ID CCL2_HUMAN Reviewed; 99 AA. AC P13500; B2R4V3; Q9UDF3; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 02-MAR-2010, entry version 140. DE RecName: Full=C-C motif chemokine 2; DE AltName: Full=Small-inducible cytokine A2; DE AltName: Full=Monocyte chemoattractant protein 1; DE AltName: Full=Monocyte chemotactic protein 1; DE Short=MCP-1; DE AltName: Full=Monocyte chemotactic and activating factor; DE Short=MCAF; DE AltName: Full=Monocyte secretory protein JE; DE AltName: Full=HC11; DE Flags: Precursor; GN Name=CCL2; Synonyms=MCP1, SCYA2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89165862; PubMed=2923622; DOI=10.1016/0006-291X(89)92430-3; RA Furutani Y., Nomura H., Notake M., Oyamada Y., Fukui T., Yamada M., RA Larsen C.G., Oppenheim J.J., Matsushima K.; RT "Cloning and sequencing of the cDNA for human monocyte chemotactic and RT activating factor (MCAF)."; RL Biochem. Biophys. Res. Commun. 159:249-255(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=90097880; PubMed=2513477; RA Rollins B.J., Stier P., Ernst T., Wong G.G.; RT "The human homolog of the JE gene encodes a monocyte secretory RT protein."; RL Mol. Cell. Biol. 9:4687-4695(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Glial tumor; RX MEDLINE=89153605; PubMed=2465924; DOI=10.1016/0014-5793(89)80590-3; RA Yoshimura T., Yuhki N., Moore S.K., Appella E., Lerman M.I., RA Leonard E.J.; RT "Human monocyte chemoattractant protein-1 (MCP-1). Full-length cDNA RT cloning, expression in mitogen-stimulated blood mononuclear RT leukocytes, and sequence similarity to mouse competence gene JE."; RL FEBS Lett. 244:487-493(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=91207938; PubMed=2518726; DOI=10.1093/intimm/1.4.388; RA Chang H.C., Hsu F., Freeman G.J., Griffin J.D., Reinherz E.L.; RT "Cloning and expression of a gamma-interferon-inducible gene in RT monocytes: a new member of a cytokine gene family."; RL Int. Immunol. 1:388-397(1989). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90290466; PubMed=2357211; DOI=10.1016/0006-291X(90)90338-N; RA Shyy Y.J., Li Y.S., Kolattukudy P.E.; RT "Structure of human monocyte chemotactic protein gene and its RT regulation by TPA."; RL Biochem. Biophys. Res. Commun. 169:346-351(1990). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92095166; PubMed=1661560; RA Yoshimura T., Leonard E.J.; RT "Human monocyte chemoattractant protein-1 (MCP-1)."; RL Adv. Exp. Med. Biol. 305:47-56(1991). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94150478; PubMed=8107690; DOI=10.1007/BF01772208; RA Li Y.S., Shyy Y.J., Wright J.G., Valente A.J., Cornhill J.F., RA Kolattukudy P.E.; RT "The expression of monocyte chemotactic protein (MCP-1) in human RT vascular endothelium in vitro and in vivo."; RL Mol. Cell. Biochem. 126:61-68(1993). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20374005; PubMed=10918580; DOI=10.1038/sj.onc.1203643; RA Finzer P., Soto U., Delius H., Patzelt A., Poustka A., Coy J.F., RA zur Hausen H., Roesl F.; RT "Differential transcriptional regulation of the monocyte- RT chemoattractant protein-1 (MCP-1) gene in tumorigenic and non- RT tumorigenic HPV 18 positive cells: the role of the chromatin structure RT and AP-1 composition."; RL Oncogene 19:3235-3244(2000). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Caput D., Ferrara P., Miloux B., Minty A., Vita N.; RT "Protein with cytokine activity, recombinant DNA, expression vector RT and hosts for obtaining it."; RL Patent number EP0488900, 03-JUN-1992. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Urinary bladder; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [15] RP PROTEIN SEQUENCE OF 24-99. RX MEDLINE=89184525; PubMed=2648385; DOI=10.1073/pnas.86.6.1850; RA Robinson E.A., Yoshimura T., Leonard E.J., Tanaka S., Griffin P.R., RA Shabanowitz J., Hunt D.F., Appella E.; RT "Complete amino acid sequence of a human monocyte chemoattractant, a RT putative mediator of cellular immune reactions."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1850-1854(1989). RN [16] RP PROTEIN SEQUENCE OF 29-53 AND 82-92. RX MEDLINE=90211336; PubMed=2322286; DOI=10.1016/0006-291X(90)90609-Q; RA Decock B., Conings R., Lenaerts J.-P., Biliau A., van Damme J.; RT "Identification of the monocyte chemotactic protein from human RT osteosarcoma cells and monocytes: detection of a novel N-terminally RT processed form."; RL Biochem. Biophys. Res. Commun. 167:904-909(1990). RN [17] RP GENE STRUCTURE. RX MEDLINE=91301709; PubMed=2071154; DOI=10.1016/0888-7543(91)90338-F; RA Rollins B.J., Morton C.C., Ledbetter D.H., Eddy R.L. Jr., Shows T.B.; RT "Assignment of the human small inducible cytokine A2 gene, SCYA2 RT (encoding JE or MCP-1), to 17q11.2-12: evolutionary relatedness of RT cytokines clustered at the same locus."; RL Genomics 10:489-492(1991). RN [18] RP MUTAGENESIS. RX MEDLINE=94253189; PubMed=8195247; RA Zhang Y.J., Rutledge B.J., Rollins B.J.; RT "Structure/activity analysis of human monocyte chemoattractant RT protein-1 (MCP-1) by mutagenesis. Identification of a mutated protein RT that inhibits MCP-1-mediated monocyte chemotaxis."; RL J. Biol. Chem. 269:15918-15924(1994). RN [19] RP EFFECT OF DELETION OF N-TERMINAL RESIDUES. RX MEDLINE=96195223; PubMed=8627182; DOI=10.1084/jem.183.2.681; RA Weber M., Uguccioni M., Baggiolini M., Clark-Lewis I., Dahinden C.A.; RT "Deletion of the NH2-terminal residue converts monocyte chemotactic RT protein 1 from an activator of basophil mediator release to an RT eosinophil chemoattractant."; RL J. Exp. Med. 183:681-685(1996). RN [20] RP SUBUNIT. RX MEDLINE=97053697; PubMed=8898111; DOI=10.1016/0014-5793(96)01024-1; RA Kim K.-S., Rajarathnam K., Clark-Lewis I., Sykes B.D.; RT "Structural characterization of a monomeric chemokine: monocyte RT chemoattractant protein-3."; RL FEBS Lett. 395:277-282(1996). RN [21] RP GAG BINDING SITES LYS-81 AND HIS-89, AND MUTAGENESIS OF LYS-81; HIS-89 RP AND 95-GLN--THR-99. RX PubMed=9792674; DOI=10.1074/jbc.273.45.29641; RA Chakravarty L., Rogers L., Quach T., Breckenridge S., RA Kolattukudy P.E.; RT "Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte RT chemoattractant protein-1 are essential for glycosaminoglycan RT binding."; RL J. Biol. Chem. 273:29641-29647(1998). RN [22] RP HOMODIMERIZATION, AND MUTAGENESIS OF PRO-31; VAL-32; THR-33 AND RP TYR-36. RX PubMed=9837883; DOI=10.1074/jbc.273.50.33157; RA Paavola C.D., Hemmerich S., Grunberger D., Polsky I., Bloom A., RA Freedman R., Mulkins M., Bhakta S., McCarley D., Wiesent L., Wong B., RA Jarnagin K., Handel T.M.; RT "Monomeric monocyte chemoattractant protein-1 (MCP-1) binds and RT activates the MCP-1 receptor CCR2B."; RL J. Biol. Chem. 273:33157-33165(1998). RN [23] RP MUTAGENESIS OF 25-PRO--PRO-31; ASP-26; ILE-28; ASN-29; PRO-31; VAL-32 RP AND THR-33. RX PubMed=10587439; DOI=10.1021/bi9912239; RA Jarnagin K., Grunberger D., Mulkins M., Wong B., Hemmerich S., RA Paavola C., Bloom A., Bhakta S., Diehl F., Freedman R., McCarley D., RA Polsky I., Ping-Tsou A., Kosaka A., Handel T.M.; RT "Identification of surface residues of the monocyte chemotactic RT protein 1 that affect signaling through the receptor CCR2."; RL Biochemistry 38:16167-16177(1999). RN [24] RP IMPORTANCE OF TYR-36; ARG-47; LYS-58; LYS-61 AND LYS-72 FOR RECEPTOR RP BINDING, AND MUTAGENESIS. RX PubMed=10529171; DOI=10.1021/bi991029m; RA Hemmerich S., Paavola C., Bloom A., Bhakta S., Freedman R., RA Grunberger D., Krstenansky J., Lee S., McCarley D., Mulkins M., RA Wong B., Pease J., Mizoue L., Mirzadegan T., Polsky I., Thompson K., RA Handel T.M., Jarnagin K.; RT "Identification of residues in the monocyte chemotactic protein-1 that RT contact the MCP-1 receptor, CCR2."; RL Biochemistry 38:13013-13025(1999). RN [25] RP GAG BINDING SITES ARG-41; LYS-42 AND ARG-47, AND MUTAGENESIS. RX PubMed=15033992; DOI=10.1074/jbc.M311224200; RA Lau E.K., Paavola C.D., Johnson Z., Gaudry J.-P., Geretti E., RA Borlat F., Kungl A.J., Proudfoot A.E., Handel T.M.; RT "Identification of the glycosaminoglycan binding site of the CC RT chemokine, MCP-1: implications for structure and function in vivo."; RL J. Biol. Chem. 279:22294-22305(2004). RN [26] RP 3D-STRUCTURE MODELING. RX MEDLINE=91312872; PubMed=1857712; DOI=10.1093/protein/4.3.263; RA Gronenborn A.M., Clore G.M.; RT "Modeling the three-dimensional structure of the monocyte chemo- RT attractant and activating protein MCAF/MCP-1 on the basis of the RT solution structure of interleukin-8."; RL Protein Eng. 4:263-269(1991). RN [27] RP STRUCTURE BY NMR. RX MEDLINE=96234959; PubMed=8639605; DOI=10.1021/bi9602270; RA Handel T.M., Domaille P.J.; RT "Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure RT of the monocyte chemoattractant protein-1 (MCP-1) dimer."; RL Biochemistry 35:6569-6584(1996). RN [28] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX MEDLINE=97143315; PubMed=8989326; DOI=10.1038/nsb0197-64; RA Lubkowski J., Bujacz G., Domaille P.J., Handel T.M., Wlodawer A.; RT "The structure of MCP-1 in two crystal forms provides a rare example RT of variable quaternary interactions."; RL Nat. Struct. Biol. 4:64-69(1997). RN [29] RP INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY. RX PubMed=16352737; DOI=10.1084/jem.20050126; RA Flores-Villanueva P.O., Ruiz-Morales J.A., Song C.-H., Flores L.M., RA Jo E.-K., Montano M., Barnes P.F., Selman M., Granados J.; RT "A functional promoter polymorphism in monocyte chemoattractant RT protein-1 is associated with increased susceptibility to pulmonary RT tuberculosis."; RL J. Exp. Med. 202:1649-1658(2005). CC -!- FUNCTION: Chemotactic factor that attracts monocytes and basophils CC but not neutrophils or eosinophils. Augments monocyte anti-tumor CC activity. Has been implicated in the pathogenesis of diseases CC characterized by monocytic infiltrates, like psoriasis, rheumatoid CC arthritis or atherosclerosis. May be involved in the recruitment CC of monocytes into the arterial wall during the disease process of CC atherosclerosis. CC -!- SUBUNIT: Monomer or homodimer; in equilibrium. Binds to CCR2 and CC CCR4. Is tethered on endothelial cells by glycosaminoglycan (GAG) CC side chains of proteoglycans. CC -!- INTERACTION: CC O41925:GAMMAHV.M3 (xeno); NbExp=1; IntAct=EBI-1034732, EBI-1034728; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Processing at the N-terminus can regulate receptor and target CC cell selectivity. Deletion of the N-terminal residue converts it CC from an activator of basophil to an eosinophil chemoattractant. CC -!- POLYMORPHISM: Genetic variations in CCL2 determine Mycobacterium CC tuberculosis susceptibility [MIM:607948]. CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL2 entry; CC URL="http://en.wikipedia.org/wiki/CCL2"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/scya2/"; 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; M24545; AAA18164.1; -; mRNA. DR EMBL; M28225; AAA60308.1; -; Genomic_DNA. DR EMBL; M28223; AAA60308.1; JOINED; Genomic_DNA. DR EMBL; M28224; AAA60308.1; JOINED; Genomic_DNA. DR EMBL; M28226; AAA60309.1; -; mRNA. DR EMBL; M31626; AAA36330.1; -; Genomic_DNA. DR EMBL; M30816; AAA36330.1; JOINED; Genomic_DNA. DR EMBL; M31625; AAA36330.1; JOINED; Genomic_DNA. DR EMBL; X14768; CAA32876.1; -; mRNA. DR EMBL; M37719; AAA18102.1; -; Genomic_DNA. DR EMBL; S71513; AAB20651.1; -; mRNA. DR EMBL; S69738; AAB29926.1; -; mRNA. DR EMBL; Y18933; CAC14049.1; -; Genomic_DNA. DR EMBL; A17786; CAA01352.1; -; mRNA. DR EMBL; BT007329; AAP35993.1; -; mRNA. DR EMBL; AF519531; AAM54046.1; -; Genomic_DNA. DR EMBL; AK311960; BAG34900.1; -; mRNA. DR EMBL; CH471147; EAW80212.1; -; Genomic_DNA. DR EMBL; BC009716; AAH09716.1; -; mRNA. DR IPI; IPI00009308; -. DR PIR; A35474; A60299. DR RefSeq; NP_002973.1; -. DR UniGene; Hs.303649; -. DR PDB; 1DOK; X-ray; 1.85 A; A/B=24-99. DR PDB; 1DOL; X-ray; 2.40 A; A=24-99. DR PDB; 1DOM; NMR; -; A/B=24-99. DR PDB; 1DON; NMR; -; A/B=24-99. DR PDB; 1MCA; Model; -; A/B=24-96. DR PDB; 1ML0; X-ray; 2.80 A; D=24-99. DR PDB; 2BDN; X-ray; 2.53 A; A=24-99. DR PDB; 2NZ1; X-ray; 2.50 A; D/E/Y=24-99. DR PDB; 3IFD; X-ray; 1.90 A; A=24-99. DR PDBsum; 1DOK; -. DR PDBsum; 1DOL; -. DR PDBsum; 1DOM; -. DR PDBsum; 1DON; -. DR PDBsum; 1MCA; -. DR PDBsum; 1ML0; -. DR PDBsum; 2BDN; -. DR PDBsum; 2NZ1; -. DR PDBsum; 3IFD; -. DR DIP; DIP-5838N; -. DR IntAct; P13500; 1. DR STRING; P13500; -. DR Ensembl; ENST00000225831; ENSP00000225831; ENSG00000108691; Homo sapiens. DR GeneID; 6347; -. DR KEGG; hsa:6347; -. DR UCSC; uc002hhy.1; human. DR CTD; 6347; -. DR GeneCards; GC17P029606; -. DR H-InvDB; HIX0013714; -. DR HGNC; HGNC:10618; CCL2. DR HPA; CAB013676; -. DR HPA; HPA019163; -. DR MIM; 158105; gene. DR MIM; 607948; phenotype. DR PharmGKB; PA130413151; -. DR eggNOG; prNOG20983; -. DR HOGENOM; HBG505826; -. DR HOVERGEN; HBG017871; -. DR InParanoid; P13500; -. DR OMA; CCYTLTN; -. DR OrthoDB; EOG9FJBV0; -. DR PhylomeDB; P13500; -. DR Pathway_Interaction_DB; il23pathway; IL23-mediated signaling events. DR DrugBank; DB01076; Atorvastatin. DR DrugBank; DB01406; Danazol. DR DrugBank; DB01055; Mimosine. DR DrugBank; DB00641; Simvastatin. DR NextBio; 24660; -. DR PMAP-CutDB; P13500; -. DR ArrayExpress; P13500; -. DR Bgee; P13500; -. DR CleanEx; HS_CCL2; -. DR Genevestigator; P13500; -. DR GermOnline; ENSG00000108691; Homo sapiens. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0031727; F:CCR2 chemokine receptor binding; TAS:UniProtKB. DR GO; GO:0008009; F:chemokine activity; TAS:ProtInc. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc. DR GO; GO:0006916; P:anti-apoptosis; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:ProtInc. DR GO; GO:0007187; P:G-protein signaling, coupled to cyclic nucl...; TAS:ProtInc. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc. DR GO; GO:0048246; P:macrophage chemotaxis; IDA:UniProtKB. DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc. DR GO; GO:0019079; P:viral genome replication; TAS:ProtInc. DR InterPro; IPR000827; CC_chemkine_sml_CS. DR InterPro; IPR001811; Chemokine_IL8. DR Pfam; PF00048; IL8; 1. DR SMART; SM00199; SCY; 1. DR SUPFAM; SSF54117; Chemokine_IL8; 1. DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Complete proteome; Cytokine; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Inflammatory response; Pyrrolidone carboxylic acid; Secreted; Signal. FT SIGNAL 1 23 FT CHAIN 24 99 C-C motif chemokine 2. FT /FTId=PRO_0000005146. FT SITE 31 31 Involved in dimerization. FT SITE 36 36 Involved in dimerization, receptor FT binding and signaling. FT SITE 41 41 Involved in GAG binding. FT SITE 42 42 Involved in GAG binding. FT SITE 47 47 Involved in GAG binding and receptor FT binding. FT SITE 58 58 Involved in dimerization. FT SITE 61 61 Involved in dimerization. FT SITE 72 72 Involved in GAG binding and receptor FT binding. FT SITE 81 81 Involved in GAG binding. FT SITE 89 89 Involved in GAG binding. FT MOD_RES 24 24 Pyrrolidone carboxylic acid. FT CARBOHYD 37 37 N-linked (GlcNAc...) (Potential). FT DISULFID 34 59 FT DISULFID 35 75 FT MUTAGEN 24 91 Missing: 83% reduction in activity. FT MUTAGEN 24 85 Missing: 90% reduction in activity. FT MUTAGEN 24 24 Missing: Loss of activity. FT MUTAGEN 25 31 Missing: Loss of signaling. FT MUTAGEN 26 26 D->A: Reduction in activity. FT MUTAGEN 28 28 I->A: Slight reduction in activity. FT MUTAGEN 29 29 N->A: 50% reduction in activity. FT MUTAGEN 31 31 P->A: Loss of dimerization; slight FT reduction of activity. FT MUTAGEN 32 32 V->A: Slight reduction in activity. FT MUTAGEN 32 32 V->E: Slight reduction in affinity. FT MUTAGEN 33 33 T->A: Slight reduction in activity. FT MUTAGEN 33 33 T->E: Slight reduction in affinity. FT MUTAGEN 36 36 Y->A: Loss of activity. FT MUTAGEN 47 47 R->F: 95% reduction in activity; strong FT reduction of receptor binding. FT MUTAGEN 50 50 S->Q: 40% reduction in activity. FT MUTAGEN 51 51 Y->D: Loss of activity. FT MUTAGEN 53 53 R->L: Loss of activity. FT MUTAGEN 79 79 K->A: No effect on heparin binding. FT MUTAGEN 81 81 K->A: Strongly reduces heparin binding. FT MUTAGEN 89 89 H->A: Strongly reduces heparin binding. FT MUTAGEN 91 91 D->L: 90% reduction in activity. FT MUTAGEN 95 99 Missing: No effect on heparin binding. FT HELIX 25 29 FT STRAND 32 34 FT HELIX 45 47 FT STRAND 48 54 FT STRAND 59 61 FT STRAND 63 68 FT STRAND 73 76 FT HELIX 81 92 SQ SEQUENCE 99 AA; 11025 MW; 45EC72361435302F CRC64; MKVSAALLCL LLIAATFIPQ GLAQPDAINA PVTCCYNFTN RKISVQRLAS YRRITSSKCP KEAVIFKTIV AKEICADPKQ KWVQDSMDHL DKQTQTPKT //