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CXL16_HUMAN
ID   CXL16_HUMAN             Reviewed;         254 AA.
AC   Q9H2A7; A0N0N4; A8K7U9; B2RCB0; Q8TC80; Q96K63; Q9BXD6; Q9H2F6;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 4.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=C-X-C motif chemokine 16;
DE   AltName: Full=Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein;
DE            Short=SR-PSOX;
DE   AltName: Full=Small-inducible cytokine B16;
DE   AltName: Full=Transmembrane chemokine CXCL16;
DE   Flags: Precursor;
GN   Name=CXCL16; Synonyms=SCYB16, SRPSOX; ORFNames=UNQ2759/PRO6714;
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], AND VARIANTS THR-123 AND VAL-181.
RX   PubMed=11017100; DOI=10.1038/79738;
RA   Matloubian M., David A., Engel S., Ryan J.E., Cyster J.G.;
RT   "A transmembrane CXC chemokine is a ligand for HIV-coreceptor Bonzo.";
RL   Nat. Immunol. 1:298-304(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-181.
RX   PubMed=11290797; DOI=10.4049/jimmunol.166.8.5145;
RA   Wilbanks A., Zondlo S.C., Murphy K., Mak S., Soler D., Langdon P.,
RA   Andrew D.P., Wu L., Briskin M.;
RT   "Expression cloning of the strl33/bonzo/tymstr ligand reveals elements of
RT   cc, cxc, and cx3c chemokines.";
RL   J. Immunol. 166:5145-5154(2001).
RN   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA   Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA   Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA   Nickerson D.A.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-123 AND VAL-181.
RC   TISSUE=Mammary gland, Synovium, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-123 AND VAL-181.
RC   TISSUE=Lung, Spleen, and Testis;
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: Acts as a scavenger receptor on macrophages, which
CC       specifically binds to OxLDL (oxidized low density lipoprotein),
CC       suggesting that it may be involved in pathophysiology such as
CC       atherogenesis (By similarity). Induces a strong chemotactic response.
CC       Induces calcium mobilization. Binds to CXCR6/Bonzo. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Secreted. Note=Also exists as a soluble
CC       form.
CC   -!- TISSUE SPECIFICITY: Expressed in T-cell areas. Expressed in spleen,
CC       lymph nodes, lung, kidney, small intestine and thymus. Weak expression
CC       in heart and liver and no expression in brain and bone marrow.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG34365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH17588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH44930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=ABK41925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB55078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAF84803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAG37507.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL16 entry;
CC       URL="https://en.wikipedia.org/wiki/CXCL16";
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DR   EMBL; AF301016; AAG34365.1; ALT_INIT; mRNA.
DR   EMBL; AF337812; AAK38275.1; -; mRNA.
DR   EMBL; AF275260; AAG31750.1; -; mRNA.
DR   EMBL; EF064742; ABK41925.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY358909; AAQ89268.1; -; mRNA.
DR   EMBL; AK027389; BAB55078.1; ALT_INIT; mRNA.
DR   EMBL; AK292114; BAF84803.1; ALT_INIT; mRNA.
DR   EMBL; AK315017; BAG37507.1; ALT_INIT; mRNA.
DR   EMBL; BC017588; AAH17588.1; ALT_INIT; mRNA.
DR   EMBL; BC044930; AAH44930.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11052.1; -.
DR   RefSeq; NP_001094282.1; NM_001100812.1.
DR   RefSeq; NP_071342.2; NM_022059.3.
DR   AlphaFoldDB; Q9H2A7; -.
DR   SMR; Q9H2A7; -.
DR   BioGRID; 121805; 86.
DR   STRING; 9606.ENSP00000293778; -.
DR   TCDB; 9.B.173.1.1; the chemokine, cxcl16 (cxcl16) family.
DR   GlyGen; Q9H2A7; 3 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; Q9H2A7; -.
DR   PhosphoSitePlus; Q9H2A7; -.
DR   BioMuta; CXCL16; -.
DR   DMDM; 209572770; -.
DR   EPD; Q9H2A7; -.
DR   jPOST; Q9H2A7; -.
DR   MassIVE; Q9H2A7; -.
DR   MaxQB; Q9H2A7; -.
DR   PaxDb; Q9H2A7; -.
DR   PeptideAtlas; Q9H2A7; -.
DR   PRIDE; Q9H2A7; -.
DR   ProteomicsDB; 80520; -.
DR   Antibodypedia; 11299; 483 antibodies from 34 providers.
DR   DNASU; 58191; -.
DR   Ensembl; ENST00000293778.12; ENSP00000293778.7; ENSG00000161921.17.
DR   Ensembl; ENST00000574412.6; ENSP00000459592.2; ENSG00000161921.17.
DR   GeneID; 58191; -.
DR   KEGG; hsa:58191; -.
DR   MANE-Select; ENST00000293778.12; ENSP00000293778.7; NM_001386809.1; NP_001373738.1.
DR   UCSC; uc002fyr.6; human.
DR   CTD; 58191; -.
DR   DisGeNET; 58191; -.
DR   GeneCards; CXCL16; -.
DR   HGNC; HGNC:16642; CXCL16.
DR   HPA; ENSG00000161921; Low tissue specificity.
DR   MIM; 605398; gene.
DR   neXtProt; NX_Q9H2A7; -.
DR   OpenTargets; ENSG00000161921; -.
DR   PharmGKB; PA27057; -.
DR   VEuPathDB; HostDB:ENSG00000161921; -.
DR   eggNOG; ENOG502T0B7; Eukaryota.
DR   GeneTree; ENSGT00390000002148; -.
DR   HOGENOM; CLU_049889_0_0_1; -.
DR   InParanoid; Q9H2A7; -.
DR   OMA; CPRYIRF; -.
DR   OrthoDB; 1450357at2759; -.
DR   PhylomeDB; Q9H2A7; -.
DR   TreeFam; TF337941; -.
DR   PathwayCommons; Q9H2A7; -.
DR   Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q9H2A7; -.
DR   BioGRID-ORCS; 58191; 8 hits in 1071 CRISPR screens.
DR   ChiTaRS; CXCL16; human.
DR   GenomeRNAi; 58191; -.
DR   Pharos; Q9H2A7; Tbio.
DR   PRO; PR:Q9H2A7; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9H2A7; protein.
DR   Bgee; ENSG00000161921; Expressed in left testis and 161 other tissues.
DR   ExpressionAtlas; Q9H2A7; baseline and differential.
DR   Genevisible; Q9H2A7; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008009; F:chemokine activity; IDA:BHF-UCL.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; ISS:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; IBA:GO_Central.
DR   GO; GO:0006935; P:chemotaxis; NAS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; NAS:UniProtKB.
DR   GO; GO:0034097; P:response to cytokine; IDA:BHF-UCL.
DR   GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
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   Cell membrane; Chemotaxis; Cytokine; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..254
FT                   /note="C-X-C motif chemokine 16"
FT                   /id="PRO_0000005118"
FT   TOPO_DOM        30..205
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          32..107
FT                   /note="Chemokine"
FT   REGION          146..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        38..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..82
FT                   /evidence="ECO:0000250"
FT   VARIANT         123
FT                   /note="I -> T"
FT                   /evidence="ECO:0000269|PubMed:11017100,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_015424"
FT   VARIANT         181
FT                   /note="A -> V (in dbSNP:rs2277680)"
FT                   /evidence="ECO:0000269|PubMed:11017100,
FT                   ECO:0000269|PubMed:11290797, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_015425"
FT   CONFLICT        67
FT                   /note="R -> W (in Ref. 6; BAG37507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="H -> L (in Ref. 6; BAB55078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="S -> P (in Ref. 6; BAG37507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="L -> P (in Ref. 2; AAK38275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  27579 MW;  EA627A87958B83B6 CRC64;
     MGRDLRPGSR VLLLLLLLLL VYLTQPGNGN EGSVTGSCYC GKRISSDSPP SVQFMNRLRK
     HLRAYHRCLY YTRFQLLSWS VCGGNKDPWV QELMSCLDLK ECGHAYSGIV AHQKHLLPTS
     PPISQASEGA SSDIHTPAQM LLSTLQSTQR PTLPVGSLSS DKELTRPNET TIHTAGHSLA
     AGPEAGENQK QPEKNAGPTA RTSATVPVLC LLAIIFILTA ALSYVLCKRR RGQSPQSSPD
     LPVHYIPVAP DSNT
 
 
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