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   27-MAR-2024, entry version 189.
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; 9606-ENSP00000296027; -.
DR   PeptideAtlas; P42830; -.
DR   ProteomicsDB; 55559; -.
DR   ABCD; P42830; 2 sequenced antibodies.
DR   Antibodypedia; 13336; 595 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   AGR; HGNC:10642; -.
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; HPKMISN; -.
DR   OrthoDB; 4170999at2759; -.
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 1117 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 cell types or tissues.
DR   ExpressionAtlas; P42830; baseline and differential.
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   Gene3D; 2.40.50.40; -; 1.
DR   InterPro; IPR039809; Chemokine_b/g/d.
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; PTHR12015:SF190; C-X-C MOTIF CHEMOKINE 5; 1.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR00436; INTERLEUKIN8.
DR   PRINTS; PR00437; SMALLCYTKCXC.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 1.
DR   PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
DR   Genevisible; P42830; HS.
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
//