ID   CXL16_PIG               Reviewed;         250 AA.
AC   Q9GKE2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=C-X-C motif chemokine 16;
DE   AltName: Full=Transmembrane chemokine CXCL16;
DE   Flags: Precursor;
GN   Name=CXCL16;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11060282; DOI=10.1074/jbc.c000761200;
RA   Shimaoka T., Kume N., Minami M., Hayashida K., Kataoka H., Kita T.,
RA   Yonehara S.;
RT   "Molecular cloning of a novel scavenger receptor for oxidized low density
RT   lipoprotein, SR-PSOX, on macrophages.";
RL   J. Biol. Chem. 275:40663-40666(2000).
CC   -!- FUNCTION: Induces a strong chemotactic response. Induces calcium
CC       mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor
CC       on macrophages, which specifically binds to OxLDL (oxidized low density
CC       lipoprotein), suggesting that it may be involved in pathophysiology
CC       such as atherogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC       {ECO:0000305}.
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DR   EMBL; AF277000; AAG31753.1; -; mRNA.
DR   RefSeq; NP_998976.1; NM_213811.1.
DR   AlphaFoldDB; Q9GKE2; -.
DR   STRING; 9823.ENSSSCP00000029924; -.
DR   PaxDb; Q9GKE2; -.
DR   Ensembl; ENSSSCT00025011216; ENSSSCP00025004502; ENSSSCG00025008424.
DR   Ensembl; ENSSSCT00045048794; ENSSSCP00045033934; ENSSSCG00045028497.
DR   Ensembl; ENSSSCT00055050019; ENSSSCP00055039962; ENSSSCG00055025229.
DR   GeneID; 396735; -.
DR   KEGG; ssc:396735; -.
DR   CTD; 58191; -.
DR   eggNOG; ENOG502T0B7; Eukaryota.
DR   HOGENOM; CLU_049889_0_0_1; -.
DR   InParanoid; Q9GKE2; -.
DR   OrthoDB; 1450357at2759; -.
DR   Reactome; R-SSC-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-SSC-418594; G alpha (i) signalling events.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q9GKE2; SS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IBA:GO_Central.
DR   GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:InterPro.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR   GO; GO:0034341; P:response to interferon-gamma; IEA:InterPro.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEA:InterPro.
DR   GO; GO:0010818; P:T cell chemotaxis; IBA:GO_Central.
DR   InterPro; IPR026296; CXCL16.
DR   PANTHER; PTHR14385; PTHR14385; 1.
PE   2: Evidence at transcript level;
KW   Chemotaxis; Cytokine; Disulfide bond; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..250
FT                   /note="C-X-C motif chemokine 16"
FT                   /id="PRO_0000378192"
FT   TOPO_DOM        25..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          105..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        33..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..77
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  27570 MW;  64ADCFA55C35421E CRC64;
     MPLWELWFFL LALFLAWLTP PGNGNEGSMA GSCPCNRRIS SHSPPTDHDM RHLRKYLNHY
     QHCTSYVRFQ LPRGSVCGGS SDQWVLKLMG CFDRGECGRA HARTVAHQQH LAPQNTRVPE
     LPERAPPDSS TPAQTNLPST LQPTQKPTLP EGMPSLAKKL IPTSETDTST VGHSLGAKSE
     ARENQEQLGK NVGATAGTSA LVPVLSLLVI IFLLTGVLLY VMCKKRQEQS RQYPPDPQLH
     YVPVASNINT