CXCL2_HUMAN
ID CXCL2_HUMAN Reviewed; 107 AA.
AC P19875; Q6FGD6; Q9UPB8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=C-X-C motif chemokine 2;
DE AltName: Full=Growth-regulated protein beta;
DE Short=Gro-beta;
DE AltName: Full=Macrophage inflammatory protein 2-alpha;
DE Short=MIP2-alpha;
DE Contains:
DE RecName: Full=GRO-beta(5-73);
DE AltName: Full=GRO-beta-T;
DE AltName: Full=Hematopoietic synergistic factor;
DE Short=HSF;
DE AltName: Full=SB-251353;
DE Flags: Precursor;
GN Name=CXCL2; Synonyms=GRO2, GROB, MIP2A, SCYB2;
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=2078213; DOI=10.1128/mcb.10.10.5596-5599.1990;
RA Iida N., Grotendorst G.R.;
RT "Cloning and sequencing of a new gro transcript from activated human
RT monocytes: expression in leukocytes and wound tissue.";
RL Mol. Cell. Biol. 10:5596-5599(1990).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-107.
RA Jang J.S., Kim B.E.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-107.
RX PubMed=2341726;
RA Sporn S.A., Eierman D.F., Johnson C.E., Morris J., Martin G., Ladner M.,
RA Haskill S.;
RT "Monocyte adherence results in selective induction of novel genes sharing
RT homology with mediators of inflammation and tissue repair.";
RL J. Immunol. 144:4434-4441(1990).
RN [9]
RP PROTEIN SEQUENCE OF 39-56, IDENTIFICATION OF GRO-BETA(5-73) BY MASS
RP SPECTROMETRY, PROTEOLYTIC PROCESSING OF N-TERMINUS, AND FUNCTION.
RX PubMed=10725737; DOI=10.4049/jimmunol.164.7.3774;
RA King A.G., Johanson K., Frey C.L., DeMarsh P.L., White J.R., McDevitt P.,
RA McNulty D., Balcarek J., Jonak Z.L., Bhatnagar P.K., Pelus L.M.;
RT "Identification of unique truncated KC/GRO beta chemokines with potent
RT hematopoietic and anti-infective activities.";
RL J. Immunol. 164:3774-3782(2000).
RN [10]
RP STRUCTURE BY NMR OF 39-107.
RX PubMed=10600366; DOI=10.1006/jmbi.1999.3333;
RA Qian Y.Q., Johanson K.O., McDevitt P.;
RT "Nuclear magnetic resonance solution structure of truncated human GRObeta
RT [5-73] and its structural comparison with CXC chemokine family members
RT GROalpha and IL-8.";
RL J. Mol. Biol. 294:1065-1072(1999).
CC -!- FUNCTION: Produced by activated monocytes and neutrophils and expressed
CC at sites of inflammation. Hematoregulatory chemokine, which, in vitro,
CC suppresses hematopoietic progenitor cell proliferation. GRO-beta(5-73)
CC shows a highly enhanced hematopoietic activity.
CC {ECO:0000269|PubMed:10725737}.
CC -!- INTERACTION:
CC P19875; P13501: CCL5; NbExp=2; IntAct=EBI-2114901, EBI-2848366;
CC P19875; P48061: CXCL12; NbExp=2; IntAct=EBI-2114901, EBI-3913254;
CC P19875; P27487: DPP4; NbExp=2; IntAct=EBI-2114901, EBI-2871277;
CC P19875; P02776: PF4; NbExp=3; IntAct=EBI-2114901, EBI-2565740;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The N-terminal processed form GRO-beta(5-73) is produced by
CC proteolytic cleavage after secretion from bone marrow stromal cells.
CC {ECO:0000269|PubMed:10725737}.
CC -!- PHARMACEUTICAL: GRO-beta(5-73) is available under the name Garnocestim
CC as immunomodulator. It is used prior to hematopoietic transplantation
CC for peripheral blood stem cell mobilization and reduction of incidence,
CC duration, and/or severity of chemotherapy induced cytopenias.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL2 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL2";
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DR EMBL; X53799; CAA37808.1; -; mRNA.
DR EMBL; M36820; AAA63183.1; -; mRNA.
DR EMBL; M57731; AAA63182.1; -; mRNA.
DR EMBL; CR542171; CAG46968.1; -; mRNA.
DR EMBL; CH471057; EAX05700.1; -; Genomic_DNA.
DR EMBL; BC015753; AAH15753.1; -; mRNA.
DR EMBL; AF043340; AAC03540.1; -; mRNA.
DR CCDS; CCDS34008.1; -.
DR PIR; JH0281; JH0281.
DR RefSeq; NP_002080.1; NM_002089.3.
DR PDB; 1QNK; NMR; -; A/B=39-107.
DR PDB; 5OB5; X-ray; 1.65 A; A=40-102.
DR PDBsum; 1QNK; -.
DR PDBsum; 5OB5; -.
DR AlphaFoldDB; P19875; -.
DR SMR; P19875; -.
DR BioGRID; 109177; 22.
DR DIP; DIP-5908N; -.
DR IntAct; P19875; 18.
DR MINT; P19875; -.
DR STRING; 9606.ENSP00000427279; -.
DR BindingDB; P19875; -.
DR ChEMBL; CHEMBL3286076; -.
DR BioMuta; CXCL2; -.
DR DMDM; 127085; -.
DR MassIVE; P19875; -.
DR MaxQB; P19875; -.
DR PaxDb; P19875; -.
DR PeptideAtlas; P19875; -.
DR PRIDE; P19875; -.
DR ProteomicsDB; 53697; -.
DR Antibodypedia; 13343; 496 antibodies from 32 providers.
DR DNASU; 2920; -.
DR Ensembl; ENST00000508487.3; ENSP00000427279.1; ENSG00000081041.9.
DR GeneID; 2920; -.
DR KEGG; hsa:2920; -.
DR MANE-Select; ENST00000508487.3; ENSP00000427279.1; NM_002089.4; NP_002080.1.
DR UCSC; uc003hhm.5; human.
DR CTD; 2920; -.
DR DisGeNET; 2920; -.
DR GeneCards; CXCL2; -.
DR HGNC; HGNC:4603; CXCL2.
DR HPA; ENSG00000081041; Tissue enriched (liver).
DR MIM; 139110; gene.
DR neXtProt; NX_P19875; -.
DR OpenTargets; ENSG00000081041; -.
DR PharmGKB; PA35051; -.
DR VEuPathDB; HostDB:ENSG00000081041; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000163986; -.
DR HOGENOM; CLU_143902_1_1_1; -.
DR InParanoid; P19875; -.
DR OMA; PHCSNLE; -.
DR OrthoDB; 1618797at2759; -.
DR PhylomeDB; P19875; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P19875; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; P19875; -.
DR BioGRID-ORCS; 2920; 57 hits in 1004 CRISPR screens.
DR ChiTaRS; CXCL2; human.
DR EvolutionaryTrace; P19875; -.
DR GenomeRNAi; 2920; -.
DR Pharos; P19875; Tbio.
DR PRO; PR:P19875; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P19875; protein.
DR Bgee; ENSG00000081041; Expressed in mucosa of paranasal sinus and 179 other tissues.
DR ExpressionAtlas; P19875; baseline and differential.
DR Genevisible; P19875; 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: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:0006935; P:chemotaxis; TAS:ProtInc.
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; IBA:GO_Central.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:BHF-UCL.
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; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Inflammatory response; Pharmaceutical; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..34
FT CHAIN 35..107
FT /note="C-X-C motif chemokine 2"
FT /id="PRO_0000005063"
FT CHAIN 39..107
FT /note="GRO-beta(5-73)"
FT /id="PRO_0000005064"
FT DISULFID 43..69
FT DISULFID 45..85
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1QNK"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5OB5"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5OB5"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5OB5"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5OB5"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5OB5"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:5OB5"
SQ SEQUENCE 107 AA; 11389 MW; 740F277E928571BA CRC64;
MARATLSAAP SNPRLLRVAL LLLLLVAASR RAAGAPLATE LRCQCLQTLQ GIHLKNIQSV
KVKSPGPHCA QTEVIATLKN GQKACLNPAS PMVKKIIEKM LKNGKSN
