGNC; HGNC:10642; CXCL5.
DR HPA; ENSG00000163735; Group enriched (lymphoid tissue, salivary gland).
DR MIM; 600324; gene.
DR neXtProt; NX_P42830; -.
DR OpenTargets; ENSG00000163735; -.
DR PharmGKB; PA35573; -.
DR VEuPathDB; HostDB:ENSG00000163735; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000163567; -.
DR HOGENOM; CLU_143902_1_0_1; -.
DR InParanoid; P42830; -.
DR OMA; CVCLQTT; -.
DR OrthoDB; 1556509at2759; -.
DR PhylomeDB; P42830; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P42830; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P42830; -.
DR BioGRID-ORCS; 6374; 15 hits in 1039 CRISPR screens.
DR GeneWiki; CXCL5; -.
DR GenomeRNAi; 6374; -.
DR Pharos; P42830; Tbio.
DR PRO; PR:P42830; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42830; protein.
DR Bgee; ENSG00000163735; Expressed in monocyte and 123 other tissues.
DR ExpressionAtlas; P42830; baseline and differential.
DR Genevisible; P42830; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR10179; PTHR10179; 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 3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:10095777,
FT ECO:0000269|PubMed:12665801"
FT CHAIN 37..114
FT /note="C-X-C motif chemokine 5"
FT /id="PRO_0000005075"
FT CHAIN 44..114
FT /note="ENA-78(8-78)"
FT /id="PRO_0000005076"
FT CHAIN 45..114
FT /note="ENA-78(9-78)"
FT /id="PRO_0000005077"
FT SITE 44..45
FT /note="Cleavage; by cathepsin G"
FT DISULFID 49..75
FT /evidence="ECO:0000269|PubMed:24695525,
FT ECO:0007744|PDB:2MGS"
FT DISULFID 51..91
FT /evidence="ECO:0000269|PubMed:24695525,
FT ECO:0007744|PDB:2MGS"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2MGS"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2MGS"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:2MGS"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:2MGS"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:2MGS"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2MGS"
SQ SEQUENCE 114 AA; 11972 MW; 56B21EE86AE952D3 CRC64;
MSLLSSRAAR VPGPSSSLCA LLVLLLLLTQ PGPIASAGPA AAVLRELRCV CLQTTQGVHP
KMISNLQVFA IGPQCSKVEV VASLKNGKEI CLDPEAPFLK KVIQKILDGG NKEN
