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CXR32_DANRE
ID   CXR32_DANRE             Reviewed;         378 AA.
AC   E9QJ73; B0S589; Q5U387;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 2.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=C-X-C chemokine receptor type 3-2 {ECO:0000305};
GN   Name=cxcr3.2 {ECO:0000312|ZFIN:ZDB-GENE-041114-186};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000312|EMBL:AAH85659.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=20424185; DOI=10.1182/blood-2010-01-262873;
RA   Zakrzewska A., Cui C., Stockhammer O.W., Benard E.L., Spaink H.P.,
RA   Meijer A.H.;
RT   "Macrophage-specific gene functions in Spi1-directed innate immunity.";
RL   Blood 116:E1-E11(2010).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=25573892; DOI=10.1242/dmm.017756;
RA   Torraca V., Cui C., Boland R., Bebelman J.P., van der Sar A.M., Smit M.J.,
RA   Siderius M., Spaink H.P., Meijer A.H.;
RT   "The CXCR3-CXCL11 signaling axis mediates macrophage recruitment and
RT   dissemination of mycobacterial infection.";
RL   Dis. Model. Mech. 8:253-269(2015).
CC   -!- FUNCTION: Receptor for the C-X-C chemokines cxcl11.1 and cxcl11.6
CC       (PubMed:25573892). Promotes macrophage chemotaxis to sites of bacterial
CC       infection (PubMed:20424185, PubMed:25573892).
CC       {ECO:0000269|PubMed:20424185, ECO:0000269|PubMed:25573892}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25573892};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Detected in developing macrophages at 28 hours
CC       post-fertilization (PubMed:20424185). Continues to be expressed in
CC       macrophages at 2 and 6 days post-fertilization (dpf) (PubMed:25573892).
CC       Also detected in neutrophils at 2 and 6 dpf (PubMed:25573892).
CC       {ECO:0000269|PubMed:20424185, ECO:0000269|PubMed:25573892}.
CC   -!- DISRUPTION PHENOTYPE: Viable with no significant effect on survival
CC       (PubMed:25573892). Macrophage and neutrophil counts are normal
CC       (PubMed:25573892). Macrophage migration in response to cxcr3.2-
CC       independent stimuli is not affected, although the basal migration rate
CC       is reduced (PubMed:25573892). Macrophage migration to sites of
CC       bacterial infection by S.typhimurium or M.marinum is reduced
CC       (PubMed:20424185, PubMed:25573892). Dissemination of bacterial
CC       infection to distant sites and granuloma formation is also reduced
CC       (PubMed:25573892). {ECO:0000269|PubMed:20424185,
CC       ECO:0000269|PubMed:25573892}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; BX005342; CAQ13805.1; -; Genomic_DNA.
DR   EMBL; CR848719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC085659; AAH85659.1; -; mRNA.
DR   RefSeq; NP_001007315.1; NM_001007314.1.
DR   AlphaFoldDB; E9QJ73; -.
DR   SMR; E9QJ73; -.
DR   STRING; 7955.ENSDARP00000122984; -.
DR   PaxDb; E9QJ73; -.
DR   Ensembl; ENSDART00000145727; ENSDARP00000122984; ENSDARG00000041041.
DR   GeneID; 791973; -.
DR   KEGG; dre:791973; -.
DR   CTD; 791973; -.
DR   ZFIN; ZDB-GENE-041114-186; cxcr3.2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244848; -.
DR   HOGENOM; CLU_1264104_0_0_1; -.
DR   OMA; STCHAQF; -.
DR   OrthoDB; 794531at2759; -.
DR   PhylomeDB; E9QJ73; -.
DR   PRO; PR:E9QJ73; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000041041; Expressed in granulocyte and 16 other tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IGI:ZFIN.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0002522; P:leukocyte migration involved in immune response; IMP:ZFIN.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; IMP:ZFIN.
DR   GO; GO:0048246; P:macrophage chemotaxis; IGI:ZFIN.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IMP:ZFIN.
DR   InterPro; IPR000248; ATII_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00241; ANGIOTENSINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Immunity; Innate immunity; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..378
FT                   /note="C-X-C chemokine receptor type 3-2"
FT                   /id="PRO_0000437521"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        48..68
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        87..107
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        165..185
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        213..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..253
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        275..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..378
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        120..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        8
FT                   /note="A -> T (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        19..21
FT                   /note="NST -> SSA (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29
FT                   /note="Y -> N (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="T -> R (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="L -> M (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        93
FT                   /note="V -> I (in Ref. 1; CAQ13805)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="E -> Q (in Ref. 2; AAH85659)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42263 MW;  45B3A05C18E7923B CRC64;
     MDNSTTAAEV SAPTDYDYNS TSYDDDNPYA APCSLTETWN FLGRFAPVAY ILVFILALVG
     NILVLCVIRR YRQSRHSPCS FSLTDTFLLH LAVSDLLLAA TLPFFAVEWI SEWVFGKVMC
     KITGALFSLN VYCGVLFLAC ISFDRYLAIV HAINISWRRK TCHAQLACAF IWVICLGLSM
     VDMHFRDLVE IPGMNRMVCQ IVYSEQYSKQ WQIGMQLVSM VLGFILPLLV MLYCYLHIFK
     ALCHATRRQK RRSLRLIISL VIVFVISWAP YNALRMTDSL QMLGVIVKSC ALNNVLDVGI
     LVTESLGLAH CALNPLLYGL VGVKFRRELA QMCKAALGPQ GCLGLVGWAN GRGSSTRRPT
     GSFSSVETEN TSYFSVMA
 
 
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