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   13-FEB-2019, entry version 156.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   cancerous human tissue.";
RL   Am. J. Pathol. 156:1937-1950(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-44, FUNCTION, AND
RP   TISSUE 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.,
RA   Chen G.;
RT   "Molecular cloning and characterization of a novel CXC chemokine
RT   macrophage inflammatory protein-2 gamma chemoattractant for human
RT   neutrophils and 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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-
RT   length human cDNAs encoding secretion or membrane proteins from oligo-
RT   capped cDNA 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
RT   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.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-111, FUNCTION, AND TISSUE
RP   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
RT   expressed 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
CC       proliferation of myeloid progenitors in colony formation assays.
CC       {ECO:0000269|PubMed:10049774, ECO:0000269|PubMed:10946286}.
CC   -!- INTERACTION:
CC       O00585:CCL21; NbExp=2; IntAct=EBI-2798068, EBI-953695;
CC       Q9Y258:CCL26; NbExp=2; IntAct=EBI-2798068, EBI-7783416;
CC       P13501:CCL5; NbExp=2; IntAct=EBI-2798068, EBI-2848366;
CC       O14625:CXCL11; NbExp=2; IntAct=EBI-2798068, EBI-2871971;
CC       P48061:CXCL12; NbExp=2; IntAct=EBI-2798068, EBI-3913254;
CC       Q07325:CXCL9; NbExp=2; IntAct=EBI-2798068, EBI-3911467;
CC       P02776:PF4; NbExp=3; IntAct=EBI-2798068, EBI-2565740;
CC       Q8IYF3:TEX11; NbExp=3; IntAct=EBI-2798068, EBI-742397;
CC       P36406:TRIM23; NbExp=3; IntAct=EBI-2798068, EBI-740098;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
CC       liver, skeletal muscle, kidney and pancreas. Highly expressed in
CC       normal tissue without inflammatory stimuli and infrequently
CC       expressed in cancer cell lines. Weakly expressed in monocyte-
CC       derived dendritic cells. Not detected in lung or unstimulated
CC       peripheral blood lymphocytes. {ECO:0000269|PubMed:10049774,
CC       ECO:0000269|PubMed:10854217, ECO:0000269|PubMed:10946286}.
CC   -!- INDUCTION: Up-regulated in peripheral blood lymphocytes in
CC       response to bacterial lipopolysaccharides (LPS).
CC       {ECO:0000269|PubMed:10854217}.
CC   -!- DOMAIN: The destruction box (D-box) acts as a recognition signal
CC       for 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)
CC       family. {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   CCDS; CCDS4188.1; -.
DR   PIR; JG0182; JG0182.
DR   RefSeq; NP_004878.2; NM_004887.4.
DR   UniGene; Hs.483444; -.
DR   PDB; 2HDL; NMR; -; A=35-111.
DR   PDBsum; 2HDL; -.
DR   ProteinModelPortal; O95715; -.
DR   SMR; O95715; -.
DR   BioGrid; 114921; 6.
DR   DIP; DIP-61148N; -.
DR   IntAct; O95715; 26.
DR   MINT; O95715; -.
DR   STRING; 9606.ENSP00000337065; -.
DR   iPTMnet; O95715; -.
DR   PhosphoSitePlus; O95715; -.
DR   BioMuta; CXCL14; -.
DR   jPOST; O95715; -.
DR   PaxDb; O95715; -.
DR   PeptideAtlas; O95715; -.
DR   PRIDE; O95715; -.
DR   ProteomicsDB; 51009; -.
DR   DNASU; 9547; -.
DR   Ensembl; ENST00000337225; ENSP00000337065; ENSG00000145824.
DR   GeneID; 9547; -.
DR   KEGG; hsa:9547; -.
DR   UCSC; uc003lay.4; human.
DR   CTD; 9547; -.
DR   DisGeNET; 9547; -.
DR   EuPathDB; HostDB:ENSG00000145824.12; -.
DR   GeneCards; CXCL14; -.
DR   HGNC; HGNC:10640; CXCL14.
DR   HPA; CAB029996; -.
DR   MIM; 604186; gene.
DR   neXtProt; NX_O95715; -.
DR   OpenTargets; ENSG00000145824; -.
DR   PharmGKB; PA35571; -.
DR   eggNOG; ENOG410J0K5; Eukaryota.
DR   eggNOG; ENOG4111XWS; LUCA.
DR   GeneTree; ENSGT00390000000618; -.
DR   HOGENOM; HOG000065700; -.
DR   HOVERGEN; HBG054250; -.
DR   InParanoid; O95715; -.
DR   KO; K10033; -.
DR   OMA; EGSKCKC; -.
DR   OrthoDB; 1504765at2759; -.
DR   PhylomeDB; O95715; -.
DR   TreeFam; TF332769; -.
DR   ChiTaRS; CXCL14; human.
DR   EvolutionaryTrace; O95715; -.
DR   GenomeRNAi; 9547; -.
DR   PRO; PR:O95715; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000145824; Expressed in 221 organ(s), highest expression level in zone of skin.
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:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR   GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IEA:Ensembl.
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; Complete proteome; Cytokine;
KW   Direct protein sequencing; Disulfide bond; Reference proteome;
KW   Secreted; Signal; Ubl conjugation.
FT   SIGNAL        1     34       {ECO:0000269|PubMed:10946286}.
FT   CHAIN        35    111       C-X-C motif chemokine 14.
FT                                /FTId=PRO_0000005115.
FT   MOTIF        67     81       D-box.
FT   DISULFID     37     63       {ECO:0000269|PubMed:16987528}.
FT   DISULFID     39     84       {ECO:0000269|PubMed:16987528}.
FT   CONFLICT    108    108       V -> F (in Ref. 2; AAF78449).
FT                                {ECO:0000305}.
FT   STRAND       41     44       {ECO:0000244|PDB:2HDL}.
FT   HELIX        48     50       {ECO:0000244|PDB:2HDL}.
FT   STRAND       51     56       {ECO:0000244|PDB:2HDL}.
FT   STRAND       63     65       {ECO:0000244|PDB:2HDL}.
FT   STRAND       68     72       {ECO:0000244|PDB:2HDL}.
FT   STRAND       74     76       {ECO:0000244|PDB:2HDL}.
FT   TURN         77     80       {ECO:0000244|PDB:2HDL}.
FT   STRAND       81     85       {ECO:0000244|PDB:2HDL}.
FT   HELIX        90    106       {ECO:0000244|PDB:2HDL}.
SQ   SEQUENCE   111 AA;  13078 MW;  C9A18B2A78CACF74 CRC64;
     MSLLPRRAPP VSMRLLAAAL LLLLLALYTA RVDGSKCKCS RKGPKIRYSD VKKLEMKPKY
     PHCEEKMVII TTKSVSRYRG QEHCLHPKLQ STKRFIKWYN AWNEKRRVYE E
//