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";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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