CCR4_CANLF
ID CCR4_CANLF Reviewed; 360 AA.
AC Q8MJW8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=C-C chemokine receptor type 4;
DE Short=C-C CKR-4;
DE Short=CC-CKR-4;
DE Short=CCR-4;
DE Short=CCR4;
DE AltName: CD_antigen=CD194;
GN Name=CCR4;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12459162; DOI=10.1016/s0165-2427(02)00232-5;
RA Maeda S., Okayama T., Omori K., Masuda K., Sakaguchi M., Ohno K.,
RA Tsujimoto H.;
RT "Expression of CC chemokine receptor 4 (CCR4) mRNA in canine atopic skin
RT lesion.";
RL Vet. Immunol. Immunopathol. 90:145-154(2002).
CC -!- FUNCTION: High affinity receptor for the C-C type chemokines CCL17/TARC
CC and CCL22/MDC. The activity of this receptor is mediated by G(i)
CC proteins which activate a phosphatidylinositol-calcium second messenger
CC system. Could play a role in lipopolysaccharide (LPS)-induced endotoxic
CC shock. In the CNS, could mediate hippocampal-neuron survival (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in thymus, spleen, heart, small intestine
CC and lymph node. {ECO:0000269|PubMed:12459162}.
CC -!- PTM: In natural killer cells, CCL22 binding induces phosphorylation on
CC yet undefined Ser/Thr residues, most probably by beta-adrenergic
CC receptor kinases 1 and 2. {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; AB080188; BAC10546.1; -; mRNA.
DR RefSeq; NP_001003020.1; NM_001003020.1.
DR RefSeq; XP_005634207.1; XM_005634150.1.
DR AlphaFoldDB; Q8MJW8; -.
DR SMR; Q8MJW8; -.
DR STRING; 9612.ENSCAFP00000006935; -.
DR BindingDB; Q8MJW8; -.
DR ChEMBL; CHEMBL4295899; -.
DR PaxDb; Q8MJW8; -.
DR Ensembl; ENSCAFT00030048328; ENSCAFP00030042287; ENSCAFG00030026136.
DR Ensembl; ENSCAFT00845041609; ENSCAFP00845032629; ENSCAFG00845023571.
DR GeneID; 403541; -.
DR KEGG; cfa:403541; -.
DR CTD; 1233; -.
DR VEuPathDB; HostDB:ENSCAFG00845023571; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; Q8MJW8; -.
DR OMA; FHTQSTG; -.
DR OrthoDB; 900867at2759; -.
DR TreeFam; TF330966; -.
DR Proteomes; UP000002254; Chromosome 23.
DR Bgee; ENSCAFG00000004658; Expressed in blood and 15 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:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:1904936; P:interneuron migration; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0002507; P:tolerance induction; IEA:Ensembl.
DR InterPro; IPR002239; Chemokine_CCR4.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF608; PTHR10489:SF608; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01109; CHEMOKINER4.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="C-C chemokine receptor type 4"
FT /id="PRO_0000069244"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 360 AA; 41355 MW; 69115F5209EC0908 CRC64;
MNPTDIADTT LDESIYNNYY LYENIPKPCT KEGIKAFGEL FLPPLYSLVF LFGLLGNSVV
VVVLFKYKRL KSMTDVYLLN LAISDLLFVL SLPFWGYYAA DQWVFGLGLC KIISWMYLVG
FYSGIFFIML MSIDRYLAIV HAVFSLRART LTYGVITSLA TWSVAVLASL PGLLFSTCYT
ERNHTYCKTK YSRNSTRWKV LSSLEINILG LVIPLGTMLF CYSMIIRTLQ HCKNEKKSKA
VRMVFAVVAL FLGFWAPYNV VLFLETLVEL EVLQDCTFER HLDYAIQATE TLAFVHCCLN
PVIYFFLGEK FRKYLVQLFK TCRGPFMLCQ YCRLLQMYSP DTPSSSYTQS TGDHDLHDAL