CXL16_MOUSE
ID CXL16_MOUSE Reviewed; 246 AA.
AC Q8BSU2; Q3UD70; Q5F2D5; Q8VE25; Q9EPB3;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
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=Srpsox;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
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 FUNCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Pituitary, Skin, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=20675388; DOI=10.1074/jbc.m110.116418;
RA Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A.,
RA Saunders L., Verdin E., Charo I.F.;
RT "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor
RT essential for spermiogenesis and male fertility.";
RL J. Biol. Chem. 285:31418-31426(2010).
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. {ECO:0000269|PubMed:11060282}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Not detected in purified B- and
CC T-cells. {ECO:0000269|PubMed:11017100, ECO:0000269|PubMed:20675388}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; AF277001; AAG31754.1; -; mRNA.
DR EMBL; AF301017; AAG34366.1; -; mRNA.
DR EMBL; AK009599; BAB26384.1; -; mRNA.
DR EMBL; AK028875; BAC26166.1; -; mRNA.
DR EMBL; AK030515; BAC27000.1; -; mRNA.
DR EMBL; AK150224; BAE29391.1; -; mRNA.
DR EMBL; AK151330; BAE30309.1; -; mRNA.
DR EMBL; AK152102; BAE30949.1; -; mRNA.
DR EMBL; AK152547; BAE31302.1; -; mRNA.
DR EMBL; AK153192; BAE31792.1; -; mRNA.
DR EMBL; AL596096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12565.1; -; Genomic_DNA.
DR EMBL; CH466596; EDL12566.1; -; Genomic_DNA.
DR EMBL; BC019961; AAH19961.1; -; mRNA.
DR CCDS; CCDS24948.1; -.
DR RefSeq; NP_075647.3; NM_023158.6.
DR AlphaFoldDB; Q8BSU2; -.
DR STRING; 10090.ENSMUSP00000019064; -.
DR PhosphoSitePlus; Q8BSU2; -.
DR MaxQB; Q8BSU2; -.
DR PaxDb; Q8BSU2; -.
DR PRIDE; Q8BSU2; -.
DR ProteomicsDB; 279227; -.
DR Antibodypedia; 11299; 483 antibodies from 34 providers.
DR DNASU; 66102; -.
DR Ensembl; ENSMUST00000019064; ENSMUSP00000019064; ENSMUSG00000018920.
DR GeneID; 66102; -.
DR KEGG; mmu:66102; -.
DR UCSC; uc007juw.1; mouse.
DR CTD; 58191; -.
DR MGI; MGI:1932682; Cxcl16.
DR VEuPathDB; HostDB:ENSMUSG00000018920; -.
DR eggNOG; ENOG502T0B7; Eukaryota.
DR GeneTree; ENSGT00390000002148; -.
DR InParanoid; Q8BSU2; -.
DR OMA; CPRYIRF; -.
DR OrthoDB; 1450357at2759; -.
DR PhylomeDB; Q8BSU2; -.
DR TreeFam; TF337941; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 66102; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cxcl16; mouse.
DR PRO; PR:Q8BSU2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BSU2; protein.
DR Bgee; ENSMUSG00000018920; Expressed in right kidney and 142 other tissues.
DR ExpressionAtlas; Q8BSU2; baseline and differential.
DR Genevisible; Q8BSU2; MM.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:MGI.
DR GO; GO:0042379; F:chemokine receptor binding; IPI:UniProtKB.
DR GO; GO:0005041; F:low-density lipoprotein particle receptor activity; IDA:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0010818; P:T cell chemotaxis; IDA:UniProtKB.
DR InterPro; IPR026296; CXCL16.
DR PANTHER; PTHR14385; PTHR14385; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Cytokine; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11017100"
FT CHAIN 27..246
FT /note="C-X-C motif chemokine 16"
FT /id="PRO_0000005119"
FT TOPO_DOM 27..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 104..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 35..65
FT /evidence="ECO:0000250"
FT DISULFID 37..79
FT /evidence="ECO:0000250"
FT CONFLICT 129
FT /note="S -> P (in Ref. 6; AAH19961)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 246 AA; 26896 MW; 2B3047AD695219FF CRC64;
MRRGFGPLSL AFFLFLLALL TLPGDGNQGS VAGSCSCDRT ISSGTQIPQG TLDHIRKYLK
AFHRCPFFIR FQLQSKSVCG GSQDQWVREL VDCFERKECG TGHGKSFHHQ KHLPQASTQT
PEAAEGTPSD TSTPAHSQST QHSTLPSGAL SLNKEHTQPW EMTTLPSGYG LEARPEAEAN
EKQQDDRQQE APGAGASTPA WVPVLSLLAI VFFLTAAMAY VLCNRRATQQ NSAGLQLWYT
PVEPRP
