CXL14_HUMAN
ID CXL14_HUMAN Reviewed; 111 AA.
AC O95715; B3KQU8; Q6UW97; Q86U69; Q9BTR1; Q9NS21;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=C-X-C motif chemokine 14;
DE AltName: Full=Chemokine BRAK;
DE AltName: Full=MIP-2G;
DE AltName: Full=Small-inducible cytokine B14;
DE Flags: Precursor;
GN Name=CXCL14; Synonyms=MIP2G, NJAC, SCYB14;
GN ORFNames=PSEC0212, UNQ240/PRO273;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Oral epithelium;
RX PubMed=10854217; DOI=10.1016/s0002-9440(10)65067-5;
RA Frederick M.J., Henderson Y., Xu X., Deavers M.T., Sahin A.A., Wu H.,
RA Lewis D.E., El-Naggar A.K., Clayman G.L.;
RT "In vivo expression of the novel CXC chemokine BRAK in normal and cancerous
RT human tissue.";
RL Am. J. Pathol. 156:1937-1950(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-44, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10946286; DOI=10.4049/jimmunol.165.5.2588;
RA Cao X., Zhang W., Wan T., He L., Chen T., Yuan Z., Ma S., Yu Y., Chen G.;
RT "Molecular cloning and characterization of a novel CXC chemokine macrophage
RT inflammatory protein-2 gamma chemoattractant for human neutrophils and
RT dendritic cells.";
RL J. Immunol. 165:2588-2595(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-111, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10049774; DOI=10.1006/bbrc.1999.0257;
RA Hromas R., Broxmeyer H.E., Kim C., Nakshatri H., Christopherson K. II,
RA Azam M., Hou Y.-H.;
RT "Cloning of BRAK, a novel divergent CXC chemokine preferentially expressed
RT in normal versus malignant cells.";
RL Biochem. Biophys. Res. Commun. 255:703-706(1999).
RN [9]
RP STRUCTURE BY NMR OF 34-111, DOMAIN D-BOX MOTIF, UBIQUITINATION, AND
RP DISULFIDE BONDS.
RX PubMed=16987528; DOI=10.1016/j.jmb.2006.08.057;
RA Peterson F.C., Thorpe J.A., Harder A.G., Volkman B.F., Schwarze S.R.;
RT "Structural determinants involved in the regulation of CXCL14/BRAK
RT expression by the 26 S proteasome.";
RL J. Mol. Biol. 363:813-822(2006).
CC -!- FUNCTION: Potent chemoattractant for neutrophils, and weaker for
CC dendritic cells. Not chemotactic for T-cells, B-cells, monocytes,
CC natural killer cells or granulocytes. Does not inhibit proliferation of
CC myeloid progenitors in colony formation assays.
CC {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10946286}.
CC -!- INTERACTION:
CC O95715; O00585: CCL21; NbExp=2; IntAct=EBI-2798068, EBI-953695;
CC O95715; Q9Y258: CCL26; NbExp=2; IntAct=EBI-2798068, EBI-7783416;
CC O95715; P13501: CCL5; NbExp=2; IntAct=EBI-2798068, EBI-2848366;
CC O95715; O14625: CXCL11; NbExp=2; IntAct=EBI-2798068, EBI-2871971;
CC O95715; P48061: CXCL12; NbExp=2; IntAct=EBI-2798068, EBI-3913254;
CC O95715; Q07325: CXCL9; NbExp=2; IntAct=EBI-2798068, EBI-3911467;
CC O95715; P02776: PF4; NbExp=3; IntAct=EBI-2798068, EBI-2565740;
CC O95715; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-2798068, EBI-742397;
CC O95715; P36406: TRIM23; NbExp=3; IntAct=EBI-2798068, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. Highly expressed in normal tissue
CC without inflammatory stimuli and infrequently expressed in cancer cell
CC lines. Weakly expressed in monocyte-derived dendritic cells. Not
CC detected in lung or unstimulated peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10854217,
CC ECO:0000269|PubMed:10946286}.
CC -!- INDUCTION: Up-regulated in peripheral blood lymphocytes in response to
CC bacterial lipopolysaccharides (LPS). {ECO:0000269|PubMed:10854217}.
CC -!- DOMAIN: The destruction box (D-box) acts as a recognition signal for
CC degradation via the ubiquitin-proteasome pathway.
CC {ECO:0000269|PubMed:16987528}.
CC -!- PTM: Ubiquitinated, followed by degradation by the proteasome.
CC {ECO:0000269|PubMed:16987528}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-13 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38944.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL14 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL14";
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DR EMBL; AF144103; AAD38944.1; ALT_INIT; mRNA.
DR EMBL; AF106911; AAF78449.1; -; mRNA.
DR EMBL; AY358906; AAQ89265.1; -; mRNA.
DR EMBL; AK075514; BAG52160.1; -; mRNA.
DR EMBL; BT007080; AAP35743.1; -; mRNA.
DR EMBL; AC034206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003513; AAH03513.1; -; mRNA.
DR EMBL; AF073957; AAD03839.1; -; mRNA.
DR PIR; JG0182; JG0182.
DR RefSeq; NP_004878.2; NM_004887.4.
DR PDB; 2HDL; NMR; -; A=35-111.
DR PDBsum; 2HDL; -.
DR AlphaFoldDB; O95715; -.
DR SMR; O95715; -.
DR BioGRID; 114921; 43.
DR DIP; DIP-61148N; -.
DR IntAct; O95715; 27.
DR MINT; O95715; -.
DR STRING; 9606.ENSP00000337065; -.
DR iPTMnet; O95715; -.
DR PhosphoSitePlus; O95715; -.
DR BioMuta; CXCL14; -.
DR jPOST; O95715; -.
DR MassIVE; O95715; -.
DR PaxDb; O95715; -.
DR PeptideAtlas; O95715; -.
DR PRIDE; O95715; -.
DR ProteomicsDB; 51009; -.
DR Antibodypedia; 14757; 328 antibodies from 33 providers.
DR DNASU; 9547; -.
DR Ensembl; ENST00000337225.5; ENSP00000337065.5; ENSG00000145824.13.
DR GeneID; 9547; -.
DR KEGG; hsa:9547; -.
DR UCSC; uc003lay.4; human.
DR CTD; 9547; -.
DR DisGeNET; 9547; -.
DR GeneCards; CXCL14; -.
DR HGNC; HGNC:10640; CXCL14.
DR HPA; ENSG00000145824; Tissue enhanced (skin).
DR MIM; 604186; gene.
DR neXtProt; NX_O95715; -.
DR OpenTargets; ENSG00000145824; -.
DR PharmGKB; PA35571; -.
DR VEuPathDB; HostDB:ENSG00000145824; -.
DR eggNOG; ENOG502S4VP; Eukaryota.
DR GeneTree; ENSGT00390000000618; -.
DR InParanoid; O95715; -.
DR OMA; QYCLHPK; -.
DR OrthoDB; 1504765at2759; -.
DR PhylomeDB; O95715; -.
DR TreeFam; TF332769; -.
DR PathwayCommons; O95715; -.
DR SignaLink; O95715; -.
DR BioGRID-ORCS; 9547; 118 hits in 1024 CRISPR screens.
DR ChiTaRS; CXCL14; human.
DR EvolutionaryTrace; O95715; -.
DR GenomeRNAi; 9547; -.
DR Pharos; O95715; Tbio.
DR PRO; PR:O95715; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O95715; protein.
DR Bgee; ENSG00000145824; Expressed in skin of hip and 190 other tissues.
DR ExpressionAtlas; O95715; baseline and differential.
DR Genevisible; O95715; HS.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0008009; F:chemokine activity; TAS:ProtInc.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR039088; CXCL14.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR15188; PTHR15188; 1.
DR Pfam; PF00048; IL8; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal; Ubl conjugation.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:10946286"
FT CHAIN 35..111
FT /note="C-X-C motif chemokine 14"
FT /id="PRO_0000005115"
FT MOTIF 67..81
FT /note="D-box"
FT DISULFID 37..63
FT /evidence="ECO:0000269|PubMed:16987528"
FT DISULFID 39..84
FT /evidence="ECO:0000269|PubMed:16987528"
FT CONFLICT 108
FT /note="V -> F (in Ref. 2; AAF78449)"
FT /evidence="ECO:0000305"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:2HDL"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2HDL"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2HDL"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2HDL"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2HDL"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2HDL"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:2HDL"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2HDL"
FT HELIX 90..106
FT /evidence="ECO:0007829|PDB:2HDL"
SQ SEQUENCE 111 AA; 13078 MW; C9A18B2A78CACF74 CRC64;
MSLLPRRAPP VSMRLLAAAL LLLLLALYTA RVDGSKCKCS RKGPKIRYSD VKKLEMKPKY
PHCEEKMVII TTKSVSRYRG QEHCLHPKLQ STKRFIKWYN AWNEKRRVYE E
