CCL28_HUMAN
ID CCL28_HUMAN Reviewed; 127 AA.
AC Q9NRJ3; D7RIE7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=C-C motif chemokine 28;
DE AltName: Full=Mucosae-associated epithelial chemokine;
DE Short=MEC;
DE AltName: Full=Protein CCK1;
DE AltName: Full=Small-inducible cytokine A28;
DE Flags: Precursor;
GN Name=CCL28; Synonyms=SCYA28;
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] (ISOFORM 1), AND RECEPTOR INTERACTION.
RC TISSUE=Fetal heart, and Osteoblast;
RX PubMed=10781587; DOI=10.1074/jbc.m001461200;
RA Wang W., Soto H., Oldham E.R., Buchanan M.E., Homey B., Catron D.,
RA Jenkins N., Copeland N.G., Gilbert D.J., Nguyen N., Abrams J.,
RA Kershenovich D., Smith K., McClanahan T., Vicari A.P., Zlotnik A.;
RT "Identification of a novel chemokine (CCL28), which binds CCR10 (GPR2).";
RL J. Biol. Chem. 275:22313-22323(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND RECEPTOR INTERACTION.
RX PubMed=10975800; DOI=10.4049/jimmunol.165.6.2943;
RA Pan J., Kunkel E.J., Gosslar U., Lazarus N., Langdon P., Broadwell K.,
RA Vierra M.A., Genovese M.C., Butcher E.C., Soler D.;
RT "A novel chemokine ligand for CCR10 and CCR3 expressed by epithelial cells
RT in mucosal tissues.";
RL J. Immunol. 165:2943-2949(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang W., He L., Yuan Z., Wan T., Cao X.;
RT "A novel CC chemokine homology with TECK.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Scanlon K.M., Mahon B.P.;
RT "Prediction and identification of a novel CCL28 splice variant CCL28chi.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Chemotactic activity for resting CD4, CD8 T-cells and
CC eosinophils. Binds to CCR3 and CCR10 and induces calcium mobilization
CC in a dose-dependent manner.
CC -!- INTERACTION:
CC Q9NRJ3; P51671: CCL11; NbExp=2; IntAct=EBI-7783254, EBI-727357;
CC Q9NRJ3; Q92583: CCL17; NbExp=3; IntAct=EBI-7783254, EBI-16640146;
CC Q9NRJ3; O00585: CCL21; NbExp=2; IntAct=EBI-7783254, EBI-953695;
CC Q9NRJ3; Q9Y258: CCL26; NbExp=2; IntAct=EBI-7783254, EBI-7783416;
CC Q9NRJ3; P13501: CCL5; NbExp=2; IntAct=EBI-7783254, EBI-2848366;
CC Q9NRJ3; P02778: CXCL10; NbExp=2; IntAct=EBI-7783254, EBI-7815386;
CC Q9NRJ3; P48061: CXCL12; NbExp=2; IntAct=EBI-7783254, EBI-3913254;
CC Q9NRJ3; Q8WTU0: DDI1; NbExp=10; IntAct=EBI-7783254, EBI-748248;
CC Q9NRJ3; P51808: DYNLT3; NbExp=3; IntAct=EBI-7783254, EBI-743027;
CC Q9NRJ3; P02776: PF4; NbExp=3; IntAct=EBI-7783254, EBI-2565740;
CC Q9NRJ3; P25788: PSMA3; NbExp=3; IntAct=EBI-7783254, EBI-348380;
CC Q9NRJ3; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-7783254, EBI-357085;
CC Q9NRJ3; Q86WV8: TSC1; NbExp=3; IntAct=EBI-7783254, EBI-12806590;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRJ3-1; Sequence=Displayed;
CC Name=2; Synonyms=CCL28chi;
CC IsoId=Q9NRJ3-2; Sequence=VSP_047735;
CC -!- TISSUE SPECIFICITY: Preferentially expressed by epithelial cells of
CC diverse tissues including normal and pathological colon, salivary
CC gland, mammary gland, trachea and rectum. Also found in prostate,
CC spleen, thyroid, psoriasis skin and in lower levels in peripheral blood
CC leukocytes, small intestine, Peyer patches, stomach and normal skin.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL28 entry;
CC URL="https://en.wikipedia.org/wiki/CCL28";
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DR EMBL; AF220210; AAF87205.1; -; mRNA.
DR EMBL; AF266504; AAG16691.1; -; mRNA.
DR EMBL; AF110384; AAG43193.1; -; mRNA.
DR EMBL; HM067700; ADH95184.1; -; mRNA.
DR EMBL; AC025457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062668; AAH62668.1; -; mRNA.
DR EMBL; BC069532; AAH69532.1; -; mRNA.
DR CCDS; CCDS3944.1; -. [Q9NRJ3-1]
DR RefSeq; NP_001288802.1; NM_001301873.1. [Q9NRJ3-1]
DR RefSeq; NP_001288803.1; NM_001301874.1. [Q9NRJ3-1]
DR RefSeq; NP_683513.1; NM_148672.3. [Q9NRJ3-1]
DR PDB; 6CWS; NMR; -; A=20-127.
DR PDBsum; 6CWS; -.
DR AlphaFoldDB; Q9NRJ3; -.
DR BMRB; Q9NRJ3; -.
DR SMR; Q9NRJ3; -.
DR BioGRID; 121147; 23.
DR DIP; DIP-57392N; -.
DR IntAct; Q9NRJ3; 26.
DR MINT; Q9NRJ3; -.
DR STRING; 9606.ENSP00000354416; -.
DR GlyGen; Q9NRJ3; 1 site.
DR iPTMnet; Q9NRJ3; -.
DR PhosphoSitePlus; Q9NRJ3; -.
DR BioMuta; CCL28; -.
DR DMDM; 12230650; -.
DR jPOST; Q9NRJ3; -.
DR MassIVE; Q9NRJ3; -.
DR PaxDb; Q9NRJ3; -.
DR PeptideAtlas; Q9NRJ3; -.
DR PRIDE; Q9NRJ3; -.
DR ProteomicsDB; 82377; -. [Q9NRJ3-1]
DR Antibodypedia; 23245; 345 antibodies from 31 providers.
DR DNASU; 56477; -.
DR Ensembl; ENST00000361115.4; ENSP00000354416.4; ENSG00000151882.11. [Q9NRJ3-1]
DR Ensembl; ENST00000489442.5; ENSP00000426424.1; ENSG00000151882.11. [Q9NRJ3-1]
DR GeneID; 56477; -.
DR KEGG; hsa:56477; -.
DR MANE-Select; ENST00000361115.4; ENSP00000354416.4; NM_148672.3; NP_683513.1.
DR UCSC; uc003jnu.4; human. [Q9NRJ3-1]
DR CTD; 56477; -.
DR DisGeNET; 56477; -.
DR GeneCards; CCL28; -.
DR HGNC; HGNC:17700; CCL28.
DR HPA; ENSG00000151882; Tissue enriched (salivary).
DR MIM; 605240; gene.
DR neXtProt; NX_Q9NRJ3; -.
DR OpenTargets; ENSG00000151882; -.
DR PharmGKB; PA38463; -.
DR VEuPathDB; HostDB:ENSG00000151882; -.
DR eggNOG; ENOG502SVUE; Eukaryota.
DR GeneTree; ENSGT00530000063923; -.
DR HOGENOM; CLU_2003113_0_0_1; -.
DR InParanoid; Q9NRJ3; -.
DR OMA; HVIKQWM; -.
DR PhylomeDB; Q9NRJ3; -.
DR TreeFam; TF337014; -.
DR PathwayCommons; Q9NRJ3; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q9NRJ3; -.
DR BioGRID-ORCS; 56477; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; CCL28; human.
DR GenomeRNAi; 56477; -.
DR Pharos; Q9NRJ3; Tbio.
DR PRO; PR:Q9NRJ3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NRJ3; protein.
DR Bgee; ENSG00000151882; Expressed in parotid gland and 137 other tissues.
DR ExpressionAtlas; Q9NRJ3; baseline and differential.
DR Genevisible; Q9NRJ3; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; TAS:UniProtKB.
DR GO; GO:0051715; P:cytolysis in another organism; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0031640; P:killing of cells of another organism; IMP:UniProtKB.
DR GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IDA:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR DisProt; DP02010; -.
DR InterPro; IPR000827; Chemokine_CC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR Pfam; PF00048; IL8; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chemotaxis; Cytokine; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..127
FT /note="C-C motif chemokine 28"
FT /id="PRO_0000005242"
FT REGION 92..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..112
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..58
FT /evidence="ECO:0000250"
FT DISULFID 31..73
FT /evidence="ECO:0000250"
FT VAR_SEQ 64..127
FT /note="ILHVKRRRICVSPHNHTVKQWMKVQAAKKNGKGNVCHRKKHHGKRNSNRAHQ
FT GKHETYGHKTPY -> MLECSDMISAHYNLHLPGSNDSPTSAFQVAGITAFMSSAEESV
FT SARTTILLSSG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047735"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:6CWS"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6CWS"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6CWS"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:6CWS"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6CWS"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:6CWS"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6CWS"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:6CWS"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6CWS"
SQ SEQUENCE 127 AA; 14280 MW; 3E8551A63A2C8D62 CRC64;
MQQRGLAIVA LAVCAALHAS EAILPIASSC CTEVSHHISR RLLERVNMCR IQRADGDCDL
AAVILHVKRR RICVSPHNHT VKQWMKVQAA KKNGKGNVCH RKKHHGKRNS NRAHQGKHET
YGHKTPY
