ID CCL7_HUMAN Reviewed; 99 AA. AC P80098; Q569J6; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 3. DT 02-OCT-2024, entry version 200. DE RecName: Full=C-C motif chemokine 7; DE AltName: Full=Monocyte chemoattractant protein 3; DE AltName: Full=Monocyte chemotactic protein 3; DE Short=MCP-3; DE AltName: Full=NC28; DE AltName: Full=Small-inducible cytokine A7; DE Flags: Precursor; GN Name=CCL7; Synonyms=MCP3, SCYA6, SCYA7; 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], AND PROTEIN SEQUENCE OF 31-67 AND 71-99. RX PubMed=8461011; DOI=10.1006/bbrc.1993.1251; RA Opdenakker G., Froyen G., Fiten P., Proost P., van Damme J.; RT "Human monocyte chemotactic protein-3 (MCP-3): molecular cloning of the RT cDNA and comparison with other chemokines."; RL Biochem. Biophys. Res. Commun. 191:535-542(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=7916328; DOI=10.1006/geno.1994.1283; RA Opdenakker G., Fiten P., Nys G., Froyen G., van Roy N., Speleman F., RA Laureys G., van Damme J.; RT "The human MCP-3 gene (SCYA7): cloning, sequence analysis, and assignment RT to the C-C chemokine gene cluster on chromosome 17q11.2-q12."; RL Genomics 21:403-408(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8318676; RA Minty A., Chalon P., Guillemot J.-C., Kaghad M., Liauzun P., Magazin M., RA Miloux B., Minty C., Ramond P., Vita N., Lupker J., Shire D., Ferrara P., RA Caput D.; RT "Molecular cloning of the MCP-3 chemokine gene and regulation of its RT expression."; RL Eur. Cytokine Netw. 4:99-110(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood, and Colon; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-99. RA Jang J.S., Kim B.E.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP PROTEIN SEQUENCE OF 30-99. RC TISSUE=Osteosarcoma; RX PubMed=1613466; DOI=10.1084/jem.176.1.59; RA van Damme J., Proost P., Lenaerts J.-P., Opdenakker G.; RT "Structural and functional identification of two human, tumor-derived RT monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine RT family."; RL J. Exp. Med. 176:59-65(1992). RN [7] RP PROTEIN SEQUENCE OF 24-38, AND PYROGLUTAMATE FORMATION AT GLN-24. 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 [8] RP INTERACTION WITH TNFAIP6, AND MUTAGENESIS OF LYS-41; LYS-42 AND LYS-45. RX PubMed=27044744; DOI=10.1074/jbc.m116.720953; RA Dyer D.P., Salanga C.L., Johns S.C., Valdambrini E., Fuster M.M., RA Milner C.M., Day A.J., Handel T.M.; RT "The Anti-inflammatory Protein TSG-6 Regulates Chemokine Function by RT Inhibiting Chemokine/Glycosaminoglycan Interactions."; RL J. Biol. Chem. 291:12627-12640(2016). RN [9] RP STRUCTURE BY NMR, AND SUBUNIT. RX 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 [10] RP STRUCTURE BY NMR. RX PubMed=9109648; DOI=10.1021/bi9627929; RA Meunier S., Bernassau J.-M., Guillemot J.-C., Ferrara P., Darbon H.; RT "Determination of the three-dimensional structure of CC chemokine monocyte RT chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy."; RL Biochemistry 36:4412-4422(1997). RN [11] RP STRUCTURE BY NMR. RA Kwon D., Lee D., Sykes B.D., Kim K.-S.; RL Submitted (AUG-1998) to the PDB data bank. CC -!- FUNCTION: Chemotactic factor that attracts monocytes and eosinophils, CC but not neutrophils. Augments monocyte anti-tumor activity. Also CC induces the release of gelatinase B. This protein can bind heparin. CC Binds to CCR1, CCR2 and CCR3. CC -!- SUBUNIT: Monomer. Interacts with TNFAIP6 (via Link domain). CC {ECO:0000269|PubMed:27044744, ECO:0000269|PubMed:8898111}. CC -!- INTERACTION: CC P80098; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-718759, EBI-741480; CC P80098; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-718759, EBI-10173939; CC P80098; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-718759, EBI-947187; CC P80098; Q2F862; Xeno; NbExp=3; IntAct=EBI-718759, EBI-16161937; CC PRO_0000005183; P98066: TNFAIP6; NbExp=2; IntAct=EBI-11711410, EBI-11700693; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: O-glycosylated. CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA50405.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA50406.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAA51055.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL7 entry; CC URL="https://en.wikipedia.org/wiki/CCL7"; 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; X72308; CAA51055.1; ALT_INIT; mRNA. DR EMBL; X72309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X71087; CAA50407.1; -; mRNA. DR EMBL; X71087; CAA50406.1; ALT_INIT; mRNA. DR EMBL; X71087; CAA50405.1; ALT_INIT; mRNA. DR EMBL; BC092436; AAH92436.1; -; mRNA. DR EMBL; BC112258; AAI12259.1; -; mRNA. DR EMBL; BC112260; AAI12261.1; -; mRNA. DR EMBL; AF043338; AAC03538.1; -; mRNA. DR CCDS; CCDS11278.1; -. DR RefSeq; NP_006264.2; NM_006273.3. DR PDB; 1BO0; NMR; -; A=24-99. DR PDB; 1NCV; NMR; -; A/B=24-99. DR PDB; 4ZKC; X-ray; 3.15 A; B=24-99. DR PDB; 7S58; X-ray; 1.82 A; E/F/H/J=24-99. DR PDB; 7S59; X-ray; 2.39 A; 2/4=41-99. DR PDB; 7SCU; X-ray; 1.86 A; B=24-99. DR PDB; 8FJ3; X-ray; 2.07 A; B=24-99. DR PDB; 8FK6; X-ray; 1.74 A; B=24-99. DR PDB; 8FK8; X-ray; 1.96 A; B=24-99. DR PDBsum; 1BO0; -. DR PDBsum; 1NCV; -. DR PDBsum; 4ZKC; -. DR PDBsum; 7S58; -. DR PDBsum; 7S59; -. DR PDBsum; 7SCU; -. DR PDBsum; 8FJ3; -. DR PDBsum; 8FK6; -. DR PDBsum; 8FK8; -. DR AlphaFoldDB; P80098; -. DR BMRB; P80098; -. DR SMR; P80098; -. DR BioGRID; 112257; 12. DR DIP; DIP-5847N; -. DR IntAct; P80098; 8. DR STRING; 9606.ENSP00000367832; -. DR ChEMBL; CHEMBL3217391; -. DR GlyCosmos; P80098; 1 site, No reported glycans. DR GlyGen; P80098; 1 site. DR BioMuta; CCL7; -. DR DMDM; 1170890; -. DR MassIVE; P80098; -. DR PaxDb; 9606-ENSP00000367832; -. DR PeptideAtlas; P80098; -. DR ProteomicsDB; 57665; -. DR Antibodypedia; 15482; 754 antibodies from 35 providers. DR DNASU; 6354; -. DR Ensembl; ENST00000378569.2; ENSP00000367832.2; ENSG00000108688.11. DR GeneID; 6354; -. DR KEGG; hsa:6354; -. DR MANE-Select; ENST00000378569.2; ENSP00000367832.2; NM_006273.4; NP_006264.2. DR UCSC; uc002hhz.5; human. DR AGR; HGNC:10634; -. DR CTD; 6354; -. DR DisGeNET; 6354; -. DR GeneCards; CCL7; -. DR HGNC; HGNC:10634; CCL7. DR HPA; ENSG00000108688; Tissue enriched (bone). DR MIM; 158106; gene. DR neXtProt; NX_P80098; -. DR OpenTargets; ENSG00000108688; -. DR PharmGKB; PA35566; -. DR VEuPathDB; HostDB:ENSG00000108688; -. DR eggNOG; ENOG502S6ZP; Eukaryota. DR GeneTree; ENSGT01100000263482; -. DR HOGENOM; CLU_141716_1_0_1; -. DR InParanoid; P80098; -. DR OMA; QKWVQEF; -. DR OrthoDB; 4265193at2759; -. DR PhylomeDB; P80098; -. DR TreeFam; TF334888; -. DR PathwayCommons; P80098; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR SignaLink; P80098; -. DR SIGNOR; P80098; -. DR BioGRID-ORCS; 6354; 17 hits in 1135 CRISPR screens. DR EvolutionaryTrace; P80098; -. DR GeneWiki; CCL7; -. DR GenomeRNAi; 6354; -. DR Pharos; P80098; Tbio. DR PRO; PR:P80098; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P80098; protein. DR Bgee; ENSG00000108688; Expressed in islet of Langerhans and 100 other cell types or tissues. DR ExpressionAtlas; P80098; 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:0048020; F:CCR chemokine receptor binding; IBA:GO_Central. DR GO; GO:0031726; F:CCR1 chemokine receptor binding; IPI:UniProtKB. DR GO; GO:0031727; F:CCR2 chemokine receptor binding; IEA:Ensembl. DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. 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:0071361; P:cellular response to ethanol; IEA:Ensembl. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB. DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; TAS:ProtInc. DR GO; GO:0002548; P:monocyte chemotaxis; IC:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB. DR GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00272; Chemokine_CC; 1. DR Gene3D; 2.40.50.40; -; 1. DR InterPro; IPR039809; Chemokine_b/g/d. DR InterPro; IPR000827; Chemokine_CC_CS. DR InterPro; IPR001811; Chemokine_IL8-like_dom. DR InterPro; IPR036048; Interleukin_8-like_sf. DR PANTHER; PTHR12015:SF161; C-C MOTIF CHEMOKINE 7; 1. DR PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1. DR Pfam; PF00048; IL8; 1. DR SMART; SM00199; SCY; 1. DR SUPFAM; SSF54117; Interleukin 8-like chemokines; 1. DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1. PE 1: Evidence at protein level; KW 3D-structure; Chemotaxis; Cytokine; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Heparin-binding; Inflammatory response; KW Proteomics identification; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 24..99 FT /note="C-C motif chemokine 7" FT /id="PRO_0000005183" FT MOD_RES 24 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:15340161" FT CARBOHYD 29 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 34..59 FT DISULFID 35..75 FT MUTAGEN 41 FT /note="K->A: Decreases binding to Link domain of TNFAIP6; FT when associated with A-42 and A-45." FT /evidence="ECO:0000269|PubMed:27044744" FT MUTAGEN 42 FT /note="K->A: Decreases binding to Link domain of TNFAIP6; FT when associated with A-41 and A-45." FT /evidence="ECO:0000269|PubMed:27044744" FT MUTAGEN 45 FT /note="K->A: Decreases binding to Link domain of TNFAIP6; FT when associated with A-41 and A-42." FT /evidence="ECO:0000269|PubMed:27044744" FT CONFLICT 30 FT /note="T -> K (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68..70 FT /note="Missing (in Ref. 6; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:1NCV" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:7SCU" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:8FK6" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:8FK6" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:7S58" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:8FK6" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:8FK6" FT STRAND 73..76 FT /evidence="ECO:0007829|PDB:8FK6" FT HELIX 81..91 FT /evidence="ECO:0007829|PDB:8FK6" SQ SEQUENCE 99 AA; 11200 MW; 96048B371C25D00E CRC64; MKASAALLCL LLTAAAFSPQ GLAQPVGINT STTCCYRFIN KKIPKQRLES YRRTTSSHCP REAVIFKTKL DKEICADPTQ KWVQDFMKHL DKKTQTPKL //