CCL1_HUMAN
ID CCL1_HUMAN Reviewed; 96 AA.
AC P22362; B2R5G9; Q2M309;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=C-C motif chemokine 1;
DE AltName: Full=Small-inducible cytokine A1;
DE AltName: Full=T lymphocyte-secreted protein I-309;
DE Flags: Precursor;
GN Name=CCL1; Synonyms=SCYA1;
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].
RX PubMed=2809212;
RA Miller M.D., Hata S., Waal Malefyt R., Krangel M.S.;
RT "A novel polypeptide secreted by activated human T lymphocytes.";
RL J. Immunol. 143:2907-2916(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2212659;
RA Miller M.D., Wilson S.D., Dorf M.E., Seuanez H.N., O'Brien S.J.,
RA Krangel M.S.;
RT "Sequence and chromosomal location of the I-309 gene. Relationship to genes
RT encoding a family of inflammatory cytokines.";
RL J. Immunol. 145:2737-2744(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 24-38.
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 FUNCTION, AND SIGNAL SEQUENCE CLEAVAGE SITE.
RX PubMed=1557400; DOI=10.1073/pnas.89.7.2950;
RA Miller M.D., Krangel M.S.;
RT "The human cytokine I-309 is a monocyte chemoattractant.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2950-2954(1992).
RN [8]
RP STRUCTURE BY NMR OF 23-96.
RX PubMed=10821677; DOI=10.1021/bi000089l;
RA Keizer D.W., Crump M.P., Lee T.W., Slupsky C.M., Clark-Lewis I.,
RA Sykes B.D.;
RT "Human CC chemokine I-309, structural consequences of the additional
RT disulfide bond.";
RL Biochemistry 39:6053-6059(2000).
CC -!- FUNCTION: Cytokine that is chemotactic for monocytes but not for
CC neutrophils. Binds to CCR8. {ECO:0000269|PubMed:1557400}.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: By phorbol myristate acetate (PMA).
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL1 entry;
CC URL="https://en.wikipedia.org/wiki/CCL1";
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; M57502; AAA61196.1; -; mRNA.
DR EMBL; M57506; AAA52705.1; -; Genomic_DNA.
DR EMBL; AK312183; BAG35116.1; -; mRNA.
DR EMBL; CH471147; EAW80204.1; -; Genomic_DNA.
DR EMBL; BC105073; AAI05074.1; -; mRNA.
DR EMBL; BC105075; AAI05076.1; -; mRNA.
DR CCDS; CCDS11282.1; -.
DR PIR; A37236; A37236.
DR RefSeq; NP_002972.1; NM_002981.2.
DR PDB; 1EL0; NMR; -; A=23-96.
DR PDB; 4OIJ; X-ray; 2.00 A; A/B=23-96.
DR PDB; 4OIK; X-ray; 2.10 A; A/B=23-96.
DR PDBsum; 1EL0; -.
DR PDBsum; 4OIJ; -.
DR PDBsum; 4OIK; -.
DR AlphaFoldDB; P22362; -.
DR BMRB; P22362; -.
DR SMR; P22362; -.
DR BioGRID; 112250; 5.
DR DIP; DIP-5835N; -.
DR IntAct; P22362; 1.
DR STRING; 9606.ENSP00000225842; -.
DR GlyGen; P22362; 1 site.
DR BioMuta; CCL1; -.
DR DMDM; 123950; -.
DR MassIVE; P22362; -.
DR PaxDb; P22362; -.
DR PeptideAtlas; P22362; -.
DR PRIDE; P22362; -.
DR Antibodypedia; 15502; 320 antibodies from 31 providers.
DR DNASU; 6346; -.
DR Ensembl; ENST00000225842.4; ENSP00000225842.3; ENSG00000108702.4.
DR GeneID; 6346; -.
DR KEGG; hsa:6346; -.
DR MANE-Select; ENST00000225842.4; ENSP00000225842.3; NM_002981.2; NP_002972.1.
DR UCSC; uc002hid.3; human.
DR CTD; 6346; -.
DR DisGeNET; 6346; -.
DR GeneCards; CCL1; -.
DR HGNC; HGNC:10609; CCL1.
DR HPA; ENSG00000108702; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 182281; gene.
DR neXtProt; NX_P22362; -.
DR OpenTargets; ENSG00000108702; -.
DR PharmGKB; PA35542; -.
DR VEuPathDB; HostDB:ENSG00000108702; -.
DR eggNOG; ENOG502SZRS; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_5_0_1; -.
DR InParanoid; P22362; -.
DR OMA; MHVSSSN; -.
DR OrthoDB; 1600839at2759; -.
DR PhylomeDB; P22362; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P22362; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P22362; -.
DR SIGNOR; P22362; -.
DR BioGRID-ORCS; 6346; 13 hits in 1059 CRISPR screens.
DR EvolutionaryTrace; P22362; -.
DR GenomeRNAi; 6346; -.
DR Pharos; P22362; Tbio.
DR PRO; PR:P22362; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P22362; protein.
DR Bgee; ENSG00000108702; Expressed in primary visual cortex and 47 other tissues.
DR Genevisible; P22362; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0008009; F:chemokine activity; IDA:CAFA.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:ProtInc.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; 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:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor 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:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:CAFA.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:CAFA.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0016032; P:viral process; TAS:ProtInc.
DR DisProt; DP00644; -.
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; PTHR12015; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:1557400"
FT CHAIN 24..96
FT /note="C-C motif chemokine 1"
FT /id="PRO_0000005141"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..57
FT DISULFID 34..73
FT DISULFID 49..91
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1EL0"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4OIJ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4OIJ"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:4OIJ"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4OIJ"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:4OIJ"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4OIJ"
FT HELIX 79..86
FT /evidence="ECO:0007829|PDB:4OIJ"
SQ SEQUENCE 96 AA; 10992 MW; 7E67F1F82892F3C7 CRC64;
MQIITTALVC LLLAGMWPED VDSKSMQVPF SRCCFSFAEQ EIPLRAILCY RNTSSICSNE
GLIFKLKRGK EACALDTVGW VQRHRKMLRH CPSKRK