CCRL2_MACMU
ID CCRL2_MACMU Reviewed; 344 AA.
AC Q9XSD7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=C-C chemokine receptor-like 2;
GN Name=CCRL2;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11461684; DOI=10.1089/088922201750290104;
RA Margulies B.J., Hauer D.A., Clements J.E.;
RT "Identification and comparison of eleven rhesus macaque chemokine
RT receptors.";
RL AIDS Res. Hum. Retroviruses 17:981-986(2001).
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}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF124381; AAD31420.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XSD7; -.
DR SMR; Q9XSD7; -.
DR STRING; 9544.ENSMMUP00000018726; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9XSD7; -.
DR Proteomes; UP000006718; Unplaced.
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:0005887; C:integral component of 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; 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:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..344
FT /note="C-C chemokine receptor-like 2"
FT /id="PRO_0000236799"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 323..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 344 AA; 39838 MW; 7EF4114B6F085173 CRC64;
MANYTLAPED EYDVLIEGEL ESDEAEQCDR YDTWALSAQL VPSLCSAVFV VGVLDNLLVV
LILVKYKGLK RVENIYLLNL AVSNLCFLLT LPFWAHAGGD PMCKILIGLY FVGLYSETFF
NCLLTLQRYL VFLHKGNFFS VRRRVPCGIV TSAVAWVTAI LATVPEFAVY KPQMEDPKYK
CAFSRTPFLP ADETFWKHFL TLKMNVSVLV FPLFIFTFLY VQMRKTLRFG EQRYSLFKLV
FAIMVVFLLM WAPYNIALFL STFKEHFSLS DCKSNYNLDK SVLITKLIAT THCCVNPLLY
VFLDGTFRKY LCRFFHRRSN TPRQPRRRFA QGTSREEPDR STEV
