CXCL2_MOUSE
ID CXCL2_MOUSE Reviewed; 100 AA.
AC P10889;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=C-X-C motif chemokine 2;
DE AltName: Full=Macrophage inflammatory protein 2;
DE Short=MIP2;
DE Flags: Precursor;
GN Name=Cxcl2; Synonyms=Mip-2, Mip2, Scyb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 PROTEIN SEQUENCE OF 28-59.
RX PubMed=2643119; DOI=10.1073/pnas.86.2.612;
RA Wolpe S.D., Sherry B., Juers D., Davatelis G., Yurt R.W., Cerami A.;
RT "Identification and characterization of macrophage inflammatory protein
RT 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:612-616(1989).
RN [3]
RP STRUCTURE BY NMR OF 28-100.
RX PubMed=9622482; DOI=10.1021/bi980112r;
RA Shao W., Jerva L.F., West J., Lolis E., Schweitzer B.I.;
RT "Solution structure of murine macrophage inflammatory protein-2.";
RL Biochemistry 37:8303-8313(1998).
CC -!- FUNCTION: Chemotactic for human polymorphonuclear leukocytes but does
CC not induce chemokinesis or an oxidative burst.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; X53798; CAA37807.1; -; mRNA.
DR CCDS; CCDS39144.1; -.
DR PIR; JH0200; JH0200.
DR RefSeq; NP_033166.1; NM_009140.2.
DR PDB; 1MI2; NMR; -; A/B=28-100.
DR PDB; 3N52; X-ray; 1.90 A; A/B/C/D=28-100.
DR PDBsum; 1MI2; -.
DR PDBsum; 3N52; -.
DR AlphaFoldDB; P10889; -.
DR SMR; P10889; -.
DR BioGRID; 203135; 1.
DR DIP; DIP-61570N; -.
DR IntAct; P10889; 1.
DR STRING; 10090.ENSMUSP00000074885; -.
DR PaxDb; P10889; -.
DR PRIDE; P10889; -.
DR ProteomicsDB; 283986; -.
DR ABCD; P10889; 2 sequenced antibodies.
DR DNASU; 20310; -.
DR Ensembl; ENSMUST00000075433; ENSMUSP00000074885; ENSMUSG00000058427.
DR GeneID; 20310; -.
DR KEGG; mmu:20310; -.
DR UCSC; uc008ybm.1; mouse.
DR CTD; 2920; -.
DR MGI; MGI:1340094; Cxcl2.
DR VEuPathDB; HostDB:ENSMUSG00000058427; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000155233; -.
DR InParanoid; P10889; -.
DR OMA; QPEVIAM; -.
DR OrthoDB; 1617719at2759; -.
DR PhylomeDB; P10889; -.
DR TreeFam; TF333433; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 20310; 1 hit in 75 CRISPR screens.
DR EvolutionaryTrace; P10889; -.
DR PRO; PR:P10889; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P10889; protein.
DR Bgee; ENSMUSG00000058427; Expressed in granulocyte and 38 other tissues.
DR ExpressionAtlas; P10889; baseline and differential.
DR Genevisible; P10889; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0008009; F:chemokine activity; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
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:0030595; P:leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0070997; P:neuron death; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:2643119"
FT CHAIN 28..100
FT /note="C-X-C motif chemokine 2"
FT /id="PRO_0000005061"
FT DISULFID 36..62
FT DISULFID 38..78
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1MI2"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1MI2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1MI2"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3N52"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3N52"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1MI2"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3N52"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:3N52"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:3N52"
SQ SEQUENCE 100 AA; 10621 MW; B9EF0A3218EE92B5 CRC64;
MAPPTCRLLS AALVLLLLLA TNHQATGAVV ASELRCQCLK TLPRVDFKNI QSLSVTPPGP
HCAQTEVIAT LKGGQKVCLD PEAPLVQKII QKILNKGKAN
