ID   CCRL2_MOUSE             Reviewed;         360 AA.
AC   O35457; O70171; Q3UKM6; Q4FK04; Q91YD7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=C-C chemokine receptor-like 2;
DE   AltName: Full=Chemokine receptor CCR11;
DE   AltName: Full=G-protein coupled beta chemokine receptor;
DE   AltName: Full=Lipopolysaccharide-inducible C-C chemokine receptor;
DE            Short=L-CCR;
GN   Name=Ccrl2; Synonyms=Ccr11, Lccr;
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], AND TISSUE SPECIFICITY.
RX   PubMed=9563519; DOI=10.1016/s0014-5793(98)00299-3;
RA   Shimada T., Matsumoto M., Tatsumi Y., Kanamaru A., Akira S.;
RT   "A novel lipopolysaccharide inducible C-C chemokine receptor related gene
RT   in murine macrophages.";
RL   FEBS Lett. 425:490-494(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=CD-1;
RX   PubMed=12555200; DOI=10.1002/glia.10156;
RA   Zuurman M.W., Heeroma J., Brouwer N., Boddeke H.W., Biber K.P.H.;
RT   "LPS-induced expression of a novel chemokine receptor (L-CCR) in mouse
RT   glial cells in vitro and in vivo.";
RL   Glia 41:327-336(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv, and C57BL/10;
RA   Luo Y., Berman M.A., Fischer F.R., Abromson-Leeman S.R., Kuziel W.A.,
RA   Gerard C., Dorf M.E.;
RT   "RANTES and eotaxin stimulate chemotaxis, chemokine/cytokine synthesis, and
RT   receptor modulation in murine astroctyes.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   FUNCTION.
RX   PubMed=12885941; DOI=10.1189/jlb.0802415;
RA   Biber K., Zuurman M.W., Homan H., Boddeke H.W.G.M.;
RT   "Expression of L-CCR in HEK 293 cells reveals functional responses to CCL2,
RT   CCL5, CCL7, and CCL8.";
RL   J. Leukoc. Biol. 74:243-251(2003).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=14999816; DOI=10.1002/glia.10352;
RA   Brouwer N., Zuurman M.W., Wei T., Ransohoff R.M., Boddeke H.W., Biber K.;
RT   "Induction of glial L-CCR mRNA expression in spinal cord and brain in
RT   experimental autoimmune encephalomyelitis.";
RL   Glia 46:84-94(2004).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=14966207; DOI=10.1177/002215540405200311;
RA   Oostendorp J., Hylkema M.N., Luinge M., Geerlings M., Meurs H., Timens W.,
RA   Zaagsma J., Postma D.S., Boddeke H.W., Biber K.;
RT   "Localization and enhanced mRNA expression of the orphan chemokine receptor
RT   L-CCR in the lung in a murine model of ovalbumin-induced airway
RT   inflammation.";
RL   J. Histochem. Cytochem. 52:401-410(2004).
RN   [10]
RP   LIGAND-BINDING, DISRUPTION PHENOTYPE, FUNCTION, AND LACK OF RESPOND TO
RP   CCL2; CCL5; CCL7 AND CCL8.
RX   PubMed=18794339; DOI=10.1084/jem.20080300;
RA   Zabel B.A., Nakae S., Zuniga L., Kim J.Y., Ohyama T., Alt C., Pan J.,
RA   Suto H., Soler D., Allen S.J., Handel T.M., Song C.H., Galli S.J.,
RA   Butcher E.C.;
RT   "Mast cell-expressed orphan receptor CCRL2 binds chemerin and is required
RT   for optimal induction of IgE-mediated passive cutaneous anaphylaxis.";
RL   J. Exp. Med. 205:2207-2220(2008).
RN   [11]
RP   TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=20606167; DOI=10.1182/blood-2009-12-259903;
RA   Otero K., Vecchi A., Hirsch E., Kearley J., Vermi W., Del Prete A.,
RA   Gonzalvo-Feo S., Garlanda C., Azzolino O., Salogni L., Lloyd C.M.,
RA   Facchetti F., Mantovani A., Sozzani S.;
RT   "Nonredundant role of CCRL2 in lung dendritic cell trafficking.";
RL   Blood 116:2942-2949(2010).
CC   -!- FUNCTION: Receptor for CCL19 and chemerin/RARRES2. Does not appear to
CC       be a signaling receptor, but may have a role in modulating chemokine-
CC       triggered immune responses by capturing and internalizing CCL19 or by
CC       presenting RARRES2 ligand to CMKLR1, a functional signaling receptor.
CC       Plays a critical role for the development of Th2 responses (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:12885941,
CC       ECO:0000269|PubMed:18794339, ECO:0000269|PubMed:20606167}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in macrophages, astrocytes, in glial
CC       cells. Constitutively expressed by mast cells. Detected in bronchial
CC       epithelium in OVA-induced airway inflammation. Up-regulated during
CC       dendritic cell (DC) maturation. {ECO:0000269|PubMed:12555200,
CC       ECO:0000269|PubMed:14966207, ECO:0000269|PubMed:14999816,
CC       ECO:0000269|PubMed:20606167, ECO:0000269|PubMed:9563519}.
CC   -!- INDUCTION: By bacterial lipopolysaccharide in astrocytes.
CC       {ECO:0000269|PubMed:12555200}.
CC   -!- DOMAIN: Lacks the conserved DRYLAIV motif in the second intracellular
CC       loop that is required for signaling of functional chemokine receptors.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Deficient-mice have normal
CC       numbers of mast cells in all tissues analyzed. Wild-type and deficient
CC       mice develop marked local inflammation when sensitized with a high dose
CC       of DNP-specific IgE, however deficient mice have significantly reduced
CC       IgE-dependent passive cutaneous anaphylaxis (PCA) reactions when lower
CC       sensitizing dose is used. Deficient-mice show normal recruitment of
CC       circulating DC into the lung, but a defective trafficking of antigen-
CC       loaded lung DC to mediastinal lymph nodes. This defect was associated
CC       to a reduction in lymph node cellularity and reduced priming of T-
CC       helper cell 2 response. {ECO:0000269|PubMed:18794339,
CC       ECO:0000269|PubMed:20606167}.
CC   -!- MISCELLANEOUS: It was initially reported that CCRL2 responds
CC       functionally to CCL2, CCL5, CCL7, and CCL8 via intracellular calcium
CC       mobilization and transwell chemotaxis although no evidence for a direct
CC       ligand-receptor interaction was provided in this report
CC       (PubMed:14999816). These results are now controversial and other
CC       studies failed to confirm CCRL2 recognition and transwell chemotaxis of
CC       these chemokines or a series of other CC- and CXC-chemokines using
CC       CCRL2-transfected cells (PubMed:18794339).
CC       {ECO:0000305|PubMed:14999816, ECO:0000305|PubMed:18794339}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AB009384; BAA25879.1; -; mRNA.
DR   EMBL; AJ318863; CAC79612.1; -; mRNA.
DR   EMBL; AF316576; AAG30950.1; -; mRNA.
DR   EMBL; AF030185; AAB86479.1; -; mRNA.
DR   EMBL; AK007808; BAB25273.1; -; mRNA.
DR   EMBL; AK145946; BAE26775.1; -; mRNA.
DR   EMBL; AK151856; BAE30745.1; -; mRNA.
DR   EMBL; CT010248; CAJ18456.1; -; mRNA.
DR   EMBL; BC038631; AAH38631.1; -; mRNA.
DR   CCDS; CCDS23582.1; -.
DR   RefSeq; NP_001289305.1; NM_001302376.1.
DR   RefSeq; NP_001289306.1; NM_001302377.1.
DR   RefSeq; NP_059494.2; NM_017466.5.
DR   AlphaFoldDB; O35457; -.
DR   SMR; O35457; -.
DR   STRING; 10090.ENSMUSP00000107519; -.
DR   GlyCosmos; O35457; 2 sites, No reported glycans.
DR   GlyGen; O35457; 2 sites.
DR   PhosphoSitePlus; O35457; -.
DR   PaxDb; 10090-ENSMUSP00000107519; -.
DR   ProteomicsDB; 281346; -.
DR   Antibodypedia; 6921; 473 antibodies from 34 providers.
DR   DNASU; 54199; -.
DR   Ensembl; ENSMUST00000111888.3; ENSMUSP00000107519.2; ENSMUSG00000043953.13.
DR   Ensembl; ENSMUST00000199839.5; ENSMUSP00000143116.2; ENSMUSG00000043953.13.
DR   GeneID; 54199; -.
DR   KEGG; mmu:54199; -.
DR   UCSC; uc009rvk.2; mouse.
DR   AGR; MGI:1920904; -.
DR   CTD; 9034; -.
DR   MGI; MGI:1920904; Ccrl2.
DR   VEuPathDB; HostDB:ENSMUSG00000043953; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01020000230359; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; O35457; -.
DR   OMA; FYKPQME; -.
DR   OrthoDB; 5265544at2759; -.
DR   PhylomeDB; O35457; -.
DR   TreeFam; TF330966; -.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   BioGRID-ORCS; 54199; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Ccrl2; mouse.
DR   PRO; PR:O35457; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O35457; Protein.
DR   Bgee; ENSMUSG00000043953; Expressed in granulocyte and 96 other cell types or tissues.
DR   ExpressionAtlas; O35457; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; ISS:MGI.
DR   GO; GO:0048020; F:CCR chemokine receptor binding; ISO:MGI.
DR   GO; GO:0042379; F:chemokine receptor binding; IPI:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   CDD; cd15171; 7tmA_CCRL2; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF655; C-C CHEMOKINE RECEPTOR-LIKE 2; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; O35457; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..360
FT                   /note="C-C chemokine receptor-like 2"
FT                   /id="PRO_0000236800"
FT   TOPO_DOM        1..42
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        95..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..141
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..202
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        224..243
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..307
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        37
FT                   /note="P -> S (in Ref. 4; BAE26775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="Q -> R (in Ref. 2; CAC79612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="I -> V (in Ref. 3; AAB86479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="F -> L (in Ref. 2; CAC79612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="V -> A (in Ref. 2; CAC79612)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334
FT                   /note="Y -> S (in Ref. 3; AAB86479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="E -> K (in Ref. 3; AAB86479)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="I -> K (in Ref. 5; CAJ18456)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40745 MW;  E0DBF990A8595E3B CRC64;
     MDNYTVAPDD EYDVLILDDY LDNSGPDQVP APEFLSPQQV LQFCCAVFAV GLLDNVLAVF
     ILVKYKGLKN LGNIYFLNLA LSNLCFLLPL PFWAHTAAHG ESPGNGTCKV LVGLHSSGLY
     SEVFSNILLL VQGYRVFSQG RLASIFTTVS CGIVACILAW AMATALSLPE SVFYEPRMER
     QKHKCAFGKP HFLPIEAPLW KYVLTSKMII LVLAFPLLVF IICCRQLRRR QSFRERQYDL
     HKPALVITGV FLLMWAPYNT VLFLSAFQEH LSLQDEKSSY HLDASVQVTQ LVATTHCCVN
     PLLYLLLDRK AFMRYLRSLF PRCNDIPYQS SGGYQQAPPR EGHGRPIELY SNLHQRQDII
//