CXCL3_HUMAN
ID CXCL3_HUMAN Reviewed; 107 AA.
AC P19876; Q4W5H9;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=C-X-C motif chemokine 3;
DE AltName: Full=GRO-gamma(1-73);
DE AltName: Full=Growth-regulated protein gamma;
DE Short=GRO-gamma;
DE AltName: Full=Macrophage inflammatory protein 2-beta;
DE Short=MIP2-beta;
DE Contains:
DE RecName: Full=GRO-gamma(5-73);
DE Flags: Precursor;
GN Name=CXCL3; Synonyms=GRO3, GROG, SCYB3;
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].
RC TISSUE=Histiocytic lymphoma;
RX PubMed=2201751; DOI=10.1084/jem.172.3.911;
RA Tekamp-Olson P., Gallegos C., Bauer D., McClain J., Sherry B., Fabre M.,
RA van Deventer S., Cerami A.;
RT "Cloning and characterization of cDNAs for murine macrophage inflammatory
RT protein 2 and its human homologues.";
RL J. Exp. Med. 172:911-919(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2217207; DOI=10.1073/pnas.87.19.7732;
RA Haskill S., Peace A., Morris J., Sporn S.A., Anisowicz A., Lee S.W.,
RA Smith T., Martin G., Ralph P., Sager R.;
RT "Identification of three related human GRO genes encoding cytokine
RT functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7732-7736(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 35-49.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP PROTEIN SEQUENCE OF 39-45, IDENTIFICATION OF GRO-GAMMA(5-73), PROTEOLYTIC
RP 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).
CC -!- FUNCTION: Ligand for CXCR2 (By similarity). Has chemotactic activity
CC for neutrophils. May play a role in inflammation and exert its effects
CC on endothelial cells in an autocrine fashion. In vitro, the processed
CC form GRO-gamma(5-73) shows a fivefold higher chemotactic activity for
CC neutrophilic granulocytes. {ECO:0000250, ECO:0000269|PubMed:10095777}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-terminal processed form GRO-gamma(5-73) is produced by
CC proteolytic cleavage after secretion from peripheral blood monocytes.
CC {ECO:0000269|PubMed:10095777}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL3 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL3";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53800; CAA37809.1; -; mRNA.
DR EMBL; M36821; AAA63184.1; -; mRNA.
DR EMBL; AC097709; AAY41006.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05698.1; -; Genomic_DNA.
DR EMBL; BC016308; AAH16308.1; -; mRNA.
DR EMBL; BC065743; AAH65743.1; -; mRNA.
DR CCDS; CCDS34007.1; -.
DR PIR; JH0282; B38290.
DR RefSeq; NP_002081.2; NM_002090.2.
DR AlphaFoldDB; P19876; -.
DR SMR; P19876; -.
DR BioGRID; 109178; 12.
DR DIP; DIP-5909N; -.
DR IntAct; P19876; 4.
DR STRING; 9606.ENSP00000296026; -.
DR BioMuta; CXCL3; -.
DR DMDM; 127086; -.
DR EPD; P19876; -.
DR MassIVE; P19876; -.
DR PaxDb; P19876; -.
DR PeptideAtlas; P19876; -.
DR PRIDE; P19876; -.
DR ProteomicsDB; 53698; -.
DR Antibodypedia; 13341; 289 antibodies from 30 providers.
DR DNASU; 2921; -.
DR Ensembl; ENST00000296026.4; ENSP00000296026.4; ENSG00000163734.4.
DR GeneID; 2921; -.
DR KEGG; hsa:2921; -.
DR MANE-Select; ENST00000296026.4; ENSP00000296026.4; NM_002090.3; NP_002081.2.
DR UCSC; uc003hhl.5; human.
DR CTD; 2921; -.
DR DisGeNET; 2921; -.
DR GeneCards; CXCL3; -.
DR HGNC; HGNC:4604; CXCL3.
DR HPA; ENSG00000163734; Tissue enhanced (adipose tissue, cervix).
DR MIM; 139111; gene.
DR neXtProt; NX_P19876; -.
DR OpenTargets; ENSG00000163734; -.
DR PharmGKB; PA35052; -.
DR VEuPathDB; HostDB:ENSG00000163734; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000163986; -.
DR HOGENOM; CLU_143902_1_1_1; -.
DR InParanoid; P19876; -.
DR OMA; QPEVIAM; -.
DR OrthoDB; 1618797at2759; -.
DR PhylomeDB; P19876; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P19876; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P19876; -.
DR BioGRID-ORCS; 2921; 15 hits in 1008 CRISPR screens.
DR GeneWiki; CXCL3; -.
DR GenomeRNAi; 2921; -.
DR Pharos; P19876; Tbio.
DR PRO; PR:P19876; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P19876; protein.
DR Bgee; ENSG00000163734; Expressed in cartilage tissue and 129 other tissues.
DR Genevisible; P19876; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; ISS:UniProtKB.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
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:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
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 Chemotaxis; Cytokine; Direct protein sequencing; Disulfide bond;
KW Inflammatory response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 35..107
FT /note="C-X-C motif chemokine 3"
FT /id="PRO_0000005065"
FT CHAIN 39..107
FT /note="GRO-gamma(5-73)"
FT /id="PRO_0000005066"
FT DISULFID 43..69
FT /evidence="ECO:0000250"
FT DISULFID 45..85
FT /evidence="ECO:0000250"
FT VARIANT 3
FT /note="H -> R (in dbSNP:rs352043)"
FT /id="VAR_059210"
FT CONFLICT 27..28
FT /note="AA -> G (in Ref. 2; AAA63184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 11342 MW; 97A69946B7F1F070 CRC64;
MAHATLSAAP SNPRLLRVAL LLLLLVAASR RAAGASVVTE LRCQCLQTLQ GIHLKNIQSV
NVRSPGPHCA QTEVIATLKN GKKACLNPAS PMVQKIIEKI LNKGSTN
