CCRL2_PIG
ID CCRL2_PIG Reviewed; 350 AA.
AC Q75ZH0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Chemokine C-C motif receptor-like 2;
GN Name=CCRL2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=15777643; DOI=10.1016/j.gene.2004.10.017;
RA Shinkai H., Morozumi T., Toki D., Eguchi T., Muneta Y., Awata T.,
RA Uenishi H.;
RT "Genomic structure of eight porcine chemokine receptors and intergene
RT sharing of an exon between CCR1 and XCR1.";
RL Gene 349:55-66(2005).
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; AB119273; BAD12136.1; -; mRNA.
DR EMBL; AB119274; BAD12137.1; -; mRNA.
DR EMBL; AP006185; BAD08650.1; -; Genomic_DNA.
DR EMBL; AP006435; BAD08657.1; -; Genomic_DNA.
DR RefSeq; NP_001001617.1; NM_001001617.1.
DR RefSeq; XP_005669514.1; XM_005669457.1.
DR RefSeq; XP_005669515.1; XM_005669458.2.
DR RefSeq; XP_013837019.1; XM_013981565.1.
DR RefSeq; XP_013837020.1; XM_013981566.1.
DR RefSeq; XP_013837021.1; XM_013981567.1.
DR RefSeq; XP_013837022.1; XM_013981568.1.
DR AlphaFoldDB; Q75ZH0; -.
DR SMR; Q75ZH0; -.
DR STRING; 9823.ENSSSCP00000024934; -.
DR PaxDb; Q75ZH0; -.
DR PRIDE; Q75ZH0; -.
DR Ensembl; ENSSSCT00000030552; ENSSSCP00000024934; ENSSSCG00000023557.
DR Ensembl; ENSSSCT00000053543; ENSSSCP00000044157; ENSSSCG00000023557.
DR Ensembl; ENSSSCT00000078903; ENSSSCP00000066840; ENSSSCG00000023557.
DR Ensembl; ENSSSCT00025071355; ENSSSCP00025030901; ENSSSCG00025052185.
DR Ensembl; ENSSSCT00025071410; ENSSSCP00025030927; ENSSSCG00025052185.
DR Ensembl; ENSSSCT00025071457; ENSSSCP00025030951; ENSSSCG00025052185.
DR Ensembl; ENSSSCT00035048162; ENSSSCP00035019253; ENSSSCG00035036343.
DR Ensembl; ENSSSCT00035048167; ENSSSCP00035019255; ENSSSCG00035036343.
DR Ensembl; ENSSSCT00035048173; ENSSSCP00035019258; ENSSSCG00035036343.
DR Ensembl; ENSSSCT00065044694; ENSSSCP00065019107; ENSSSCG00065032930.
DR Ensembl; ENSSSCT00065044698; ENSSSCP00065019109; ENSSSCG00065032930.
DR Ensembl; ENSSSCT00065044704; ENSSSCP00065019112; ENSSSCG00065032930.
DR Ensembl; ENSSSCT00070014431; ENSSSCP00070011906; ENSSSCG00070007487.
DR Ensembl; ENSSSCT00070014437; ENSSSCP00070011912; ENSSSCG00070007487.
DR GeneID; 414370; -.
DR KEGG; ssc:414370; -.
DR CTD; 9034; -.
DR VGNC; VGNC:86375; CCRL2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q75ZH0; -.
DR OMA; CKSNYNL; -.
DR OrthoDB; 1277718at2759; -.
DR TreeFam; TF330966; -.
DR Reactome; R-SSC-380108; Chemokine receptors bind chemokines.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Bgee; ENSSSCG00000023557; Expressed in blood and 36 other tissues.
DR Genevisible; Q75ZH0; SS.
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:0048020; F:CCR chemokine receptor binding; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..350
FT /note="Chemokine C-C motif receptor-like 2"
FT /id="PRO_0000236801"
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..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 329..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 350 AA; 40592 MW; 468622AAF673A363 CRC64;
MANYTSAPED DYDVFIEDDL SNDERELCSP YDPQALLAQL VPYLFITVFL VGLLDNILVV
LIMVKYKGLK QVENIYLLNL AVCNLCFLCT LPFWVHMAWH EGDPGEPLCK ILLVLYSVGL
FSEAFFNVLL TVQRYQKFFQ MRGFFSATRM VAGSIFPSAL VWVIAVLVML PELAFYKPQM
ENQKYKCFFG RPLFLPADET FWKHFLTLKM NILGFLLPLF VFVFCYVRMR RTLKFGERGY
DLFKLVFTIM VVFLLMWGPY NIALFLSAFN EHFSLHGCES SHNLDRSTLI TKIIATTHCC
VNPLLYVFFD EAFRKHLYHF CHLCNDTAPQ PTEEPAQGTS REEPCLSTKM
