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C-C motif chemokine 15 (Chemokine CC-2) (HCC-2) (Leukotactin-1) (LKN-1) (MIP-1 delta) (Macrophage inflammatory protein 5) (MIP-5) (Mrp-2b) (NCC-3) (Small-inducible cytokine A15) [Cleaved into: CCL15(22-92); CCL15(25-92); CCL15(29-92)]

 CCL15_HUMAN             Reviewed;         113 AA.
Q16663; B2RU34; E1P651; Q9UM74;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
27-SEP-2017, entry version 159.
RecName: Full=C-C motif chemokine 15;
AltName: Full=Chemokine CC-2;
Short=HCC-2;
AltName: Full=Leukotactin-1;
Short=LKN-1;
AltName: Full=MIP-1 delta;
AltName: Full=Macrophage inflammatory protein 5;
Short=MIP-5;
AltName: Full=Mrp-2b;
AltName: Full=NCC-3;
AltName: Full=Small-inducible cytokine A15;
Contains:
RecName: Full=CCL15(22-92);
Contains:
RecName: Full=CCL15(25-92);
Contains:
RecName: Full=CCL15(29-92);
Flags: Precursor;
Name=CCL15; Synonyms=MIP5, NCC3, SCYA15;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-24.
PubMed=9548457;
Youn B.-S., Zhang S.M., Lee E.K., Park D.H., Broxmeyer H.E.,
Murphy P.M., Locati M., Pease J.E., Kim K.K., Antol K., Kwon B.S.;
"Molecular cloning of leukotactin-1: a novel human beta-chemokine, a
chemoattractant for neutrophils, monocytes, and lymphocytes, and a
potent agonist at CC chemokine receptors 1 and 3.";
J. Immunol. 159:5201-5205(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=9624581; DOI=10.1023/A:1020535106684;
Wang W., Bacon K.B., Oldham E.R., Schall T.J.;
"Molecular cloning and functional characterization of human MIP-1
delta, a new C-C chemokine related to mouse CCF-18 and C10.";
J. Clin. Immunol. 18:214-222(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-24, AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=9600961; DOI=10.1073/pnas.95.11.6308;
Pardigol A., Forssmann U., Zucht H.-D., Loetscher P.,
Schulz-Knappe P., Baggiolini M., Forssmann W.-G., Maegert H.-J.;
"HCC-2, a human chemokine: gene structure, expression pattern, and
biological activity.";
Proc. Natl. Acad. Sci. U.S.A. 95:6308-6313(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-24.
PubMed=10213461; DOI=10.1089/107999099314153;
Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.;
"Organization of the chemokine gene cluster on human chromosome
17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and
RANTES.";
J. Interferon Cytokine Res. 19:227-234(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-24.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-24.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-113.
Coulin F., Power C.A., Alouani S., Peitsch M.C., Schroeder J.-M.,
Moshizuki M., Clark-Lewis I., Wells T.N.C.;
Submitted (JAN-1997) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 22-36.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[9]
DISCUSSION OF SEQUENCE.
PubMed=9129202;
Wells T.N.C., Peitsch M.C.;
"The chemokine information source: identification and characterization
of novel chemokines using the WorldWideWeb and expressed sequence tag
databases.";
J. Leukoc. Biol. 61:545-550(1997).
[10]
TISSUE SPECIFICITY.
PubMed=9558365;
Youn B.-S., Zhang S.M., Broxmeyer H.E., Cooper S., Antol K.,
Fraser M. Jr., Kwon B.S.;
"Characterization of CKbeta8 and CKbeta8-1: two alternatively spliced
forms of human beta-chemokine, chemoattractants for neutrophils,
monocytes, and lymphocytes, and potent agonists at CC chemokine
receptor 1.";
Blood 91:3118-3126(1998).
[11]
IDENTIFICATION OF CCL15(22-92); CCL15(25-92) AND CCL15(29-92),
PROTEOLYTIC PROCESSING OF N-TERMINUS, TISSUE SPECIFICITY, AND
FUNCTION.
PubMed=15905581; DOI=10.4049/jimmunol.174.11.7341;
Berahovich R.D., Miao Z., Wang Y., Premack B., Howard M.C.,
Schall T.J.;
"Proteolytic activation of alternative CCR1 ligands in inflammation.";
J. Immunol. 174:7341-7351(2005).
[12]
STRUCTURE BY NMR OF 48-113, SUBUNIT, AND DISULFIDE BONDS.
PubMed=10320325; DOI=10.1021/bi990065i;
Sticht H., Escher S.E., Schweimer K., Forssmann W.G., Rosch P.,
Adermann K.;
"Solution structure of the human CC chemokine 2: A monomeric
representative of the CC chemokine subtype.";
Biochemistry 38:5995-6002(1999).
-!- FUNCTION: Chemotactic factor that attracts T-cells and monocytes,
but not neutrophils, eosinophils, or B-cells. Acts mainly via CC
chemokine receptor CCR1. Also binds to CCR3. CCL15(22-92),
CCL15(25-92) and CCL15(29-92) are more potent chemoattractants
than the small-inducible cytokine A15.
{ECO:0000269|PubMed:15905581}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10320325}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Most abundant in heart, skeletal muscle and
adrenal gland. Lower levels in placenta, liver, pancreas and bone
marrow. CCL15(22-92), CCL15(25-92) and CCL15(29-92) are found in
high levels in synovial fluids from rheumatoid patients.
{ECO:0000269|PubMed:15905581, ECO:0000269|PubMed:9558365}.
-!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CCL15 entry;
URL="https://en.wikipedia.org/wiki/CCL15";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U58914; AAD10847.1; -; mRNA.
EMBL; AF031587; AAB94617.1; -; mRNA.
EMBL; Z70293; CAA94308.1; -; mRNA.
EMBL; Z70292; CAA94306.1; -; mRNA.
EMBL; AF088219; AAC63328.1; -; Genomic_DNA.
EMBL; CH471147; EAW80110.1; -; Genomic_DNA.
EMBL; CH471147; EAW80111.1; -; Genomic_DNA.
EMBL; CH471147; EAW80112.1; -; Genomic_DNA.
EMBL; CH471147; EAW80113.1; -; Genomic_DNA.
EMBL; BC140941; AAI40942.1; -; mRNA.
CCDS; CCDS11304.1; -.
RefSeq; NP_116741.2; NM_032965.5.
UniGene; Hs.272493; -.
PDB; 2HCC; NMR; -; A=48-113.
PDBsum; 2HCC; -.
ProteinModelPortal; Q16663; -.
SMR; Q16663; -.
BioGrid; 112262; 4.
DIP; DIP-6218N; -.
MINT; MINT-1528582; -.
STRING; 9606.ENSP00000432034; -.
BioMuta; CCL15; -.
DMDM; 3915594; -.
PaxDb; Q16663; -.
PeptideAtlas; Q16663; -.
PRIDE; Q16663; -.
DNASU; 6359; -.
Ensembl; ENST00000614050; ENSP00000477788; ENSG00000275528.
Ensembl; ENST00000617897; ENSP00000484078; ENSG00000275718.
GeneID; 6359; -.
KEGG; hsa:6359; -.
UCSC; uc032gbw.1; human.
CTD; 6359; -.
DisGeNET; 6359; -.
EuPathDB; HostDB:ENSG00000275718.1; -.
GeneCards; CCL15; -.
HGNC; HGNC:10613; CCL15.
HPA; HPA058608; -.
MIM; 601393; gene.
neXtProt; NX_Q16663; -.
PharmGKB; PA35546; -.
eggNOG; ENOG410J4DG; Eukaryota.
eggNOG; ENOG4111C2C; LUCA.
HOGENOM; HOG000036685; -.
HOVERGEN; HBG017871; -.
InParanoid; Q16663; -.
KO; K05511; -.
OrthoDB; EOG091G14Y2; -.
PhylomeDB; Q16663; -.
TreeFam; TF334888; -.
EvolutionaryTrace; Q16663; -.
GenomeRNAi; 6359; -.
PRO; PR:Q16663; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000275718; -.
ExpressionAtlas; Q16663; baseline and differential.
Genevisible; Q16663; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005102; F:receptor binding; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:ProtInc.
GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
InterPro; IPR030592; CCL15.
InterPro; IPR000827; Chemokine_CC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
PANTHER; PTHR12015:SF123; PTHR12015:SF123; 1.
Pfam; PF00048; IL8; 1.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
1: Evidence at protein level;
3D-structure; Chemotaxis; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Heparin-binding;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:15340161}.
CHAIN 22 113 C-C motif chemokine 15.
/FTId=PRO_0000005208.
CHAIN 43 113 CCL15(22-92).
/FTId=PRO_0000041868.
CHAIN 46 113 CCL15(25-92).
/FTId=PRO_0000041869.
CHAIN 50 113 CCL15(29-92).
/FTId=PRO_0000041870.
DISULFID 53 77 {ECO:0000269|PubMed:10320325}.
DISULFID 54 93 {ECO:0000269|PubMed:10320325}.
DISULFID 64 104 {ECO:0000269|PubMed:10320325}.
VARIANT 24 24 I -> T (in dbSNP:rs854625).
{ECO:0000269|PubMed:10213461,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9548457,
ECO:0000269|PubMed:9600961,
ECO:0000269|Ref.5}.
/FTId=VAR_011640.
CONFLICT 14 14 V -> I (in Ref. 1; AAD10847).
{ECO:0000305}.
STRAND 59 61 {ECO:0000244|PDB:2HCC}.
HELIX 64 66 {ECO:0000244|PDB:2HCC}.
STRAND 67 72 {ECO:0000244|PDB:2HCC}.
STRAND 77 79 {ECO:0000244|PDB:2HCC}.
STRAND 82 86 {ECO:0000244|PDB:2HCC}.
TURN 87 89 {ECO:0000244|PDB:2HCC}.
STRAND 90 94 {ECO:0000244|PDB:2HCC}.
HELIX 101 107 {ECO:0000244|PDB:2HCC}.
SEQUENCE 113 AA; 12248 MW; 0BA0FCE7B8A30A04 CRC64;
MKVSVAALSC LMLVAVLGSQ AQFINDAETE LMMSKLPLEN PVVLNSFHFA ADCCTSYISQ
SIPCSLMKSY FETSSECSKP GVIFLTKKGR QVCAKPSGPG VQDCMKKLKP YSI


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